Entry stringlengths 6 10 | Entry Name stringlengths 5 11 | Sequence stringlengths 2 35.2k | EC number stringlengths 7 118 ⌀ | Cofactor stringlengths 38 1.77k ⌀ | Gene Ontology (biological process) stringlengths 18 11.3k ⌀ | Gene Ontology (cellular component) stringlengths 17 1.75k ⌀ | Gene Ontology (molecular function) stringlengths 24 2.09k ⌀ | Pfam stringlengths 8 232 ⌀ | Gene3D stringlengths 10 250 ⌀ | Protein families stringlengths 9 237 ⌀ | Post-translational modification stringlengths 16 8.52k ⌀ | Subcellular location [CC] stringlengths 29 6.18k ⌀ | Catalytic activity stringlengths 64 35.7k ⌀ | Kinetics stringlengths 69 11.7k ⌀ | Pathway stringlengths 27 908 ⌀ | pH dependence stringlengths 64 955 ⌀ | Temperature dependence stringlengths 70 1.16k ⌀ | Function [CC] stringlengths 17 15.3k ⌀ | Organism stringlengths 8 196 |
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P0AE67 | CHEY_ECOLI | MADKELKFLVVDDFSTMRRIVRNLLKELGFNNVEEAEDGVDALNKLQAGGYGFVISDWNMPNMDGLELLKTIRADGAMSALPVLMVTAEAKKENIIAAAQAGASGYVVKPFTAATLEEKLNKIFEKLGM | null | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:8176739}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:8176739}; | aerotaxis [GO:0009454]; bacterial-type flagellum-dependent swimming motility [GO:0071977]; chemotaxis [GO:0006935]; internal peptidyl-lysine acetylation [GO:0018393]; phosphorelay signal transduction system [GO:0000160]; regulation of bacterial-type flagellum-dependent cell motility [GO:1902021]; regulation of chemotax... | bacterial-type flagellum [GO:0009288]; bacterial-type flagellum basal body, C ring [GO:0009433]; bacterial-type flagellum rotor complex [GO:0120107]; cytoplasm [GO:0005737]; cytosol [GO:0005829] | acetyltransferase activity [GO:0016407]; histidine phosphotransfer kinase activity [GO:0009927]; magnesium ion binding [GO:0000287]; phosphorelay response regulator activity [GO:0000156]; phosphorelay sensor kinase activity [GO:0000155] | PF00072; | 3.40.50.2300; | null | PTM: Phosphorylated by CheA or acetylated by acetyl-CoA synthetase, depending on which acetate metabolism pathway is available. The major acetylation site seems to be Lys-92. Dephosphorylated (inactivated) by CheZ. {ECO:0000269|PubMed:11359578, ECO:0000269|PubMed:1390767, ECO:0000269|PubMed:2689446, ECO:0000269|PubMed:... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | null | null | null | null | null | FUNCTION: Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. In its active (phosphorylated or acetylated) form, CheY exhibits enhanced binding to a switch component, FliM, at the flagellar motor which induces a change from counterclockwise to clockwise flagellar rotation. O... | Escherichia coli (strain K12) |
P0AE70 | MAZF_ECOLI | MVSRYVPDMGDLIWVDFDPTKGSEQAGHRPAVVLSPFMYNNKTGMCLCVPCTTQSKGYPFEVVLSGQERDGVALADQVKSIAWRARGATKKGTVAPEELQLIKAKINVLIG | 3.1.27.- | null | defense response to virus [GO:0051607]; mRNA catabolic process [GO:0006402]; negative regulation of cell growth [GO:0030308]; positive regulation of programmed cell death [GO:0043068]; quorum sensing [GO:0009372]; regulation of DNA-templated transcription [GO:0006355]; regulation of growth [GO:0040008]; regulation of t... | protein-containing complex [GO:0032991]; toxin-antitoxin complex [GO:0110001] | DNA binding [GO:0003677]; molecular function activator activity [GO:0140677]; protein homodimerization activity [GO:0042803]; protein-containing complex binding [GO:0044877]; RNA binding [GO:0003723]; RNA endonuclease activity [GO:0004521] | PF02452; | 2.30.30.110; | PemK/MazF family | PTM: (Microbial infection) ADP-ribosylated by enterobacteria phage T4. {ECO:0000269|PubMed:26395283}. | null | null | null | null | null | null | FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system. A sequence-specific endoribonuclease it inhibits protein synthesis by cleaving mRNA and inducing bacterial stasis. It is stable, single-strand specific with mRNA cleavage independent of the ribosome, although translation enhances cleavage for some mRNA... | Escherichia coli (strain K12) |
P0AE72 | MAZE_ECOLI | MIHSSVKRWGNSPAVRIPATLMQALNLNIDDEVKIDLVDGKLIIEPVRKEPVFTLAELVNDITPENLHENIDWGEPKDKEVW | null | null | regulation of DNA-templated transcription [GO:0006355]; regulation of growth [GO:0040008]; single-species biofilm formation [GO:0044010] | protein-containing complex [GO:0032991]; toxin-antitoxin complex [GO:0110001] | DNA binding [GO:0003677]; double-stranded DNA binding [GO:0003690]; protein homodimerization activity [GO:0042803]; protein-containing complex binding [GO:0044877]; toxin sequestering activity [GO:0097351] | PF04014; | 2.10.260.10; | PemI family | PTM: Degraded by the ClpPA and Lon proteases. {ECO:0000269|PubMed:12972253, ECO:0000269|PubMed:24375411, ECO:0000269|PubMed:8650219}. | null | null | null | null | null | null | FUNCTION: Antitoxin component of a type II toxin-antitoxin (TA) system. Labile antitoxin that binds to the MazF endoribonuclease toxin and neutralizes its endoribonuclease activity. Is considered to be an 'addiction' molecule as the cell dies in its absence. Toxicity results when the levels of MazE decrease in the cell... | Escherichia coli (strain K12) |
P0AE82 | CPXA_ECOLI | MIGSLTARIFAIFWLTLALVLMLVLMLPKLDSRQMTELLDSEQRQGLMIEQHVEAELANDPPNDLMWWRRLFRAIDKWAPPGQRLLLVTTEGRVIGAERSEMQIIRNFIGQADNADHPQKKKYGRVELVGPFSVRDGEDNYQLYLIRPASSSQSDFINLLFDRPLLLLIVTMLVSTPLLLWLAWSLAKPARKLKNAADEVAQGNLRQHPELEAGPQEFLAAGASFNQMVTALERMMTSQQRLLSDISHELRTPLTRLQLGTALLRRRSGESKELERIETEAQRLDSMINDLLVMSRNQQKNALVSETIKANQLWSEVLDN... | 2.7.13.3 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:9401031}; Note=Phosphotransfer to CpxR is stimulated by Mg(2+) and/or Mn(2+). {ECO:0000269|PubMed:9401031}; | cell adhesion involved in biofilm formation [GO:0043708]; cellular response to cell envelope stress [GO:0036460]; response to radiation [GO:0009314]; signal transduction [GO:0007165] | plasma membrane [GO:0005886] | ATP binding [GO:0005524]; identical protein binding [GO:0042802]; phosphoprotein phosphatase activity [GO:0004721]; phosphorelay sensor kinase activity [GO:0000155] | PF16527;PF00672;PF02518;PF00512; | 1.10.287.130;3.30.565.10;3.30.450.210; | null | PTM: Autophosphorylated (PubMed:24492262, PubMed:9401031). Maximal phosphorylation of the dimeric isolated cytoplasmic domain (residues 188-457) is about 70%, suggesting the protein may be hemiphosphorylated in vivo; probably occurs via a trans-autophosphorylation mechanism, i.e. one subunit phosphorylates the other (P... | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:25207645, ECO:0000269|PubMed:3058985}; Multi-pass membrane protein {ECO:0000305|PubMed:15919996, ECO:0000305|PubMed:3058985}. | CATALYTIC ACTIVITY: Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.; EC=2.7.13.3; Evidence={ECO:0000269|PubMed:9401031}; | null | null | null | null | FUNCTION: Histidine kinase member of the two-component regulatory system CpxA/CpxR which responds to envelope stress response by activating expression of downstream genes including cpxP, degP, dsbA and ppiA (PubMed:7883164, PubMed:9401031, PubMed:9473036). Activates CpxR by phosphorylation; has autokinase, phosphotrans... | Escherichia coli (strain K12) |
P0AE85 | CPXP_ECOLI | MRIVTAAVMASTLAVSSLSHAAEVGSGDNWHPGEELTQRSTQSHMFDGISLTEHQRQQMRDLMQQARHEQPPVNVSELETMHRLVTAENFDENAVRAQAEKMANEQIARQVEMAKVRNQMYRLLTPEQQAVLNEKHQQRMEQLRDVTQWQKSSSLKLLSSSNSRSQ | null | null | null | outer membrane-bounded periplasmic space [GO:0030288] | identical protein binding [GO:0042802]; unfolded protein binding [GO:0051082] | PF07813; | 1.20.120.1490; | CpxP/Spy family | PTM: Degraded by DegP; some CpxP mutant proteins are more susceptible to the protease than others (PubMed:16166523). Degradation probably occurs when CpxP is associated with some misfolded proteins; overexpression of PapE leads to DegP-mediated degradation of CpxP and PapE, which requires the N-terminus of PapE. Overex... | SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:25207645, ECO:0000269|PubMed:9473036}. | null | null | null | null | null | FUNCTION: Acts as an auxiliary protein in the Cpx two-component envelope stress response system, helping modulate the Cpx response systems response to some inducers (PubMed:16303867, PubMed:25207645). Binds the periplasmic domain of sensor histidine kinase CpxA, inhibiting induction of the Cpx envelope stress response ... | Escherichia coli (strain K12) |
P0AE88 | CPXR_ECOLI | MNKILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLLDDSIDLLLLDVMMPKKNGIDTLKALRQTHQTPVIMLTARGSELDRVLGLELGADDYLPKPFNDRELVARIRAILRRSHWSEQQQNNDNGSPTLEVDALVLNPGRQEASFDGQTLELTGTEFTLLYLLAQHLGQVVSREHLSQEVLGKRLTPFDRAIDMHISNLRRKLPDRKDGHPWFKTLRGRGYLMVSAS | null | null | cell adhesion [GO:0007155]; negative regulation of DNA-templated transcription [GO:0045892]; positive regulation of DNA-templated transcription [GO:0045893]; regulation of cell-substrate adhesion [GO:0010810]; regulation of DNA-templated transcription [GO:0006355] | cytosol [GO:0005829]; protein-DNA complex [GO:0032993] | DNA-binding transcription factor activity [GO:0003700]; phosphorelay response regulator activity [GO:0000156]; transcription cis-regulatory region binding [GO:0000976] | PF00072;PF00486; | 3.40.50.2300;6.10.250.690;1.10.10.10; | null | PTM: Phosphorylated by CpxA. {ECO:0000269|PubMed:17259177, ECO:0000269|PubMed:9401031, ECO:0000305|PubMed:7883164}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | null | null | null | null | null | FUNCTION: Response regulator member of the two-component regulatory system CpxA/CpxR which responds to envelope stress response by activating expression of downstream genes including cpxP, degP, dsbA and ppiA (PubMed:7883164, PubMed:9401031). Required for efficient binding of stationary phase cells to hydrophobic surfa... | Escherichia coli (strain K12) |
P0AEA8 | CYSG_ECOLI | MDHLPIFCQLRDRDCLIVGGGDVAERKARLLLDAGARLTVNALAFIPQFTAWADAGMLTLVEGPFDESLLDTCWLAIAATDDDALNQRVSEAAEARRIFCNVVDAPKAASFIMPSIIDRSPLMVAVSSGGTSPVLARLLREKLESLLPLHLGQVAKYAGQLRGRVKQQFATMGERRRFWEKLFVNDRLAQSLANNDQKAITETTEQLINEPLDHRGEVVLVGAGPGDAGLLTLKGLQQIQQADVVVYDRLVSDDIMNLVRRDADRVFVGKRAGYHCVPQEEINQILLREAQKGKRVVRLKGGDPFIFGRGGEELETLCNA... | 1.3.1.76; 2.1.1.107; 4.99.1.4 | null | cobalamin biosynthetic process [GO:0009236]; methylation [GO:0032259]; response to osmotic stress [GO:0006970]; siroheme biosynthetic process [GO:0019354] | null | NAD binding [GO:0051287]; precorrin-2 dehydrogenase activity [GO:0043115]; protein homodimerization activity [GO:0042803]; sirohydrochlorin ferrochelatase activity [GO:0051266]; uroporphyrin-III C-methyltransferase activity [GO:0004851] | PF10414;PF13241;PF14824;PF00590; | 3.40.50.720;1.10.8.210; | Precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase family; Precorrin methyltransferase family | null | null | CATALYTIC ACTIVITY: Reaction=2 S-adenosyl-L-methionine + uroporphyrinogen III = H(+) + precorrin-2 + 2 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:32459, ChEBI:CHEBI:15378, ChEBI:CHEBI:57308, ChEBI:CHEBI:57856, ChEBI:CHEBI:58827, ChEBI:CHEBI:59789; EC=2.1.1.107; Evidence={ECO:0000255|HAMAP-Rule:MF_01646, ECO:0000269|PubM... | null | PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis; precorrin-2 from uroporphyrinogen III: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01646, ECO:0000305|PubMed:2407234}.; PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis; sirohydrochlorin from precorrin-2: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01646, ... | null | null | FUNCTION: Multifunctional enzyme that catalyzes the SAM-dependent methylations of uroporphyrinogen III at position C-2 and C-7 to form precorrin-2 via precorrin-1. Then it catalyzes the NAD-dependent ring dehydrogenation of precorrin-2 to yield sirohydrochlorin. Finally, it catalyzes the ferrochelation of sirohydrochlo... | Escherichia coli (strain K12) |
P0AEB2 | DACA_ECOLI | MNTIFSARIMKRLALTTALCTAFISAAHADDLNIKTMIPGVPQIDAESYILIDYNSGKVLAEQNADVRRDPASLTKMMTSYVIGQAMKAGKFKETDLVTIGNDAWATGNPVFKGSSLMFLKPGMQVPVSQLIRGINLQSGNDACVAMADFAAGSQDAFVGLMNSYVNALGLKNTHFQTVHGLDADGQYSSARDMALIGQALIRDVPNEYSIYKEKEFTFNGIRQLNRNGLLWDNSLNVDGIKTGHTDKAGYNLVASATEGQMRLISAVMGGRTFKGREAESKKLLTWGFRFFETVNPLKVGKEFASEPVWFGDSDRASLG... | 3.4.16.4; 3.5.2.6 | null | cell wall organization [GO:0071555]; peptidoglycan biosynthetic process [GO:0009252]; peptidoglycan metabolic process [GO:0000270]; proteolysis [GO:0006508]; regulation of cell shape [GO:0008360] | outer membrane-bounded periplasmic space [GO:0030288]; plasma membrane [GO:0005886] | beta-lactamase activity [GO:0008800]; carboxypeptidase activity [GO:0004180]; penicillin binding [GO:0008658]; protein homodimerization activity [GO:0042803]; serine-type D-Ala-D-Ala carboxypeptidase activity [GO:0009002] | PF07943;PF00768; | 2.60.410.10;3.40.710.10; | Peptidase S11 family | null | SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. Note=N-terminal lies in the periplasmic space. | CATALYTIC ACTIVITY: Reaction=Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.; EC=3.4.16.4; CATALYTIC ACTIVITY: Reaction=a beta-lactam + H2O = a substituted beta-amino acid; Xref=Rhea:RHEA:20401, ChEBI:CHEBI:15377, ChEBI:CHEBI... | null | PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. | null | null | FUNCTION: Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors. | Escherichia coli (strain K12) |
P0AEC3 | ARCB_ECOLI | MKQIRLLAQYYVDLMMKLGLVRFSMLLALALVVLAIVVQMAVTMVLHGQVESIDVIRSIFFGLLITPWAVYFLSVVVEQLEESRQRLSRLVQKLEEMRERDLSLNVQLKDNIAQLNQEIAVREKAEAELQETFGQLKIEIKEREETQIQLEQQSSFLRSFLDASPDLVFYRNEDKEFSGCNRAMELLTGKSEKQLVHLKPADVYSPEAAAKVIETDEKVFRHNVSLTYEQWLDYPDGRKACFEIRKVPYYDRVGKRHGLMGFGRDITERKRYQDALERASRDKTTFISTISHELRTPLNGIVGLSRILLDTELTAEQEKY... | 2.7.13.3 | null | protein autophosphorylation [GO:0046777]; regulation of DNA-templated transcription [GO:0006355]; response to oxygen levels [GO:0070482]; signal transduction [GO:0007165] | cytosol [GO:0005829]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; phosphoprotein phosphatase activity [GO:0004721]; phosphorelay sensor kinase activity [GO:0000155] | PF02518;PF00512;PF18415;PF01627;PF00989;PF00072; | 1.10.287.130;3.40.50.2300;1.10.287.970;3.30.565.10;1.20.120.160;3.30.450.20; | null | PTM: Activation requires a sequential transfer of a phosphate group from a His in the primary transmitter domain, to an Asp in the receiver domain and to a His in the secondary transmitter domain. | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000269|PubMed:15919996}. | CATALYTIC ACTIVITY: Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.; EC=2.7.13.3; | null | null | null | null | FUNCTION: Member of the two-component regulatory system ArcB/ArcA. Sensor-regulator protein for anaerobic repression of the arc modulon. Activates ArcA via a four-step phosphorelay. ArcB can also dephosphorylate ArcA by a reverse phosphorelay involving His-717 and Asp-576. | Escherichia coli (strain K12) |
P0AEC5 | BARA_ECOLI | MTNYSLRARMMILILAPTVLIGLLLSIFFVVHRYNDLQRQLEDAGASIIEPLAVSTEYGMSLQNRESIGQLISVLHRRHSDIVRAISVYDENNRLFVTSNFHLDPSSMQLGSNVPFPRQLTVTRDGDIMILRTPIISESYSPDESPSSDAKNSQNMLGYIALELDLKSVRLQQYKEIFISSVMMLFCIGIALIFGWRLMRDVTGPIRNMVNTVDRIRRGQLDSRVEGFMLGELDMLKNGINSMAMSLAAYHEEMQHNIDQATSDLRETLEQMEIQNVELDLAKKRAQEAARIKSEFLANMSHELRTPLNGVIGFTRLTLK... | 2.7.13.3 | null | cellular hyperosmotic response [GO:0071474]; response to acetate [GO:0010034]; response to formic acid [GO:1901425]; response to hydrogen peroxide [GO:0042542] | plasma membrane [GO:0005886] | ATP binding [GO:0005524]; histidine phosphotransfer kinase activity [GO:0009927]; phosphoprotein phosphatase activity [GO:0004721]; phosphorelay sensor kinase activity [GO:0000155]; protein histidine kinase activity [GO:0004673]; protein homodimerization activity [GO:0042803] | PF00672;PF02518;PF00512;PF01627;PF00072;PF09984; | 1.10.287.130;3.40.50.2300;6.10.340.10;3.30.565.10;1.20.120.160; | null | PTM: Autophosphorylated (PubMed:11022030, PubMed:1574005). Activation requires a sequential transfer of a phosphate group from a His in the primary transmitter domain, to an Asp in the receiver domain and to a His in the secondary transmitter domain (Probable). {ECO:0000269|PubMed:11022030, ECO:0000269|PubMed:1574005, ... | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.; EC=2.7.13.3; Evidence={ECO:0000305|PubMed:11022030}; | null | null | null | null | FUNCTION: Member of the two-component regulatory system UvrY/BarA involved in the regulation of carbon metabolism via the CsrA/CsrB regulatory system (PubMed:12193630, PubMed:12533459). Phosphorylates UvrY, probably via a four-step phosphorelay (PubMed:11022030). {ECO:0000269|PubMed:11022030, ECO:0000269|PubMed:1219363... | Escherichia coli (strain K12) |
P0AEC8 | DCUS_ECOLI | MRHSLPYRMLRKRPMKLSTTVILMVSAVLFSVLLVVHLIYFSQISDMTRDGLANKALAVARTLADSPEIRQGLQKKPQESGIQAIAEAVRKRNDLLFIVVTDMQSLRYSHPEAQRIGQPFKGDDILKALNGEENVAINRGFLAQALRVFTPIYDENHKQIGVVAIGLELSRVTQQINDSRWSIIWSVLFGMLVGLIGTCILVKVLKKILFGLEPYEISTLFEQRQAMLQSIKEGVVAVDDRGEVTLINDAAQELLNYRKSQDDEKLSTLSHSWSQVVDVSEVLRDGTPRRDEEITIKDRLLLINTVPVRSNGVIIGAIST... | 2.7.13.3 | null | phosphorelay signal transduction system [GO:0000160]; regulation of DNA-templated transcription [GO:0006355]; signal transduction [GO:0007165] | cytosol [GO:0005829]; outer membrane-bounded periplasmic space [GO:0030288]; plasma membrane [GO:0005886]; protein histidine kinase complex [GO:0009365] | ATP binding [GO:0005524]; identical protein binding [GO:0042802]; phosphorelay sensor kinase activity [GO:0000155]; protein histidine kinase activity [GO:0004673] | PF02518;PF00989;PF17203;PF14689; | 1.10.287.130;3.30.565.10;3.30.450.20; | null | PTM: Autophosphorylated (PubMed:12167640). The phosphoryl group is rapidly transferred to DcuR (PubMed:12167640). {ECO:0000269|PubMed:12167640}. | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:12167640, ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.; EC=2.7.13.3; Evidence={ECO:0000305|PubMed:12167640}; | null | null | null | null | FUNCTION: Member of the two-component regulatory system DcuR/DcuS (PubMed:12167640, PubMed:9765574, PubMed:9973351). Involved in the C4-dicarboxylate-stimulated regulation of the genes encoding the anaerobic fumarate respiratory system (frdABCD; nuoAN; dcuB; sdhCDAB; etc.) (PubMed:9765574, PubMed:9973351). Weakly regul... | Escherichia coli (strain K12) |
P0AED7 | DAPE_ECOLI | MSCPVIELTQQLIRRPSLSPDDAGCQALLIERLQAIGFTVERMDFADTQNFWAWRGQGETLAFAGHTDVVPPGDADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPNHTGRLAFLITSDEEASAHNGTVKVVEALMARNERLDYCLVGEPSSIEVVGDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPFLNELVAIEWDQGNEFFPATSMQIANIQAGTGSNNVIPGELFVQFNFRFSTELTDEMIKAQVLALLEKHQLRYTVDWWLSGQPFLTARGKLVDAVVNAVEHYNEIKPQLLT... | 3.5.1.18 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:3276674}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000269|PubMed:3276674}; Note=Binds 2 Zn(2+) or Co(2+) ions per subunit. {ECO:0000269|PubMed:3276674}; | diaminopimelate biosynthetic process [GO:0019877]; lysine biosynthetic process via diaminopimelate [GO:0009089] | cell division site [GO:0032153]; cytosol [GO:0005829] | cobalt ion binding [GO:0050897]; identical protein binding [GO:0042802]; succinyl-diaminopimelate desuccinylase activity [GO:0009014]; zinc ion binding [GO:0008270] | PF07687;PF01546; | 3.40.630.10; | Peptidase M20A family, DapE subfamily | null | null | CATALYTIC ACTIVITY: Reaction=H2O + N-succinyl-(2S,6S)-2,6-diaminoheptanedioate = (2S,6S)-2,6-diaminoheptanedioate + succinate; Xref=Rhea:RHEA:22608, ChEBI:CHEBI:15377, ChEBI:CHEBI:30031, ChEBI:CHEBI:57609, ChEBI:CHEBI:58087; EC=3.5.1.18; Evidence={ECO:0000269|PubMed:3276674}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.41 mM for L,L-SDAP (in the presence of Zn(2+) at pH 7.0) {ECO:0000269|PubMed:3276674}; | PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 3/3. | null | null | FUNCTION: Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls. {ECO:0000269|PubMed:3276674}. | Escherichia coli (strain K12) |
P0AEE3 | DEGS_ECOLI | MFVKLLRSVAIGLIVGAILLVAMPSLRSLNPLSTPQFDSTDETPASYNLAVRRAAPAVVNVYNRGLNTNSHNQLEIRTLGSGVIMDQRGYIITNKHVINDADQIIVALQDGRVFEALLVGSDSLTDLAVLKINATGGLPTIPINARRVPHIGDVVLAIGNPYNLGQTITQGIISATGRIGLNPTGRQNFLQTDASINHGNSGGALVNSLGELMGINTLSFDKSNDGETPEGIGFAIPFQLATKIMDKLIRDGRVIRGYIGIGGREIAPLHAQGGGIDQLQGIVVNEVSPDGPAANAGIQVNDLIISVDNKPAISALETMD... | 3.4.21.107 | null | cellular response to misfolded protein [GO:0071218]; protein quality control for misfolded or incompletely synthesized proteins [GO:0006515]; proteolysis [GO:0006508] | outer membrane-bounded periplasmic space [GO:0030288]; plasma membrane [GO:0005886] | identical protein binding [GO:0042802]; peptidase activity [GO:0008233]; serine-type endopeptidase activity [GO:0004252]; serine-type peptidase activity [GO:0008236] | PF13180;PF13365; | 2.30.42.10;2.40.10.10; | Peptidase S1C family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305|PubMed:11442831}; Single-pass membrane protein {ECO:0000305|PubMed:11442831}. Note=It is unclear how this protein is anchored to the inner membrane, programs predict a signal sequence, but replacing the N-terminal 26 residues with a known signal sequence gives a pr... | CATALYTIC ACTIVITY: Reaction=Acts on substrates that are at least partially unfolded. The cleavage site P1 residue is normally between a pair of hydrophobic residues, such as Val-|-Val.; EC=3.4.21.107; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=33 uM for RseA-YQF {ECO:0000269|PubMed:17981123, ECO:0000269|PubMed:19836340}; Vmax=0.6 umol/sec/mg enzyme {ECO:0000269|PubMed:17981123, ECO:0000269|PubMed:19836340}; | null | null | null | FUNCTION: A site-1 protease (S1P) that cleaves the peptide bond between 'Val-148' and 'Ser-149' in RseA. Part of a regulated intramembrane proteolysis (RIP) cascade. When heat shock or other environmental stresses disrupt protein folding in the periplasm, DegS senses the accumulation of unassembled outer membrane porin... | Escherichia coli (strain K12) |
P0AEE5 | MGLB_ECOLI | MNKKVLTLSAVMASMLFGAAAHAADTRIGVTIYKYDDNFMSVVRKAIEQDAKAAPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPVVFFNKEPSRKALDSYDKAYYVGTDSKESGIIQGDLIAKHWAANQGWDLNKDGQIQFVLLKGEPGHPDAEARTTYVIKELNDKGIKTEQLQLDTAMWDTAQAKDKMDAWLSGPNANKIEVVIANNDAMAMGAVEALKAHNKSSIPVFGVDALPEALALVKSGALAGTVLNDANNQAKATFDLAKNLADGKGAADGTNWKIDNKVVRVPYVG... | null | null | chemotaxis [GO:0006935]; galactose transmembrane transport [GO:0015757]; methylgalactoside transport [GO:0015765] | ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing [GO:0055052]; membrane [GO:0016020]; outer membrane-bounded periplasmic space [GO:0030288] | calcium ion binding [GO:0005509]; carbohydrate binding [GO:0030246] | PF13407; | 3.40.50.2300; | Bacterial solute-binding protein 2 family | null | SUBCELLULAR LOCATION: Periplasm. | null | null | null | null | null | FUNCTION: Part of the ABC transporter complex MglABC involved in galactose/methyl galactoside import (Probable). In addition, binds D-galactose and D-glucose and plays a role in the chemotaxis towards these two sugars by interacting with the Trg chemoreceptor (PubMed:3057628, PubMed:4927373). Chemotaxis requires MglB, ... | Escherichia coli (strain K12) |
P0AEE8 | DMA_ECOLI | MKKNRAFLKWAGGKYPLLDDIKRHLPKGECLVEPFVGAGSVFLNTDFSRYILADINSDLISLYNIVKMRTDEYVQAARELFVPETNCAEVYYQFREEFNKSQDPFRRAVLFLYLNRYGYNGLCRYNLRGEFNVPFGRYKKPYFPEAELYHFAEKAQNAFFYCESYADSMARADDASVVYCDPPYAPLSATANFTAYHTNSFTLEQQAHLAEIAEGLVERHIPVLISNHDTMLTREWYQRAKLHVVKVRRSISSNGGTRKKVDELLALYKPGVVSPAKK | 2.1.1.72 | null | bacterial-type DNA replication initiation [GO:1902328]; DNA-templated DNA replication [GO:0006261]; macromolecule modification [GO:0043412]; methylation [GO:0032259]; mismatch repair [GO:0006298]; response to UV [GO:0009411] | null | S-adenosyl-L-methionine binding [GO:1904047]; sequence-specific DNA binding [GO:0043565]; site-specific DNA-methyltransferase (adenine-specific) activity [GO:0009007] | PF02086; | 1.10.1020.10;3.40.50.150; | N(4)/N(6)-methyltransferase family | null | null | CATALYTIC ACTIVITY: Reaction=a 2'-deoxyadenosine in DNA + S-adenosyl-L-methionine = an N(6)-methyl-2'-deoxyadenosine in DNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:15197, Rhea:RHEA-COMP:12418, Rhea:RHEA-COMP:12419, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:90615, ChEBI:CHEBI:90616;... | null | null | null | null | FUNCTION: An alpha subtype methylase that recognizes the double-stranded sequence 5'-GATC-3' and methylates A-2 on both strands (Probable) (PubMed:12654995). Although it shares sequence specificity with a number of type II restriction endonucleases and methylases, it is thought to act in methyl-directed mismatch repair... | Escherichia coli (strain K12) |
P0AEG4 | DSBA_ECOLI | MKKIWLALAGLVLAFSASAAQYEDGKQYTTLEKPVAGAPQVLEFFSFFCPHCYQFEEVLHISDNVKKKLPEGVKMTKYHVNFMGGDLGKDLTQAWAVAMALGVEDKVTVPLFEGVQKTQTIRSASDIRDVFINAGIKGEEYDAAWNSFVVKSLVAQQEKAAADVQLRGVPAMFVNGKYQLNPQGMDTSNMDVFVQQYADTVKYLSEKK | null | null | cellular response to antibiotic [GO:0071236] | outer membrane-bounded periplasmic space [GO:0030288] | protein disulfide isomerase activity [GO:0003756]; protein-disulfide reductase activity [GO:0015035] | PF01323; | 3.40.30.10; | Thioredoxin family, DsbA subfamily | null | SUBCELLULAR LOCATION: Periplasm. | null | null | null | null | null | FUNCTION: Required for disulfide bond formation in some periplasmic proteins such as PhoA or OmpA. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbA is reoxidized by DsbB. Required for pilus biogenesis. PhoP-regulated transcription is redox-sensitive, being activated when the... | Escherichia coli (strain K12) |
P0AEG6 | DSBC_ECOLI | MKKGFMLFTLLAAFSGFAQADDAAIQQTLAKMGIKSSDIQPAPVAGMKTVLTNSGVLYITDDGKHIIQGPMYDVSGTAPVNVTNKMLLKQLNALEKEMIVYKAPQEKHVITVFTDITCGYCHKLHEQMADYNALGITVRYLAFPRQGLDSDAEKEMKAIWCAKDKNKAFDDVMAGKSVAPASCDVDIADHYALGVQLGVSGTPAVVLSNGTLVPGYQPPKEMKEFLDEHQKMTSGK | null | null | chaperone-mediated protein folding [GO:0061077]; response to copper ion [GO:0046688] | outer membrane-bounded periplasmic space [GO:0030288]; periplasmic space [GO:0042597] | protein disulfide isomerase activity [GO:0003756]; protein homodimerization activity [GO:0042803]; protein-disulfide reductase activity [GO:0015035] | PF10411;PF13098; | 3.10.450.70;3.40.30.10; | Thioredoxin family, DsbC subfamily | null | SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:8168498}. | null | null | null | null | null | FUNCTION: Acts as a disulfide isomerase, interacting with incorrectly folded proteins to correct non-native disulfide bonds. DsbG and DsbC are part of a periplasmic reducing system that controls the level of cysteine sulfenylation, and provides reducing equivalents to rescue oxidatively damaged secreted proteins. Acts ... | Escherichia coli (strain K12) |
P0AEH1 | RSEP_ECOLI | MLSFLWDLASFIVALGVLITVHEFGHFWVARRCGVRVERFSIGFGKALWRRTDKLGTEYVIALIPLGGYVKMLDERAEPVVPELRHHAFNNKSVGQRAAIIAAGPVANFIFAIFAYWLVFIIGVPGVRPVVGEIAANSIAAEAQIAPGTELKAVDGIETPDWDAVRLQLVDKIGDESTTITVAPFGSDQRRDVKLDLRHWAFEPDKEDPVSSLGIRPRGPQIEPVLENVQPNSAASKAGLQAGDRIVKVDGQPLTQWVTFVMLVRDNPGKSLALEIERQGSPLSLTLIPESKPGNGKAIGFVGIEPKVIPLPDEYKVVRQ... | 3.4.24.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305}; | cellular response to cell envelope stress [GO:0036460]; positive regulation of DNA-templated transcription [GO:0045893]; proteolysis [GO:0006508] | plasma membrane [GO:0005886] | anti-sigma factor antagonist activity [GO:0043856]; metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222] | PF17820;PF02163; | 2.30.42.10; | Peptidase M50B family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:11689431, ECO:0000269|PubMed:11750129, ECO:0000269|PubMed:11867724, ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000269|PubMed:11689431, ECO:0000269|PubMed:11750129, ECO:0000269|PubMed:11867724, ECO:0000269|PubMed:15919996}. | null | null | null | null | null | FUNCTION: A site-2 regulated intramembrane protease (S2P) that cleaves the peptide bond between 'Ala-108' and 'Cys-109' in the transmembrane region of RseA. Part of a regulated intramembrane proteolysis (RIP) cascade. Acts on DegS-cleaved RseA to release the cytoplasmic domain of RseA, residue 'Val-148' of RseA may be ... | Escherichia coli (strain K12) |
P0AEI1 | MIAB_ECOLI | MTKKLHIKTWGCQMNEYDSSKMADLLDATHGYQLTDVAEEADVLLLNTCSIREKAQEKVFHQLGRWKLLKEKNPDLIIGVGGCVASQEGEHIRQRAHYVDIIFGPQTLHRLPEMINSVRGDRSPVVDISFPEIEKFDRLPEPRAEGPTAFVSIMEGCNKYCTYCVVPYTRGEEVSRPSDDILFEIAQLAAQGVREVNLLGQNVNAWRGENYDGTTGSFADLLRLVAAIDGIDRIRFTTSHPIEFTDDIIEVYRDTPELVSFLHLPVQSGSDRILNLMGRTHTALEYKAIIRKLRAARPDIQISSDFIVGFPGETTEDFEK... | 2.8.4.3 | COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000305|PubMed:11882645}; Note=Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. {ECO:0000305|PubMed:11882645}; | tRNA methylation [GO:0030488]; tRNA methylthiolation [GO:0035600] | cytosol [GO:0005829] | 4 iron, 4 sulfur cluster binding [GO:0051539]; metal ion binding [GO:0046872]; N6-isopentenyladenosine methylthiotransferase activity [GO:0035597] | PF04055;PF01938;PF00919; | 3.40.50.12160;3.80.30.20; | Methylthiotransferase family, MiaB subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01864}. | CATALYTIC ACTIVITY: Reaction=[sulfur carrier]-SH + AH2 + N(6)-dimethylallyladenosine(37) in tRNA + 2 S-adenosyl-L-methionine = 2-methylsulfanyl-N(6)-dimethylallyladenosine(37) in tRNA + 5'-deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:37067, Rhea:RHEA-COMP:1... | null | null | null | null | FUNCTION: Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine. {ECO:0000255|HAMAP-Rule:MF_01864, ECO:0000269|PubMed:10572129}. | Escherichia coli (strain K12) |
P0AEJ2 | ENTC_ECOLI | MDTSLAEEVQQTMATLAPNRFFFMSPYRSFTTSGCFARFDEPAVNGDSPDSPFQQKLAALFADAKAQGIKNPVMVGAIPFDPRQPSSLYIPESWQSFSRQEKQASARRFTRSQSLNVVERQAIPEQTTFEQMVARAAALTATPQVDKVVLSRLIDITTDAAIDSGVLLERLIAQNPVSYNFHVPLADGGVLLGASPELLLRKDGERFSSIPLAGSARRQPDEVLDREAGNRLLASEKDRHEHELVTQAMKEVLRERSSELHVPSSPQLITTPTLWHLATPFEGKANSQENALTLACLLHPTPALSGFPHQAATQVIAELE... | 5.4.4.2 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:20079748}; Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000269|PubMed:20079748}; | enterobactin biosynthetic process [GO:0009239]; salicylic acid biosynthetic process [GO:0009697] | null | isochorismate synthase activity [GO:0008909]; magnesium ion binding [GO:0000287] | PF00425; | 3.60.120.10; | Isochorismate synthase family | null | null | CATALYTIC ACTIVITY: Reaction=chorismate = isochorismate; Xref=Rhea:RHEA:18985, ChEBI:CHEBI:29748, ChEBI:CHEBI:29780; EC=5.4.4.2; Evidence={ECO:0000269|PubMed:17243787, ECO:0000269|PubMed:20079748, ECO:0000269|PubMed:2139795}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5 uM for isochorismate (at pH 7.8 and 37 degrees Celsius) {ECO:0000269|PubMed:2139795}; KM=7 uM for chorismate {ECO:0000269|PubMed:20079748}; KM=14 uM for chorismate (at pH 7.8 and 37 degrees Celsius) {ECO:0000269|PubMed:2139795}; KM=41 uM for chorismate {ECO:00002... | PATHWAY: Siderophore biosynthesis; enterobactin biosynthesis. {ECO:0000305}. | null | null | FUNCTION: Involved in the biosynthesis of the siderophore enterobactin (macrocyclic trimeric lactone of N-(2,3-dihydroxybenzoyl)-serine). Catalyzes the reversible conversion of chorismate to isochorismate. {ECO:0000269|PubMed:17243787, ECO:0000269|PubMed:20079748, ECO:0000269|PubMed:2139795, ECO:0000269|PubMed:2536681,... | Escherichia coli (strain K12) |
P0AEJ4 | ENVZ_ECOLI | MRRLRFSPRSSFARTLLLIVTLLFASLVTTYLVVLNFAILPSLQQFNKVLAYEVRMLMTDKLQLEDGTQLVVPPAFRREIYRELGISLYSNEAAEEAGLRWAQHYEFLSHQMAQQLGGPTEVRVEVNKSSPVVWLKTWLSPNIWVRVPLTEIHQGDFSPLFRYTLAIMLLAIGGAWLFIRIQNRPLVDLEHAALQVGKGIIPPPLREYGASEVRSVTRAFNHMAAGVKQLADDRTLLMAGVSHDLRTPLTRIRLATEMMSEQDGYLAESINKDIEECNAIIEQFIDYLRTGQEMPMEMADLNAVLGEVIAAESGYEREIE... | 2.7.13.3 | null | phosphorelay signal transduction system [GO:0000160]; phosphorylation [GO:0016310]; protein autophosphorylation [GO:0046777]; response to osmotic stress [GO:0006970]; signal transduction [GO:0007165] | cytosol [GO:0005829]; outer membrane-bounded periplasmic space [GO:0030288]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; identical protein binding [GO:0042802]; phosphoprotein phosphatase activity [GO:0004721]; phosphorelay sensor kinase activity [GO:0000155]; protein homodimerization activity [GO:0042803] | PF00672;PF02518;PF00512; | 1.10.287.130;3.30.565.10; | null | PTM: Autophosphorylated (PubMed:2277041, PubMed:2656684, PubMed:2668281, PubMed:2668953, PubMed:3056929, PubMed:8132603). Incubation of isolated EnvZ C-terminal fragment (residues 180-450) with increasing levels of NaCl or sucrose increases its autophosphorylation (PubMed:17635923). {ECO:0000269|PubMed:17635923, ECO:00... | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:1323560, ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:2824492}; Multi-pass membrane protein {ECO:0000305|PubMed:1323560, ECO:0000305|PubMed:15919996, ECO:0000305|PubMed:2824492}. | CATALYTIC ACTIVITY: Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.; EC=2.7.13.3; Evidence={ECO:0000269|PubMed:2668953, ECO:0000305|PubMed:2656684, ECO:0000305|PubMed:2668281, ECO:0000305|PubMed:2674113}; | null | null | null | null | FUNCTION: Member of the two-component regulatory system EnvZ/OmpR involved in osmoregulation (particularly of genes ompF and ompC) as well as other genes (PubMed:2997120, PubMed:3536870). EnvZ functions as a membrane-associated protein kinase that phosphorylates OmpR in response to environmental signals; at low osmolar... | Escherichia coli (strain K12) |
P0AEJ6 | EUTB_ECOLI | MKLKTTLFGNVYQFKDVKEVLAKANELRSGDVLAGVAAASSQERVAAKQVLSEMTVADIRNNPVIAYEDDCVTRLIQDDVNETAYNQIKNWSISELREYVLSDETSVDDIAFTRKGLTSEVVAAVAKICSNADLIYGAKKMPVIKKANTTIGIPGTFSARLQPNDTRDDVQSIAAQIYEGLSFGVGDAVIGVNPVTDDVENLSRVLDTIYGVIDKFNIPTQGCVLAHVTTQIEAIRRGAPGGLIFQSICGSEKGLKEFGVELAMLDEARAVGAEFNRIAGENCLYFETGQGSALSAGANFGADQVTMEARNYGLARHYDP... | 4.3.1.7 | COFACTOR: Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408; Evidence={ECO:0000255|HAMAP-Rule:MF_00861, ECO:0000269|PubMed:19762342, ECO:0000269|PubMed:20519496, ECO:0000269|PubMed:21142024, ECO:0000269|PubMed:29797764}; Note=Binds 1 AdoCbl between the large and small subunits, with 6 cofactors per holoenzyme. {ECO:0... | amino acid metabolic process [GO:0006520]; ethanolamine catabolic process [GO:0046336] | cytosol [GO:0005829]; ethanolamine ammonia-lyase complex [GO:0009350]; ethanolamine degradation polyhedral organelle [GO:0031471] | cobalamin binding [GO:0031419]; ethanolamine ammonia-lyase activity [GO:0008851] | PF06751; | 3.20.20.70;2.30.170.30;1.10.220.70; | EutB family | null | SUBCELLULAR LOCATION: Bacterial microcompartment {ECO:0000255|HAMAP-Rule:MF_00861}. | CATALYTIC ACTIVITY: Reaction=ethanolamine = acetaldehyde + NH4(+); Xref=Rhea:RHEA:15313, ChEBI:CHEBI:15343, ChEBI:CHEBI:28938, ChEBI:CHEBI:57603; EC=4.3.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00861, ECO:0000269|PubMed:15466038, ECO:0000269|PubMed:19762342}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=8.2 uM for ethanolamine {ECO:0000269|PubMed:19762342}; KM=0.055 uM for adenosylcob(III)alamin {ECO:0000269|PubMed:19762342}; | PATHWAY: Amine and polyamine degradation; ethanolamine degradation. {ECO:0000255|HAMAP-Rule:MF_00861}. | null | null | FUNCTION: Catalyzes the deamination of various vicinal amino-alcohols to oxo compounds (PubMed:19762342). Allows this organism to utilize ethanolamine as the sole source of nitrogen and carbon in the presence of external vitamin B12. It is spontaneously inactivated by its substrate and reactivated by EutA (PubMed:15466... | Escherichia coli (strain K12) |
P0AEK2 | FABG_ECOLI | MNFEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKGLMLNVTDPASIESVLEKIRAEFGEVDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLIGFSKSLAREVASRGITVNVVAPGFIETDMTRALSDDQRAGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGETLHVNGGMYMV | 1.1.1.100 | null | biotin biosynthetic process [GO:0009102]; fatty acid biosynthetic process [GO:0006633]; fatty acid elongation [GO:0030497]; lipid biosynthetic process [GO:0008610] | cytosol [GO:0005829] | 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity [GO:0004316]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; NAD binding [GO:0051287]; NADP binding [GO:0050661]; oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor [GO:0016616] | PF13561; | 3.40.50.720; | Short-chain dehydrogenases/reductases (SDR) family | null | null | CATALYTIC ACTIVITY: Reaction=a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + H(+) + NADPH; Xref=Rhea:RHEA:17397, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78776, ChEBI:CHEBI:78827; EC=1.1.1.100; Evidence={ECO:0000269|PubMed:10629181, ECO:0000... | null | PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000269|PubMed:14996818, ECO:0000269|PubMed:7592873}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is between 6.0 and 7.0. {ECO:0000269|PubMed:4381013}; | null | FUNCTION: Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis. {ECO:0000269|PubMed:10629181, ECO:0000269|PubMed:14996818, ECO:0000269|PubMed:7592873, ECO:0000269|PubMed:8631920, ECO:0000269|... | Escherichia coli (strain K12) |
P0AEK4 | FABI_ECOLI | MGFLSGKRILVTGVASKLSIAYGIAQAMHREGAELAFTYQNDKLKGRVEEFAAQLGSDIVLQCDVAEDASIDTMFAELGKVWPKFDGFVHSIGFAPGDQLDGDYVNAVTREGFKIAHDISSYSFVAMAKACRSMLNPGSALLTLSYLGAERAIPNYNVMGLAKASLEANVRYMANAMGPEGVRVNAISAGPIRTLAASGIKDFRKMLAHCEAVTPIRRTVTIEDVGNSAAFLCSDLSAGISGEVVHVDGGFSIAAMNELELK | 1.3.1.9 | null | biotin biosynthetic process [GO:0009102]; fatty acid elongation [GO:0030497]; lipid biosynthetic process [GO:0008610]; protein homotetramerization [GO:0051289]; response to antibiotic [GO:0046677] | catalytic complex [GO:1902494]; cytosol [GO:0005829]; membrane [GO:0016020]; protein-containing complex [GO:0032991] | enoyl-[acyl-carrier-protein] reductase (NADH) activity [GO:0004318]; enoyl-[acyl-carrier-protein] reductase activity [GO:0016631]; identical protein binding [GO:0042802]; NADH binding [GO:0070404] | PF13561; | 3.40.50.720; | Short-chain dehydrogenases/reductases (SDR) family, FabI subfamily | null | null | CATALYTIC ACTIVITY: Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] + H(+) + NADH; Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9; Evidence={ECO:0000269|PubMed:10629181, ECO:00002... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.3 uM for trans-2-dodecenoyl-ACP (DD-ACP)(at 25 degrees Celsius and pH 8) {ECO:0000269|PubMed:17012233}; KM=22 uM for crotonyl-ACP (at 30 degrees Celsius and pH 7.5) {ECO:0000269|PubMed:8119879}; KM=24 uM for trans-2-dodecenoyl-CoA (DD-CoA)(at 25 degrees Celsius a... | PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000269|PubMed:7592873}.; PATHWAY: Cofactor biosynthesis; biotin biosynthesis. {ECO:0000305|PubMed:20693992}. | null | null | FUNCTION: Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism and in the biotin biosynthesis. {ECO:0000269|PubMed:10629181, ECO:0000269|PubMed:20693992,... | Escherichia coli (strain K12) |
P0AEK7 | FDNI_ECOLI | MSKSKMIVRTKFIDRACHWTVVICFFLVALSGISFFFPTLQWLTQTFGTPQMGRILHPFFGIAIFVALMFMFVRFVHHNIPDKKDIPWLLNIVEVLKGNEHKVADVGKYNAGQKMMFWSIMSMIFVLLVTGVIIWRPYFAQYFPMQVVRYSLLIHAAAGIILIHAILIHMYMAFWVKGSIKGMIEGKVSRRWAKKHHPRWYREIEKAEAKKESEEGI | null | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000269|PubMed:11884747}; Note=Binds 2 heme groups per subunit. Heme 1 is located at the cytoplasmic interface, heme 2 is located at the periplasmic interface. Electrons are transferred from the periplasmic to the cytoplasmic heme. {ECO:0000269|PubMed:11884747}... | anaerobic electron transport chain [GO:0019645]; anaerobic respiration [GO:0009061]; formate oxidation [GO:0015944]; heme oxidation [GO:0006788] | formate dehydrogenase complex [GO:0009326]; membrane [GO:0016020]; plasma membrane [GO:0005886] | electron transfer activity [GO:0009055]; formate dehydrogenase (NAD+) activity [GO:0008863]; formate dehydrogenase (quinone) activity [GO:0036397]; heme binding [GO:0020037]; metal ion binding [GO:0046872] | PF01292; | 1.20.950.20; | Formate dehydrogenase gamma subunit family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:11884747}; Multi-pass membrane protein {ECO:0000269|PubMed:11884747}. | null | null | null | null | null | FUNCTION: Formate dehydrogenase allows E.coli to use formate as major electron donor during anaerobic respiration, when nitrate is used as electron acceptor. Subunit gamma is the cytochrome b556 component of the formate dehydrogenase-N, and also contains a menaquinone reduction site that receives electrons from the bet... | Escherichia coli (strain K12) |
P0AEL0 | FDOI_ECOLI | MKRRDTIVRYTAPERINHWITAFCFILAAVSGLGFLFPSFNWLMQIMGTPQLARILHPFVGVVMFASFIIMFFRYWHHNLINRDDIFWAKNIRKIVVNEEVGDTGRYNFGQKCVFWAAIIFLVLLLVSGVIIWRPYFAPAFSIPVIRFALMLHSFAAVALIVVIMVHIYAALWVKGTITAMVEGWVTSAWAKKHHPRWYREVRKTTEKKAE | null | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250}; Note=Binds 2 heme groups per subunit. Heme 1 is located at the cytoplasmic interface, heme 2 is located at the periplasmic interface. Electrons are transferred from the periplasmic to the cytoplasmic heme. {ECO:0000250}; | anaerobic electron transport chain [GO:0019645]; anaerobic respiration [GO:0009061]; cellular respiration [GO:0045333]; DNA damage response [GO:0006974]; formate oxidation [GO:0015944]; heme oxidation [GO:0006788] | formate dehydrogenase complex [GO:0009326]; membrane [GO:0016020]; plasma membrane [GO:0005886] | electron transfer activity [GO:0009055]; formate dehydrogenase (NAD+) activity [GO:0008863]; formate dehydrogenase (quinone) activity [GO:0036397]; metal ion binding [GO:0046872] | PF01292; | 1.20.950.20; | Formate dehydrogenase gamma subunit family | null | SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. | null | null | null | null | null | FUNCTION: Allows to use formate as major electron donor during aerobic respiration. Subunit gamma is probably the cytochrome b556(FDO) component of the formate dehydrogenase. | Escherichia coli (strain K12) |
P0AEM0 | FKBX_ECOLI | MSESVQSNSAVLVHFTLKLDDGTTAESTRNNGKPALFRLGDASLSEGLEQHLLGLKVGDKTTFSLEPDAAFGVPSPDLIQYFSRREFMDAGEPEIGAIMLFTAMDGSEMPGVIREINGDSITVDFNHPLAGQTVHFDIEVLEIDPALEA | 5.2.1.8 | null | chaperone-mediated protein folding [GO:0061077] | cytosol [GO:0005829] | peptidyl-prolyl cis-trans isomerase activity [GO:0003755] | PF00254; | 2.40.10.330;3.10.50.40; | FKBP-type PPIase family | null | null | CATALYTIC ACTIVITY: Reaction=[protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833, ChEBI:CHEBI:83834; EC=5.2.1.8; Evidence={ECO:0000269|PubMed:9188461}; | null | null | null | null | FUNCTION: PPIases accelerate the folding of proteins (Probable). Substrate specificity investigated with 'Suc-Ala-Xaa-Pro-Phe-4-nitroanilide' where Xaa is the amino acid tested, was found to be Phe > Leu >> Ile > Lys = Ala > Trp > His >> Gln (PubMed:9188461). {ECO:0000269|PubMed:9188461, ECO:0000305}. | Escherichia coli (strain K12) |
P0AEM6 | FLIA_ECOLI | MNSLYTAEGVMDKHSLWQRYVPLVRHEALRLQVRLPASVELDDLLQAGGIGLLNAVERYDALQGTAFTTYAVQRIRGAMLDELRSRDWVPRSVRRNAREVAQAIGQLEQELGRNATETEVAERLGIDIADYRQMLLDTNNSQLFSYDEWREEHGDSIELVTDDHQRENPLQQLLDSNLRQRVMEAIETLPEREKLVLTLYYQEELNLKEIGAVLEVGESRVSQLHSQAIKRLRTKLGKL | null | null | bacterial-type flagellum assembly [GO:0044780]; bacterial-type flagellum-dependent cell motility [GO:0071973]; DNA-templated transcription initiation [GO:0006352]; regulation of DNA-templated transcription [GO:0006355]; regulation of DNA-templated transcription initiation [GO:2000142] | cytosol [GO:0005829]; cytosolic DNA-directed RNA polymerase complex [GO:0000345] | DNA binding [GO:0003677]; DNA-directed 5'-3' RNA polymerase activity [GO:0003899]; sigma factor activity [GO:0016987] | PF04542;PF04539;PF04545; | 1.10.1740.10;1.20.140.160; | Sigma-70 factor family, FliA subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00962}. | null | null | null | null | null | FUNCTION: Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor controls the expression of flagella-related genes. {ECO:0000255|HAMAP-Rule:MF_00962, ECO:0000269|PubMed:2644646, ECO:0000269|PubMed:3536871, ECO:0000269|PubM... | Escherichia coli (strain K12) |
P0AEM9 | TCYJ_ECOLI | MKLAHLGRQALMGVMAVALVAGMSVKSFADEGLLNKVKERGTLLVGLEGTYPPFSFQGDDGKLTGFEVEFAQQLAKHLGVEASLKPTKWDGMLASLDSKRIDVVINQVTISDERKKKYDFSTPYTISGIQALVKKGNEGTIKTADDLKGKKVGVGLGTNYEEWLRQNVQGVDVRTYDDDPTKYQDLRVGRIDAILVDRLAALDLVKKTNDTLAVTGEAFSRQESGVALRKGNEDLLKAVNDAIAEMQKDGTLQALSEKWFGADVTK | null | null | cysteine transmembrane transport [GO:1903712]; L-cystine transport [GO:0015811]; sulfur utilization [GO:0006791] | ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing [GO:0055052]; outer membrane-bounded periplasmic space [GO:0030288] | amino acid binding [GO:0016597]; L-cystine transmembrane transporter activity [GO:0015184]; ligand-gated monoatomic ion channel activity [GO:0015276] | PF00497; | 3.40.190.10; | Bacterial solute-binding protein 3 family | null | SUBCELLULAR LOCATION: Periplasm {ECO:0000305|PubMed:20351115}. | null | null | null | null | null | FUNCTION: Part of the ABC transporter complex TcyJLN involved in L-cystine import (PubMed:20351115, PubMed:25139244, PubMed:25837721, PubMed:26350134). This high affinity cystine transporter is involved in resistance to oxidative stress by forming a L-cysteine/L-cystine shuttle system with the EamA transporter, which e... | Escherichia coli (strain K12) |
P0AEN1 | FRE_ECOLI | MTTLSCKVTSVEAITDTVYRVRIVPDAAFSFRAGQYLMVVMDERDKRPFSMASTPDEKGFIELHIGASEINLYAKAVMDRILKDHQIVVDIPHGEAWLRDDEERPMILIAGGTGFSYARSILLTALARNPNRDITIYWGGREEQHLYDLCELEALSLKHPGLQVVPVVEQPEAGWRGRTGTVLTAVLQDHGTLAEHDIYIAGRFEMAKIARDLFCSERNAREDRLFGDAFAFI | 1.5.1.41 | null | iron ion transport [GO:0006826]; protein repair [GO:0030091]; response to oxidative stress [GO:0006979] | cytosol [GO:0005829] | enzyme activator activity [GO:0008047]; riboflavin reductase (NAD(P)H) activity [GO:0052875]; riboflavin reductase (NADPH) activity [GO:0042602] | PF00970;PF00175; | 3.40.50.80;2.40.30.10; | Fre/LuxG FAD/NAD(P) flavoprotein oxidoreductase family | null | null | CATALYTIC ACTIVITY: Reaction=NADP(+) + reduced riboflavin = 2 H(+) + NADPH + riboflavin; Xref=Rhea:RHEA:19377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17607, ChEBI:CHEBI:57783, ChEBI:CHEBI:57986, ChEBI:CHEBI:58349; EC=1.5.1.41; Evidence={ECO:0000250|UniProtKB:Q9L6L9}; CATALYTIC ACTIVITY: Reaction=NAD(+) + reduced riboflavin = 2... | null | null | null | null | FUNCTION: Catalyzes the reduction of soluble flavins by reduced pyridine nucleotides. {ECO:0000250|UniProtKB:Q9L6L9}. | Escherichia coli (strain K12) |
P0AEN4 | FTSL_ECOLI | MISRVTEALSKVKGSMGSHERHALPGVIGDDLLRFGKLPLCLFICIILTAVTVVTTAHHTRLLTAQREQLVLERDALDIEWRNLILEENALGDHSRVERIATEKLQMQHVDPSQENIVVQK | null | null | cell division [GO:0051301]; division septum assembly [GO:0000917]; FtsZ-dependent cytokinesis [GO:0043093] | cell division site [GO:0032153]; divisome complex [GO:1990586]; FtsBL complex [GO:1990588]; FtsQBL complex [GO:1990587]; plasma membrane [GO:0005886] | null | PF04999; | null | FtsL family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_00910, ECO:0000269|PubMed:10027987, ECO:0000269|PubMed:11703663, ECO:0000269|PubMed:11948172, ECO:0000269|PubMed:1332942, ECO:0000269|PubMed:15165235}; Single-pass type II membrane protein {ECO:0000255|HAMAP-Rule:MF_00910, ECO:0000269|PubMed:10027987,... | null | null | null | null | null | FUNCTION: Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic. Can also mediate Zn(2+)-sensitivity probably by increasing the permeability of the inner membrane. {ECO:... | Escherichia coli (strain K12) |
P0AEN8 | FUCM_ECOLI | MLKTISPLISPELLKVLAEMGHGDEIIFSDAHFPAHSMGPQVIRADGLLVSDLLQAIIPLFELDSYAPPLVMMAAVEGDTLDPEVERRYRNALSLQAPCPDIIRINRFAFYERAQKAFAIVITGERAKYGNILLKKGVTP | 5.1.3.29; 5.4.99.62 | null | fucose metabolic process [GO:0006004]; fucosylation [GO:0036065]; L-fucose metabolic process [GO:0042354] | cytoplasm [GO:0005737] | D-ribose pyranase activity [GO:0062193]; fucose binding [GO:0042806]; identical protein binding [GO:0042802]; L-fucose mutarotase activity [GO:0036373]; racemase and epimerase activity, acting on carbohydrates and derivatives [GO:0016857] | PF05025; | 3.40.1650.10; | RbsD / FucU family, FucU mutarotase subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=alpha-L-fucose = beta-L-fucose; Xref=Rhea:RHEA:25580, ChEBI:CHEBI:42548, ChEBI:CHEBI:42589; EC=5.1.3.29; Evidence={ECO:0000269|PubMed:15060078, ECO:0000269|PubMed:19524593}; CATALYTIC ACTIVITY: Reaction=beta-D-ribopyranose = beta-D-ribofuranose; Xref=Rhea:RHEA:25432, ChEBI:CHEBI:27476, ChEB... | null | PATHWAY: Carbohydrate metabolism; L-fucose metabolism. {ECO:0000269|PubMed:15060078, ECO:0000269|PubMed:19524593}. | null | null | FUNCTION: Involved in the anomeric conversion of L-fucose. Catalyzes also the interconversion of beta-pyran and beta-furan forms of D-ribose. {ECO:0000269|PubMed:15060078, ECO:0000269|PubMed:19524593}. | Escherichia coli (strain K12) |
P0AEP3 | GALU_ECOLI | MAAINTKVKKAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSIENHFDTSFELEAMLEKRVKRQLLDEVQSICPPHVTIMQVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDVILDEYESDLSQDNLAEMIRRFDETGHSQIMVEPVADVTAYGVVDCKGVELAPGESVPMVGVVEKPKADVAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTDAIDMLIEKETVEAYHMKGKSHDCGNKLGYMQAFVEYGIRHNTLGTEFKAWLEEEMGIKK | 2.7.7.9 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:7961613}; | colanic acid biosynthetic process [GO:0009242]; galactose catabolic process via UDP-galactose [GO:0033499]; lipopolysaccharide core region biosynthetic process [GO:0009244]; osmoregulated periplasmic glucan biosynthetic process [GO:1900727]; UDP-glucose metabolic process [GO:0006011] | cytosol [GO:0005829]; protein-containing complex [GO:0032991] | identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; UTP:glucose-1-phosphate uridylyltransferase activity [GO:0003983] | PF00483; | null | UDPGP type 2 family | null | null | CATALYTIC ACTIVITY: Reaction=alpha-D-glucose 1-phosphate + H(+) + UTP = diphosphate + UDP-alpha-D-glucose; Xref=Rhea:RHEA:19889, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:58601, ChEBI:CHEBI:58885; EC=2.7.7.9; Evidence={ECO:0000269|PubMed:7961613}; | null | null | null | null | FUNCTION: May play a role in stationary phase survival. | Escherichia coli (strain K12) |
P0AEP7 | GCL_ECOLI | MAKMRAVDAAMYVLEKEGITTAFGVPGAAINPFYSAMRKHGGIRHILARHVEGASHMAEGYTRATAGNIGVCLGTSGPAGTDMITALYSASADSIPILCITGQAPRARLHKEDFQAVDIEAIAKPVSKMAVTVREAALVPRVLQQAFHLMRSGRPGPVLVDLPFDVQVAEIEFDPDMYEPLPVYKPAASRMQIEKAVEMLIQAERPVIVAGGGVINADAAALLQQFAELTSVPVIPTLMGWGCIPDDHELMAGMVGLQTAHRYGNATLLASDMVFGIGNRFANRHTGSVEKYTEGRKIVHIDIEPTQIGRVLCPDLGIVS... | 4.1.1.47 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250}; COFACTOR: Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; Evidence={ECO:0000250}; Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000250}; | glycolate catabolic process [GO:0046296]; glyoxylate catabolic process [GO:0009436]; isoleucine biosynthetic process [GO:0009097]; valine biosynthetic process [GO:0009099] | acetolactate synthase complex [GO:0005948] | FAD binding [GO:0071949]; flavin adenine dinucleotide binding [GO:0050660]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; tartronate-semialdehyde synthase activity [GO:0009028]; thiamine pyrophosphate binding [GO:0030976] | PF02775;PF00205;PF02776; | 3.40.50.970;3.40.50.1220; | TPP enzyme family | null | null | CATALYTIC ACTIVITY: Reaction=2 glyoxylate + H(+) = 2-hydroxy-3-oxopropanoate + CO2; Xref=Rhea:RHEA:10136, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:36655, ChEBI:CHEBI:57978; EC=4.1.1.47; | null | PATHWAY: Organic acid metabolism; glycolate degradation; 3-phospho-D-glycerate from glycolate: step 2/4. | null | null | FUNCTION: Catalyzes the condensation of two molecules of glyoxylate to give 2-hydroxy-3-oxopropanoate (also termed tartronate semialdehyde). | Escherichia coli (strain K12) |
P0AEP9 | GLCD_ECOLI | MSILYEERLDGALPDVDRTSVLMALREHVPGLEILHTDEEIIPYECDGLSAYRTRPLLVVLPKQMEQVTAILAVCHRLRVPVVTRGAGTGLSGGALPLEKGVLLVMARFKEILDINPVGRRARVQPGVRNLAISQAVAPHNLYYAPDPSSQIACSIGGNVAENAGGVHCLKYGLTVHNLLKIEVQTLDGEALTLGSDALDSPGFDLLALFTGSEGMLGVTTEVTVKLLPKPPVARVLLASFDSVEKAGLAVGDIIANGIIPGGLEMMDNLSIRAAEDFIHAGYPVDAEAILLCELDGVESDVQEDCERVNDILLKAGATD... | 1.1.99.14 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305}; | DNA damage response [GO:0006974]; glycolate catabolic process [GO:0046296] | glycolate oxidase complex [GO:0009339]; plasma membrane [GO:0005886] | (S)-2-hydroxy-acid oxidase activity [GO:0003973]; D-2-hydroxy-acid dehydrogenase activity [GO:0047809]; FAD binding [GO:0071949]; glycolate dehydrogenase activity [GO:0019154] | PF02913;PF01565; | 3.30.465.10;3.30.70.2190;3.30.70.2740;3.30.43.10; | FAD-binding oxidoreductase/transferase type 4 family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:2689218}. Note=Glycolate oxidoreductase activity was shown to be firmly associated with the cytoplasmic membranes. {ECO:0000269|PubMed:2689218}. | CATALYTIC ACTIVITY: Reaction=A + glycolate = AH2 + glyoxylate; Xref=Rhea:RHEA:21264, ChEBI:CHEBI:13193, ChEBI:CHEBI:17499, ChEBI:CHEBI:29805, ChEBI:CHEBI:36655; EC=1.1.99.14; Evidence={ECO:0000269|PubMed:4557653, ECO:0000305|PubMed:8606183}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21265; Evidence={ECO:0000... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=40 uM for glycolate {ECO:0000269|PubMed:4557653}; KM=0.7 mM for D-lactate {ECO:0000269|PubMed:4557653}; Note=Parameters measured from a partially purified enzyme from extracts of glycolate grown cells. {ECO:0000305|PubMed:4557653}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0-8.8. {ECO:0000269|PubMed:4557653}; | null | FUNCTION: Component of a complex that catalyzes the oxidation of glycolate to glyoxylate (PubMed:4557653, PubMed:8606183). Is required for E.coli to grow on glycolate as a sole source of carbon (PubMed:8606183). Is also able to oxidize D-lactate ((R)-lactate) with a similar rate (PubMed:4557653). Does not link directly... | Escherichia coli (strain K12) |
P0AER0 | GLPF_ECOLI | MSQTSTLKGQCIAEFLGTGLLIFFGVGCVAALKVAGASFGQWEISVIWGLGVAMAIYLTAGVSGAHLNPAVTIALWLFACFDKRKVIPFIVSQVAGAFCAAALVYGLYYNLFFDFEQTHHIVRGSVESVDLAGTFSTYPNPHINFVQAFAVEMVITAILMGLILALTDDGNGVPRGPLAPLLIGLLIAVIGASMGPLTGFAMNPARDFGPKVFAWLAGWGNVAFTGGRDIPYFLVPLFGPIVGAIVGAFAYRKLIGRHLPCDICVVEEKETTTPSEQKASL | null | null | cellular response to mercury ion [GO:0071288]; glycerol transmembrane transport [GO:0015793] | plasma membrane [GO:0005886] | glycerol channel activity [GO:0015254]; glycerol transmembrane transporter activity [GO:0015168]; urea transmembrane transporter activity [GO:0015204] | PF00230; | 1.20.1080.10; | MIP/aquaporin (TC 1.A.8) family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:11039922, ECO:0000269|PubMed:11964478, ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000269|PubMed:11039922, ECO:0000269|PubMed:11964478}. | CATALYTIC ACTIVITY: Reaction=glycerol(in) = glycerol(out); Xref=Rhea:RHEA:29675, ChEBI:CHEBI:17754; Evidence={ECO:0000269|PubMed:11039922, ECO:0000269|PubMed:11226336, ECO:0000269|PubMed:6998951, ECO:0000269|PubMed:7512955}; | null | null | null | null | FUNCTION: Mediates glycerol diffusion across the cytoplasmic membrane via a pore-type mechanism (PubMed:11039922, PubMed:11226336, PubMed:6998951, PubMed:7512955). Is highly permeable to glycerol, but less well permeated by water (PubMed:11226336). Does not transport ions (PubMed:7512955). It may also have limited perm... | Escherichia coli (strain K12) |
P0AES0 | GSP_ECOLI | MSKGTTSQDAPFGTLLGYAPGGVAIYSSDYSSLDPQEYEDDAVFRSYIDDEYMGHKWQCVEFARRFLFLNYGVVFTDVGMAWEIFSLRFLREVVNDNILPLQAFPNGSPRAPVAGALLIWDKGGEFKDTGHVAIITQLHGNKVRIAEQNVIHSPLPQGQQWTRELEMVVENGCYTLKDTFDDTTILGWMIQTEDTEYSLPQPEIAGELLKISGARLENKGQFDGKWLDEKDPLQNAYVQANGQVINQDPYHYYTITESAEQELIKATNELHLMYLHATDKVLKDDNLLALFDIPKILWPRLRLSWQRRRHHMITGRMDFC... | 3.5.1.78; 6.3.1.8 | null | glutathione metabolic process [GO:0006749]; spermidine metabolic process [GO:0008216] | cytosol [GO:0005829] | ATP binding [GO:0005524]; glutathionylspermidine amidase activity [GO:0008884]; glutathionylspermidine synthase activity [GO:0008885]; metal ion binding [GO:0046872] | PF05257;PF03738; | 3.30.1490.330;3.90.1720.10; | Glutathionylspermidine synthase preATP-grasp family | PTM: Oxidation of Cys-59 to sulfenic acid during oxidative stress selectively inhibits the amidase activity which leads to a rapid increase in the amounts of intracellular Gsp and Gsp S-thiolated proteins (GspSSPs). {ECO:0000269|PubMed:20530482}. | null | CATALYTIC ACTIVITY: Reaction=ATP + glutathione + spermidine = ADP + glutathionylspermidine + H(+) + phosphate; Xref=Rhea:RHEA:21272, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57834, ChEBI:CHEBI:57835, ChEBI:CHEBI:57925, ChEBI:CHEBI:456216; EC=6.3.1.8; Evidence={ECO:0000269|PubMed:20530482, EC... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=100 uM for ATP (at pH 6.8) {ECO:0000269|PubMed:17124497, ECO:0000269|PubMed:7775463}; KM=800 uM for glutathione (at pH 6.8) {ECO:0000269|PubMed:17124497, ECO:0000269|PubMed:7775463}; KM=218 uM for glutathione {ECO:0000269|PubMed:17124497, ECO:0000269|PubMed:7775463... | PATHWAY: Sulfur metabolism; glutathione metabolism.; PATHWAY: Amine and polyamine metabolism; spermidine metabolism. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is around 6.8 for Gsp synthetase activity. {ECO:0000269|PubMed:7775463}; | null | FUNCTION: Catalyzes the formation of an amide bond between glutathione (GSH) and spermidine coupled with hydrolysis of ATP; also catalyzes the opposing reaction, i.e. the hydrolysis of glutathionylspermidine (Gsp) back to glutathione and spermidine. The amidase active site can also hydrolyze Gsp-disulfide (Gsp-S-S-Gsp)... | Escherichia coli (strain K12) |
P0AES1 | GSP_SHIFL | MSKGTTSQDAPFGTLLGYAPGGVAIYSSDYSSLDPQEYEDDAVFRSYIDDEYMGHKWQCVEFARRFLFLNYGVVFTDVGMAWEIFSLRFLREVVNDNILPLQAFPNGSPRAPVAGALLIWDKGGEFKDTGHVAIITQLHGNKVRIAEQNVIHSPLPQGQQWTRELEMVVENGCYTLKDTFDDTTILGWMIQTEDTEYSLPQPEIAGELLKISGARLENKGQFDGKWLDEKDPLQNAYVQANGQVINQDPYHYYTITESAEQELIKATNELHLMYLHATDKVLKDDNLLALFDIPKILWPRLRLSWQRRRHHMITGRMDFC... | 3.5.1.78; 6.3.1.8 | null | glutathione metabolic process [GO:0006749]; spermidine metabolic process [GO:0008216] | null | ATP binding [GO:0005524]; glutathionylspermidine amidase activity [GO:0008884]; glutathionylspermidine synthase activity [GO:0008885]; metal ion binding [GO:0046872] | PF05257;PF03738; | 3.30.1490.330;3.90.1720.10; | Glutathionylspermidine synthase preATP-grasp family | PTM: Oxidation of Cys-59 to sulfenic acid during oxidative stress selectively inhibits the amidase activity. {ECO:0000250|UniProtKB:P0AES0}. | null | CATALYTIC ACTIVITY: Reaction=ATP + glutathione + spermidine = ADP + glutathionylspermidine + H(+) + phosphate; Xref=Rhea:RHEA:21272, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57834, ChEBI:CHEBI:57835, ChEBI:CHEBI:57925, ChEBI:CHEBI:456216; EC=6.3.1.8; Evidence={ECO:0000250|UniProtKB:P0AES0}; ... | null | PATHWAY: Sulfur metabolism; glutathione metabolism.; PATHWAY: Amine and polyamine metabolism; spermidine metabolism. | null | null | FUNCTION: Catalyzes the formation of an amide bond between glutathione (GSH) and spermidine coupled with hydrolysis of ATP; also catalyzes the opposing reaction, i.e. the hydrolysis of glutathionylspermidine (Gsp) back to glutathione and spermidine. May act synergistically with glutaredoxin to regulate the redox enviro... | Shigella flexneri |
P0AES2 | GUDD_ECOLI | MSSQFTTPVVTEMQVIPVAGHDSMLMNLSGAHAPFFTRNIVIIKDNSGHTGVGEIPGGEKIRKTLEDAIPLVVGKTLGEYKNVLTLVRNTFADRDAGGRGLQTFDLRTTIHVVTGIEAAMLDLLGQHLGVNVASLLGDGQQRSEVEMLGYLFFVGNRKATPLPYQSQPDDSCDWYRLRHEEAMTPDAVVRLAEAAYEKYGFNDFKLKGGVLAGEEEAESIVALAQRFPQARITLDPNGAWSLNEAIKIGKYLKGSLAYAEDPCGAEQGFSGREVMAEFRRATGLPTATNMIATDWRQMGHTLSLQSVDIPLADPHFWTMQ... | 4.2.1.40 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:10769114}; | D-glucarate catabolic process [GO:0042838] | null | glucarate dehydratase activity [GO:0008872]; magnesium ion binding [GO:0000287] | PF13378; | 3.20.20.120;3.30.390.10; | Mandelate racemase/muconate lactonizing enzyme family, GlucD subfamily | null | null | CATALYTIC ACTIVITY: Reaction=D-glucarate = 5-dehydro-4-deoxy-D-glucarate + H2O; Xref=Rhea:RHEA:14573, ChEBI:CHEBI:15377, ChEBI:CHEBI:30612, ChEBI:CHEBI:42819; EC=4.2.1.40; Evidence={ECO:0000269|PubMed:9772162}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=16 uM for idarate {ECO:0000269|PubMed:9772162}; KM=60 uM for glucarate {ECO:0000269|PubMed:9772162}; | PATHWAY: Carbohydrate acid metabolism; D-glucarate degradation; 2,5-dioxopentanoate from D-glucarate: step 1/2. | null | null | FUNCTION: Catalyzes the dehydration of glucarate or L-idarate to 5-keto-4-deoxy-D-glucarate (5-kdGluc) (PubMed:9772162). Also catalyzes the epimerization of D-glucarate and L-idarate (PubMed:11513584). {ECO:0000269|PubMed:11513584, ECO:0000269|PubMed:9772162}. | Escherichia coli (strain K12) |
P0AES4 | GYRA_ECOLI | MSDLAREITPVNIEEELKSSYLDYAMSVIVGRALPDVRDGLKPVHRRVLYAMNVLGNDWNKAYKKSARVVGDVIGKYHPHGDSAVYDTIVRMAQPFSLRYMLVDGQGNFGSIDGDSAAAMRYTEIRLAKIAHELMADLEKETVDFVDNYDGTEKIPDVMPTKIPNLLVNGSSGIAVGMATNIPPHNLTEVINGCLAYIDDEDISIEGLMEHIPGPDFPTAAIINGRRGIEEAYRTGRGKVYIRARAEVEVDAKTGRETIIVHEIPYQVNKARLIEKIAELVKEKRVEGISALRDESDKDGMRIVIEVKRDAVGEVVLNNL... | 5.6.2.2 | null | DNA topological change [GO:0006265]; DNA-templated DNA replication [GO:0006261]; DNA-templated transcription [GO:0006351]; negative regulation of DNA-templated DNA replication [GO:2000104]; response to antibiotic [GO:0046677]; response to xenobiotic stimulus [GO:0009410] | chromosome [GO:0005694]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex [GO:0009330]; membrane [GO:0016020] | ATP binding [GO:0005524]; ATP-dependent activity, acting on DNA [GO:0008094]; DNA binding [GO:0003677]; DNA negative supercoiling activity [GO:0034335]; DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity [GO:0003918]; identical protein binding [GO:0042802] | PF03989;PF00521; | 3.30.1360.40;2.120.10.90;3.90.199.10;1.10.268.10; | Type II topoisomerase GyrA/ParC subunit family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01897}. | CATALYTIC ACTIVITY: Reaction=ATP-dependent breakage, passage and rejoining of double-stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000255|HAMAP-Rule:MF_01897, ECO:0000269|PubMed:12051842, ECO:0000269|PubMed:18642932, ECO:0000269|PubMed:186775, ECO:0000269|PubMed:19965760, ECO:0000269|PubMed:9278055}; | null | null | null | null | FUNCTION: A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to maintain chromosomes in an underwound state (PubMed:12051842, PubMed:18642932, PubMed:186775, PubMed:19060136, PubMed:19965760, PubMed:20356737, PubMed:22457353, PubMed:23294697, PubMed:30... | Escherichia coli (strain K12) |
P0AES6 | GYRB_ECOLI | MSNSYDSSSIKVLKGLDAVRKRPGMYIGDTDDGTGLHHMVFEVVDNAIDEALAGHCKEIIVTIHADNSVSVQDDGRGIPTGIHPEEGVSAAEVIMTVLHAGGKFDDNSYKVSGGLHGVGVSVVNALSQKLELVIQREGKIHRQIYEHGVPQAPLAVTGETEKTGTMVRFWPSLETFTNVTEFEYEILAKRLRELSFLNSGVSIRLRDKRDGKEDHFHYEGGIKAFVEYLNKNKTPIHPNIFYFSTEKDGIGVEVALQWNDGFQENIYCFTNNIPQRDGGTHLAGFRAAMTRTLNAYMDKEGYSKKAKVSATGDDAREGLI... | 5.6.2.2 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_01898, ECO:0000269|PubMed:12051843, ECO:0000269|PubMed:18642932}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP-Rule:MF_01898, ECO:0000269|PubMed:12051843, ECO:0000269|PubMed:18642932}; Name=Ca(2+); Xref=ChEBI:CHEBI:29... | DNA topological change [GO:0006265]; DNA-templated DNA replication [GO:0006261]; DNA-templated transcription [GO:0006351]; response to antibiotic [GO:0046677]; response to xenobiotic stimulus [GO:0009410] | chromosome [GO:0005694]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex [GO:0009330] | ATP binding [GO:0005524]; ATP-dependent activity, acting on DNA [GO:0008094]; DNA binding [GO:0003677]; DNA negative supercoiling activity [GO:0034335]; DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity [GO:0003918]; metal ion binding [GO:0046872] | PF00204;PF00986;PF21249;PF18053;PF02518;PF01751; | 3.10.20.690;3.30.230.10;3.40.50.670;3.30.565.10; | Type II topoisomerase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01898}. | CATALYTIC ACTIVITY: Reaction=ATP-dependent breakage, passage and rejoining of double-stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000255|HAMAP-Rule:MF_01898, ECO:0000269|PubMed:12051842, ECO:0000269|PubMed:12051843, ECO:0000269|PubMed:18642932, ECO:0000269|PubMed:186775, ECO:0000269|PubMed:19965760, ECO:0000269|PubMed:206... | null | null | null | null | FUNCTION: DNA gyrase negatively supercoils closed circular double-stranded DNA in an ATP-dependent manner to maintain chromosomes in an underwound state (PubMed:12051842, PubMed:12051843, PubMed:1323022, PubMed:18642932, PubMed:186775, PubMed:19060136, PubMed:19965760, PubMed:20356737, PubMed:20675723, PubMed:22457353,... | Escherichia coli (strain K12) |
P0AES9 | HDEA_ECOLI | MKKVLGVILGGLLLLPVVSNAADAQKAADNKKPVNSWTCEDFLAVDESFQPTAVGFAEALNNKDKPEDAVLDVQGIATVTPAIVQACTQDKQANFKDKVKGEWDKIKKDM | null | null | cellular stress response to acidic pH [GO:1990451]; chaperone-mediated protein folding [GO:0061077] | outer membrane-bounded periplasmic space [GO:0030288] | identical protein binding [GO:0042802]; protein folding chaperone [GO:0044183]; protein homodimerization activity [GO:0042803]; unfolded protein binding [GO:0051082] | PF06411; | 1.10.890.10; | HdeA family | null | SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_00946, ECO:0000269|PubMed:17085547}. | null | null | null | null | null | FUNCTION: Required for optimal acid stress protection. Exhibits a chaperone-like activity only at pH below 3 by suppressing non-specifically the aggregation of denaturated periplasmic proteins. Important for survival of enteric bacteria in the acidic environment of the host stomach. Also promotes the solubilization at ... | Escherichia coli (strain K12) |
P0AET2 | HDEB_ECOLI | MNISSLRKAFIFMGAVAALSLVNAQSALAANESAKDMTCQEFIDLNPKAMTPVAWWMLHEETVYKGGDTVTLNETDLTQIPKVIEYCKKNPQKNLYTFKNQASNDLPN | null | null | cellular stress response to acidic pH [GO:1990451]; response to acidic pH [GO:0010447] | outer membrane-bounded periplasmic space [GO:0030288] | unfolded protein binding [GO:0051082] | PF06411; | 1.10.890.10; | HdeB family | null | SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_00947, ECO:0000269|PubMed:17085547}. | null | null | null | null | null | FUNCTION: Required for optimal acid stress protection, which is important for survival of enteric bacteria in the acidic environment of the host stomach. Exhibits a chaperone-like activity at acidic pH by preventing the aggregation of many different periplasmic proteins. {ECO:0000255|HAMAP-Rule:MF_00947, ECO:0000269|Pu... | Escherichia coli (strain K12) |
P0AET8 | HDHA_ECOLI | MFNSDNLRLDGKCAIITGAGAGIGKEIAITFATAGASVVVSDINADAANHVVDEIQQLGGQAFACRCDITSEQELSALADFAISKLGKVDILVNNAGGGGPKPFDMPMADFRRAYELNVFSFFHLSQLVAPEMEKNGGGVILTITSMAAENKNINMTSYASSKAAASHLVRNMAFDLGEKNIRVNGIAPGAILTDALKSVITPEIEQKMLQHTPIRRLGQPQDIANAALFLCSPAASWVSGQILTVSGGGVQELN | 1.1.1.159 | null | bile acid catabolic process [GO:0030573]; lipid catabolic process [GO:0016042] | cytosol [GO:0005829]; protein-containing complex [GO:0032991] | chenodeoxycholate 7-alpha-dehydrogenase (NAD+) activity [GO:0106281]; cholate 7-alpha-dehydrogenase activity [GO:0008709]; identical protein binding [GO:0042802]; NAD binding [GO:0051287] | PF13561; | 3.40.50.720; | Short-chain dehydrogenases/reductases (SDR) family | null | null | CATALYTIC ACTIVITY: Reaction=cholate + NAD(+) = 3alpha,12alpha-dihydroxy-7-oxo-5beta-cholanate + H(+) + NADH; Xref=Rhea:RHEA:19409, ChEBI:CHEBI:11893, ChEBI:CHEBI:15378, ChEBI:CHEBI:29747, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.159; Evidence={ECO:0000269|PubMed:2007545, ECO:0000269|PubMed:9722677}; Physiologica... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.19 mM for taurochenodeoxycholate {ECO:0000269|PubMed:2007545}; KM=0.43 mM for chenodeoxycholate {ECO:0000269|PubMed:2007545}; KM=1.2 mM for cholate {ECO:0000269|PubMed:2007545}; KM=1.25 mM for glycocholate {ECO:0000269|PubMed:2007545}; KM=2 mM for taurocholate {E... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5 (PubMed:2007545). The enzyme is stable between pH 8 and 9 (PubMed:2007545). {ECO:0000269|PubMed:2007545}; | null | FUNCTION: 7alpha-hydroxysteroid dehydrogenase involved in the metabolism of bile acids. Catalyzes the NAD(+)-dependent oxidation of the 7alpha-hydroxy group of 7alpha-hydroxysteroids, such as the major human bile acids cholate and chenodeoxycholate, to the corresponding 7-oxosteroids. To a lesser extent, can also act o... | Escherichia coli (strain K12) |
P0AEU7 | SKP_ECOLI | MKKWLLAAGLGLALATSAQAADKIAIVNMGSLFQQVAQKTGVSNTLENEFKGRASELQRMETDLQAKMKKLQSMKAGSDRTKLEKDVMAQRQTFAQKAQAFEQDRARRSNEERGKLVTRIQTAVKSVANSQDIDLVVDANAVAYNSSDVKDITADVLKQVK | null | null | chaperone-mediated protein folding [GO:0061077]; Gram-negative-bacterium-type cell outer membrane assembly [GO:0043165]; protein folding [GO:0006457]; protein insertion into membrane from inner side [GO:0032978]; protein maturation by protein folding [GO:0022417]; protein stabilization [GO:0050821] | cytosol [GO:0005829]; outer membrane-bounded periplasmic space [GO:0030288] | identical protein binding [GO:0042802]; lipopolysaccharide binding [GO:0001530]; unfolded protein binding [GO:0051082] | PF03938; | 3.30.910.20; | Skp family | null | SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:1838129, ECO:0000269|PubMed:8730870}. | null | null | null | null | null | FUNCTION: Molecular chaperone that interacts specifically with outer membrane proteins, thus maintaining the solubility of early folding intermediates during passage through the periplasm. Required for the efficient release of OmpA from the inner membrane, the maintenance of its solubility in the periplasm, and, in ass... | Escherichia coli (strain K12) |
P0AEV1 | RSSB_ECOLI | MTQPLVGKQILIVEDEQVFRSLLDSWFSSLGATTVLAADGVDALELLGGFTPDLMICDIAMPRMNGLKLLEHIRNRGDQTPVLVISATENMADIAKALRLGVEDVLLKPVKDLNRLREMVFACLYPSMFNSRVEEEERLFRDWDAMVDNPAAAAKLLQELQPPVQQVISHCRVNYRQLVAADKPGLVLDIAALSENDLAFYCLDVTRAGHNGVLAALLLRALFNGLLQEQLAHQNQRLPELGALLKQVNHLLRQANLPGQFPLLVGYYHRELKNLILVSAGLNATLNTGEHQVQISNGVPLGTLGNAYLNQLSQRCDAWQ... | null | null | negative regulation of DNA-templated transcription [GO:0045892]; positive regulation of proteolysis [GO:0045862]; protein destabilization [GO:0031648]; regulation of DNA-templated transcription [GO:0006355] | cytosol [GO:0005829]; protein-DNA complex [GO:0032993]; sigma factor antagonist complex [GO:1903865] | phosphorelay response regulator activity [GO:0000156]; sigma factor antagonist activity [GO:0016989]; transcription cis-regulatory region binding [GO:0000976] | PF00072; | 3.40.50.2300;3.60.40.10; | RssB family | PTM: Phosphorylated. Phosphorylation stimulates the interaction with RpoS and, therefore, the proteolysis of RpoS. {ECO:0000255|HAMAP-Rule:MF_00958, ECO:0000269|PubMed:10339606, ECO:0000269|PubMed:11442836, ECO:0000269|PubMed:24352426, ECO:0000269|PubMed:9515704}. | null | null | null | null | null | null | FUNCTION: Regulates the turnover of the sigma S factor (RpoS) by promoting its proteolysis in exponentially growing cells. Acts by binding and delivering RpoS to the ClpXP protease. RssB is not co-degraded with RpoS, but is released from the complex and can initiate a new cycle of RpoS recognition and degradation. In s... | Escherichia coli (strain K12) |
P0AEV9 | HYCI_ECOLI | MTDVLLCVGNSMMGDDGAGPLLAEKCAAAPKGNWVVIDGGSAPENDIVAIRELRPTRLLIVDATDMGLNPGEIRIIDPDDIAEMFMMTTHNMPLNYLIDQLKEDIGEVIFLGIQPDIVGFYYPMTQPIKDAVETVYQRLEGWEGNGGFAQLAVEEE | 3.4.23.51 | null | protein processing [GO:0016485] | null | aspartic-type endopeptidase activity [GO:0004190]; endopeptidase activity [GO:0004175]; enzyme activator activity [GO:0008047]; metal ion binding [GO:0046872] | PF01750; | 3.40.50.1450; | Peptidase A31 family | null | null | CATALYTIC ACTIVITY: Reaction=This enzyme specifically removes a 32-amino acid peptide from the C-terminus of the precursor of the large subunit of E.coli hydrogenase 3 by cleavage at the C-terminal side of Arg-537.; EC=3.4.23.51; Evidence={ECO:0000269|PubMed:10727938}; | null | null | null | null | FUNCTION: Protease involved in the C-terminal processing of HycE, the large subunit of hydrogenase 3. {ECO:0000269|PubMed:10727938}. | Escherichia coli (strain K12) |
P0AEW6 | INGK_ECOLI | MKFPGKRKSKHYFPVNARDPLLQQFQPENETSAAWVVGIDQTLVDIEAKVDDEFIERYGLSAGHSLVIEDDVAEALYQELKQKNLITHQFAGGTIGNTMHNYSVLADDRSVLLGVMCSNIEIGSYAYRYLCNTSSRTDLNYLQGVDGPIGRCFTLIGESGERTFAISPGHMNQLRAESIPEDVIAGASALVLTSYLVRCKPGEPMPEATMKAIEYAKKYNVPVVLTLGTKFVIAENPQWWQQFLKDHVSILAMNEDEAEALTGESDPLLASDKALDWVDLVLCTAGPIGLYMAGFTEDEAKRKTQHPLLPGAIAEFNQYE... | 2.7.1.73 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_02246, ECO:0000269|PubMed:10879466, ECO:0000269|PubMed:7665468}; Note=Mg(2+) is probably required for activity in addition to its role in forming the Mg-ATP complex. {ECO:0000269|PubMed:10879466}; | GMP salvage [GO:0032263]; IMP salvage [GO:0032264]; phosphorylation [GO:0016310]; purine ribonucleoside salvage [GO:0006166] | null | ATP binding [GO:0005524]; guanosine kinase activity [GO:0106366]; guanosine tetraphosphate binding [GO:0097216]; inosine kinase activity [GO:0008906] | PF00294; | 3.40.1190.20; | Carbohydrate kinase PfkB family | null | null | CATALYTIC ACTIVITY: Reaction=ATP + guanosine = ADP + GMP + H(+); Xref=Rhea:RHEA:27710, ChEBI:CHEBI:15378, ChEBI:CHEBI:16750, ChEBI:CHEBI:30616, ChEBI:CHEBI:58115, ChEBI:CHEBI:456216; EC=2.7.1.73; Evidence={ECO:0000255|HAMAP-Rule:MF_02246, ECO:0000269|PubMed:10879466, ECO:0000269|PubMed:7665468}; PhysiologicalDirection=... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=6.1 uM for guanosine {ECO:0000269|PubMed:7665468}; KM=7.8 uM for guanosine {ECO:0000269|PubMed:10879466}; KM=2.1 mM for inosine {ECO:0000269|PubMed:7665468}; KM=1.5 mM for inosine {ECO:0000269|PubMed:10879466}; KM=4.3 mM for deoxyguanosine {ECO:0000269|PubMed:10879... | PATHWAY: Purine metabolism; IMP biosynthesis via salvage pathway; IMP from inosine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_02246, ECO:0000305|PubMed:11440147}.; PATHWAY: Purine metabolism; GMP biosynthesis via salvage pathway. {ECO:0000255|HAMAP-Rule:MF_02246, ECO:0000305|PubMed:11440147}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.2 for guanosine kinase activity. Optimum pH is 6.9 for inosine kinase activity. {ECO:0000269|PubMed:7665468}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 38 degrees Celsius for guanosine kinase activity and between 26 and 39 degrees Celsius for inosine kinase activity. {ECO:0000269|PubMed:7665468}; | FUNCTION: Catalyzes the phosphorylation of guanosine and inosine to GMP and IMP, respectively (PubMed:10879466, PubMed:7665468, PubMed:7721718). Can also use deoxyguanosine and xanthosine, but not adenosine, uridine, cytidine or deoxythymidine (PubMed:10879466, PubMed:7665468). Shows a strong preference for guanosine (... | Escherichia coli (strain K12) |
P0AEW9 | K1PF_ECOLI | MSRRVATITLNPAYDLVGFCPEIERGEVNLVKTTGLHAAGKGINVAKVLKDLGIDVTVGGFLGKDNQDGFQQLFSELGIANRFQVVQGRTRINVKLTEKDGEVTDFNFSGFEVTPADWERFVTDSLSWLGQFDMVCVSGSLPSGVSPEAFTDWMTRLRSQCPCIIFDSSREALVAGLKAAPWLVKPNRRELEIWAGRKLPEMKDVIEAAHALREQGIAHVVISLGAEGALWVNASGEWIAKPPSVDVVSTVGAGDSMVGGLIYGLLMRESSEHTLRLATAVAALAVSQSNVGITDRPQLAAMMARVDLQPFN | 2.7.1.56 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|Ref.6}; Note=Can also use Mn(2+) or Co(2+), with lower efficiency. {ECO:0000269|Ref.6}; | fructose catabolic process [GO:0006001] | cytosol [GO:0005829] | 1-phosphofructokinase activity [GO:0008662]; ATP binding [GO:0005524]; phosphofructokinase activity [GO:0008443] | PF00294; | 3.40.1190.20; | Carbohydrate kinase PfkB family | null | null | CATALYTIC ACTIVITY: Reaction=ATP + beta-D-fructose 1-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+); Xref=Rhea:RHEA:14213, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:32966, ChEBI:CHEBI:138881, ChEBI:CHEBI:456216; EC=2.7.1.56; Evidence={ECO:0000269|PubMed:10833389, ECO:0000269|Ref.6}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.25 mM for fructose 1-phosphate {ECO:0000269|Ref.6}; KM=0.36 mM for fructose 1-phosphate (in the absence of KCl) {ECO:0000269|PubMed:10833389}; KM=0.125 mM for fructose 1-phosphate (in the presence of 50 mM KCl) {ECO:0000269|PubMed:10833389}; KM=0.12 mM for ATP {E... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.8 in 50 mM Tris-HC1 and 8.5 in 50 mM NH(4)HCO(3). {ECO:0000269|Ref.6}; | null | FUNCTION: Catalyzes the ATP-dependent phosphorylation of fructose-l-phosphate to fructose-l,6-bisphosphate (PubMed:10833389, Ref.6). Is specific for fructose-l-phosphate (Ref.6). GTP, UTP and CTP can also function as phosphoryl donors showing 60%, 20% and 10% of the activity of ATP (Ref.6). {ECO:0000269|PubMed:10833389... | Escherichia coli (strain K12) |
P0AEX7 | LIVH_ECOLI | MSEQFLYFLQQMFNGVTLGSTYALIAIGYTMVYGIIGMINFAHGEVYMIGSYVSFMIIAALMMMGIDTGWLLVAAGFVGAIVIASAYGWSIERVAYRPVRNSKRLIALISAIGMSIFLQNYVSLTEGSRDVALPSLFNGQWVVGHSENFSASITTMQAVIWIVTFLAMLALTIFIRYSRMGRACRACAEDLKMASLLGINTDRVIALTFVIGAAMAAVAGVLLGQFYGVINPYIGFMAGMKAFTAAVLGGIGSIPGAMIGGLILGIAEALSSAYLSTEYKDVVSFALLILVLLVMPTGILGRPEVEKV | null | null | branched-chain amino acid transport [GO:0015803]; D-alanine transmembrane transport [GO:0042941]; isoleucine transmembrane transport [GO:1903714]; L-alanine transport [GO:0015808]; L-isoleucine import across plasma membrane [GO:1903806]; L-valine transmembrane transport [GO:1903785]; leucine import across plasma membra... | ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing [GO:0055052]; membrane [GO:0016020]; plasma membrane [GO:0005886] | branched-chain amino acid transmembrane transporter activity [GO:0015658]; L-isoleucine transmembrane transporter activity [GO:0015188]; L-leucine transmembrane transporter activity [GO:0015190]; L-phenylalanine transmembrane transporter activity [GO:0015192]; L-valine transmembrane transporter activity [GO:0005304] | PF02653; | null | Binding-protein-dependent transport system permease family, LivHM subfamily | null | SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. | null | null | null | null | null | FUNCTION: Part of the binding-protein-dependent transport system for branched-chain amino acids. Probably responsible for the translocation of the substrates across the membrane. | Escherichia coli (strain K12) |
P0AEX9 | MALE_ECOLI | MKIKTGARILALSALTTMMFSASALAKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVN... | null | null | carbohydrate transport [GO:0008643]; cell chemotaxis [GO:0060326]; detection of maltose stimulus [GO:0034289]; DNA damage response [GO:0006974]; maltodextrin transmembrane transport [GO:0042956]; maltose transport [GO:0015768] | ATP-binding cassette (ABC) transporter complex [GO:0043190]; ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing [GO:0055052]; maltose transport complex [GO:1990060]; membrane [GO:0016020]; outer membrane-bounded periplasmic space [GO:0030288]; periplasmic space [GO:0042597] | carbohydrate transmembrane transporter activity [GO:0015144]; maltose binding [GO:1901982] | PF01547; | 3.40.190.10; | Bacterial solute-binding protein 1 family | null | SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:4215651}. | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.9 uM for maltose {ECO:0000269|PubMed:776623}; KM=2 uM for maltotriose {ECO:0000269|PubMed:776623}; | null | null | null | FUNCTION: Part of the ABC transporter complex MalEFGK involved in maltose/maltodextrin import. Binds maltose and higher maltodextrins such as maltotriose. {ECO:0000269|PubMed:2026607, ECO:0000269|PubMed:2155217, ECO:0000269|PubMed:4215651, ECO:0000269|PubMed:776623}. | Escherichia coli (strain K12) |
P0AEY3 | MAZG_ECOLI | MNQIDRLLTIMQRLRDPENGCPWDKEQTFATIAPYTLEETYEVLDAIAREDFDDLRGELGDLLFQVVFYAQMAQEEGRFDFNDICAAISDKLERRHPHVFADSSAENSSEVLARWEQIKTEERAQKAQHSALDDIPRSLPALMRAQKIQKRCANVGFDWTTLGPVVDKVYEEIDEVMYEARQAVVDQAKLEEEMGDLLFATVNLARHLGTKAEIALQKANEKFERRFREVERIVAARGLEMTGVDLETMEEVWQQVKRQEIDL | 3.6.1.8 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; | cellular response to starvation [GO:0009267]; dATP catabolic process [GO:0046061]; dGTP catabolic process [GO:0006203]; dTTP catabolic process [GO:0046076]; dUTP catabolic process [GO:0046081]; TTP catabolic process [GO:0046047]; UTP catabolic process [GO:0046052] | null | ATP binding [GO:0005524]; ATP diphosphatase activity [GO:0047693]; metal ion binding [GO:0046872]; nucleoside triphosphate diphosphatase activity [GO:0047429] | PF03819; | 1.10.287.1080; | Nucleoside triphosphate pyrophosphohydrolase family | null | null | CATALYTIC ACTIVITY: Reaction=ATP + H2O = AMP + diphosphate + H(+); Xref=Rhea:RHEA:14245, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:456215; EC=3.6.1.8; Evidence={ECO:0000269|PubMed:12218018, ECO:0000269|PubMed:18353782}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.34 mM for dATP (at pH 9.6 and at 37 degrees Celsius in the presence of 5 mM magnesium) {ECO:0000269|PubMed:20529853}; KM=0.71 mM for UTP (at pH 9.6 and at 37 degrees Celsius in the presence of 5 mM magnesium) {ECO:0000269|PubMed:20529853}; KM=0.36 mM for 8-oxo-dG... | null | null | null | FUNCTION: Involved in the regulation of bacterial cell survival under conditions of nutritional stress. Regulates the type II MazE-MazF toxin-antitoxin (TA) system which mediates programmed cell death (PCD). This is achieved by lowering the cellular concentration of (p)ppGpp produced by RelA under amino acid starvation... | Escherichia coli (strain K12) |
P0AEY5 | MDAB_ECOLI | MSNILIINGAKKFAHSNGQLNDTLTEVADGTLRDLGHDVRIVRADSDYDVKAEVQNFLWADVVIWQMPGWWMGAPWTVKKYIDDVFTEGHGTLYASDGRTRKDPSKKYGSGGLVQGKKYMLSLTWNAPMEAFTEKDQFFHGVGVDGVYLPFHKANQFLGMEPLPTFIANDVIKMPDVPRYTEEYRKHLVEIFG | 1.6.5.10 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:8611590}; | null | cytosol [GO:0005829] | flavin adenine dinucleotide binding [GO:0050660]; NADPH dehydrogenase (quinone) activity [GO:0008753] | PF02525; | 3.40.50.360; | Oxidoreductase MdaB family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8611590}. | CATALYTIC ACTIVITY: Reaction=a quinone + H(+) + NADPH = a quinol + NADP(+); Xref=Rhea:RHEA:46164, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:132124; EC=1.6.5.10; Evidence={ECO:0000269|PubMed:8611590}; CATALYTIC ACTIVITY: Reaction=H(+) + menadione + NADPH = menadiol + NADP(+)... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=10.5 uM for NADPH {ECO:0000269|PubMed:8611590}; KM=6 uM for menadione {ECO:0000269|PubMed:8611590}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. {ECO:0000269|PubMed:8611590}; | null | FUNCTION: NADPH-specific quinone reductase (PubMed:8611590). Is most active with quinone derivatives and ferricyanide as electron acceptors (PubMed:8611590). Can use menadione, 1,4-naphthoquinone and 1,4-benzoquinone (PubMed:8611590). May work in concert with YgiN to form a quinone redox cycle (PubMed:15613473). {ECO:0... | Escherichia coli (strain K12) |
P0AEY8 | MDFA_ECOLI | MQNKLASGARLGRQALLFPLCLVLYEFSTYIGNDMIQPGMLAVVEQYQAGIDWVPTSMTAYLAGGMFLQWLLGPLSDRIGRRPVMLAGVVWFIVTCLAILLAQNIEQFTLLRFLQGISLCFIGAVGYAAIQESFEEAVCIKITALMANVALIAPLLGPLVGAAWIHVLPWEGMFVLFAALAAISFFGLQRAMPETATRIGEKLSLKELGRDYKLVLKNGRFVAGALALGFVSLPLLAWIAQSPIIIITGEQLSSYEYGLLQVPIFGALIAGNLLLARLTSRRTVRSLIIMGGWPIMIGLLVAAAATVISSHAYLWMTAGL... | null | null | regulation of cellular pH [GO:0030641]; response to antibiotic [GO:0046677]; xenobiotic detoxification by transmembrane export across the plasma membrane [GO:1990961] | plasma membrane [GO:0005886] | potassium:proton antiporter activity [GO:0015386]; sodium:proton antiporter activity [GO:0015385] | PF07690; | 1.20.1720.10; | Major facilitator superfamily, MdfA family | null | SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5. {ECO:0000269|PubMed:9644262}; | null | FUNCTION: Efflux pump driven by the proton motive force. Confers resistance to a broad spectrum of chemically unrelated drugs. Confers resistance to a diverse group of cationic or zwitterionic lipophilic compounds such as ethidium bromide, tetraphenylphosphonium, rhodamine, daunomycin, benzalkonium, rifampicin, tetracy... | Escherichia coli (strain K12) |
P0AEZ1 | METF_ECOLI | MSFFHASQRDALNQSLAEVQGQINVSFEFFPPRTSEMEQTLWNSIDRLSSLKPKFVSVTYGANSGERDRTHSIIKGIKDRTGLEAAPHLTCIDATPDELRTIARDYWNNGIRHIVALRGDLPPGSGKPEMYASDLVTLLKEVADFDISVAAYPEVHPEAKSAQADLLNLKRKVDAGANRAITQFFFDVESYLRFRDRCVSAGIDVEIIPGILPVSNFKQAKKFADMTNVRIPAWMAQMFDGLDDDAETRKLVGANIAMDMVKILSREGVKDFHFYTLNRAEMSYAICHTLGVRPGL | 1.5.1.54 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:10201405, ECO:0000269|PubMed:11371182, ECO:0000269|PubMed:14275142, ECO:0000269|PubMed:16114881, ECO:0000269|PubMed:16605249, ECO:0000269|PubMed:19610625, ECO:0000269|PubMed:9922232}; | methionine biosynthetic process [GO:0009086]; tetrahydrofolate interconversion [GO:0035999] | cytosol [GO:0005829]; protein-containing complex [GO:0032991] | FAD binding [GO:0071949]; methylenetetrahydrofolate reductase (NAD(P)H) activity [GO:0004489]; methylenetetrahydrofolate reductase NADH activity [GO:0106312]; protein-folding chaperone binding [GO:0051087] | PF02219; | 3.20.20.220; | Methylenetetrahydrofolate reductase family | null | null | CATALYTIC ACTIVITY: Reaction=(6S)-5-methyl-5,6,7,8-tetrahydrofolate + NAD(+) = (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + H(+) + NADH; Xref=Rhea:RHEA:19821, ChEBI:CHEBI:15378, ChEBI:CHEBI:15636, ChEBI:CHEBI:18608, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.5.1.54; Evidence={ECO:0000269|PubMed:11371182, ECO:0000269|... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=13 uM for NADH (at pH 7.2 and 15 degrees Celsius) {ECO:0000269|PubMed:9922232}; KM=0.8 uM for (6R)-5,10-methylenetetrahydrofolate (at pH 7.2 and 15 degrees Celsius) {ECO:0000269|PubMed:9922232}; KM=17 uM for NADH (at pH 7.2 and 15 degrees Celsius) {ECO:0000269|PubM... | PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.; PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway. {ECO:0000305|PubMed:14275142}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.3-6.4. {ECO:0000269|PubMed:14275142}; | null | FUNCTION: Catalyzes the NADH-dependent reduction of 5,10-methylenetetrahydrofolate to 5-methyltetrahydrofolate (PubMed:9922232). Is required to provide the methyl group necessary for methionine synthetase to convert homocysteine to methionine; the methyl group is given by 5-methyltetrahydrofolate. Can also use NADPH as... | Escherichia coli (strain K12) |
P0AEZ3 | MIND_ECOLI | MARIIVVTSGKGGVGKTTSSAAIATGLAQKGKKTVVIDFDIGLRNLDLIMGCERRVVYDFVNVIQGDATLNQALIKDKRTENLYILPASQTRDKDALTREGVAKVLDDLKAMDFEFIVCDSPAGIETGALMALYFADEAIITTNPEVSSVRDSDRILGILASKSRRAENGEEPIKEHLLLTRYNPGRVSRGDMLSMEDVLEILRIKLVGVIPEDQSVLRASNQGEPVILDINADAGKAYADTVERLLGEERPFRFIEEEKKGFLKRLFGG | null | null | cell division [GO:0051301]; chromosome segregation [GO:0007059]; division septum assembly [GO:0000917]; negative regulation of cell division [GO:0051782] | cell pole [GO:0060187]; cytoplasmic side of plasma membrane [GO:0009898]; cytosol [GO:0005829]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; identical protein binding [GO:0042802] | PF01656; | 3.40.50.300; | ParA family, MinD subfamily | null | SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. | null | null | null | null | null | FUNCTION: ATPase required for the correct placement of the division site. Cell division inhibitors MinC and MinD act in concert to form an inhibitor capable of blocking formation of the polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they matu... | Escherichia coli (strain K12) |
P0AF06 | MOTB_ECOLI | MKNQAHPIIVVKRRKAKSHGAAHGSWKIAYADFMTAMMAFFLVMWLISISSPKELIQIAEYFRTPLATAVTGGDRISNSESPIPGGGDDYTQSQGEVNKQPNIEELKKRMEQSRLRKLRGDLDQLIESDPKLRALRPHLKIDLVQEGLRIQIIDSQNRPMFRTGSADVEPYMRDILRAIAPVLNGIPNRISLSGHTDDFPYASGEKGYSNWELSADRANASRRELMVGGLDSGKVLRVVGMAATMRLSDRGPDDAVNRRISLLVLNKQAEQAILHENAESQNEPVSALEKPEVAPQVSVPTMPSAEPR | null | null | bacterial-type flagellum-dependent cell motility [GO:0071973]; chemotaxis [GO:0006935]; proton transmembrane transport [GO:1902600] | bacterial-type flagellum [GO:0009288]; bacterial-type flagellum stator complex [GO:0120101]; plasma membrane [GO:0005886] | proton channel activity [GO:0015252] | PF13677;PF00691; | 3.30.1330.60; | MotB family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:2447650}; Single-pass type II membrane protein {ECO:0000269|PubMed:2447650}. Note=The OmpA-like domain probably functions to anchor the complex to the cell wall. | null | null | null | null | null | FUNCTION: MotA and MotB comprise the stator element of the flagellar motor complex. Required for the rotation of the flagellar motor. Probably a linker that fastens the torque-generating machinery to the cell wall. Overexpression of this protein with MotA improves motility in a pdeH disruption, (a c-di-GMP phosphodiest... | Escherichia coli (strain K12) |
P0AF12 | MTNN_ECOLI | MKIGIIGAMEEEVTLLRDKIENRQTISLGGCEIYTGQLNGTEVALLKSGIGKVAAALGATLLLEHCKPDVIINTGSAGGLAPTLKVGDIVVSDEARYHDADVTAFGYEYGQLPGCPAGFKADDKLIAAAEACIAELNLNAVRGLIVSGDAFINGSVGLAKIRHNFPQAIAVEMEATAIAHVCHNFNVPFVVVRAISDVADQQSHLSFDEFLAVAAKQSSLMVESLVQKLAHG | 3.2.2.9 | null | L-methionine salvage from methylthioadenosine [GO:0019509]; L-methionine salvage from S-adenosylmethionine [GO:0019284]; purine deoxyribonucleoside catabolic process [GO:0046124]; toxic metabolite repair [GO:0110052] | cytosol [GO:0005829] | adenosylhomocysteine nucleosidase activity [GO:0008782]; identical protein binding [GO:0042802]; methylthioadenosine nucleosidase activity [GO:0008930]; protein homodimerization activity [GO:0042803] | PF01048; | 3.40.50.1580; | PNP/UDP phosphorylase family, MtnN subfamily | null | null | CATALYTIC ACTIVITY: Reaction=H2O + S-adenosyl-L-homocysteine = adenine + S-(5-deoxy-D-ribos-5-yl)-L-homocysteine; Xref=Rhea:RHEA:17805, ChEBI:CHEBI:15377, ChEBI:CHEBI:16708, ChEBI:CHEBI:57856, ChEBI:CHEBI:58195; EC=3.2.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_01684, ECO:0000269|PubMed:16101288, ECO:0000269|PubMed:39119... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.4 uM for 5'-methylthioadenosine (at pH 7 and 37 degrees Celsius) {ECO:0000269|PubMed:3911944}; KM=0.8 uM for 5'-methylthioadenosine (at pH 7 and 22 degrees Celsius) {ECO:0000269|PubMed:16101288}; KM=4.3 uM for S-adenosylhomocysteine (at pH 7 and 37 degrees Celsiu... | PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-thioadenosine (hydrolase route): step 1/2. {ECO:0000255|HAMAP-Rule:MF_01684}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Exhibits activity across a broad pH range. Enzyme activity is moderately improved under acidic conditions. {ECO:0000269|PubMed:8941345}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37-45 degrees Celsius. Rapidly inactivated after exposure for 10 minutes at 55 degrees Celsius. {ECO:0000269|PubMed:8941345}; | FUNCTION: Catalyzes the irreversible cleavage of the glycosidic bond in both 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH/AdoHcy) to adenine and the corresponding thioribose, 5'-methylthioribose and S-ribosylhomocysteine, respectively (PubMed:16101288, PubMed:3911944). Also cleaves 5'-deoxyadenosine, a ... | Escherichia coli (strain K12) |
P0AF16 | MURJ_ECOLI | MNLLKSLAAVSSMTMFSRVLGFARDAIVARIFGAGMATDAFFVAFKLPNLLRRIFAEGAFSQAFVPILAEYKSKQGEDATRVFVSYVSGLLTLALAVVTVAGMLAAPWVIMVTAPGFADTADKFALTSQLLKITFPYILLISLASLVGAILNTWNRFSIPAFAPTLLNISMIGFALFAAPYFNPPVLALAWAVTVGGVLQLVYQLPHLKKIGMLVLPRINFHDAGAMRVVKQMGPAILGVSVSQISLIINTIFASFLASGSVSWMYYADRLMEFPSGVLGVALGTILLPSLSKSFASGNHDEYNRLMDWGLRLCFLLALP... | null | null | cell wall organization [GO:0071555]; glycolipid translocation [GO:0034203]; lipid translocation [GO:0034204]; lipid-linked peptidoglycan transport [GO:0015836]; peptidoglycan biosynthetic process [GO:0009252]; regulation of cell shape [GO:0008360] | division septum [GO:0000935]; plasma membrane [GO:0005886] | cardiolipin binding [GO:1901612]; lipid-linked peptidoglycan transporter activity [GO:0015648] | PF03023; | null | MurJ/MviN family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_02078, ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:23935042}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_02078, ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:23935042}. | null | null | PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. {ECO:0000255|HAMAP-Rule:MF_02078, ECO:0000269|PubMed:25013077}. | null | null | FUNCTION: Involved in peptidoglycan biosynthesis. Transports lipid-linked peptidoglycan precursors from the inner to the outer leaflet of the cytoplasmic membrane. {ECO:0000255|HAMAP-Rule:MF_02078, ECO:0000269|PubMed:18708495, ECO:0000269|PubMed:18832143, ECO:0000269|PubMed:25013077}. | Escherichia coli (strain K12) |
P0AF18 | NAGA_ECOLI | MYALTQGRIFTGHEFLDDHAVVIADGLIKSVCPVAELPPEIEQRSLNGAILSPGFIDVQLNGCGGVQFNDTAEAVSVETLEIMQKANEKSGCTNYLPTLITTSDELMKQGVRVMREYLAKHPNQALGLHLEGPWLNLVKKGTHNPNFVRKPDAALVDFLCENADVITKVTLAPEMVPAEVISKLANAGIVVSAGHSNATLKEAKAGFRAGITFATHLYNAMPYITGREPGLAGAILDEADIYCGIIADGLHVDYANIRNAKRLKGDKLCLVTDATAPAGANIEQFIFAGKTIYYRNGLCVDENGTLSGSSLTMIEGVRNL... | 3.5.1.25 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:16630633, ECO:0000269|PubMed:17567047, ECO:0000269|PubMed:17567048}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000269|PubMed:16630633, ECO:0000269|PubMed:17567047, ECO:0000269|PubMed:17567048}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evi... | N-acetylglucosamine catabolic process [GO:0006046]; N-acetylneuraminate catabolic process [GO:0019262]; protein homotetramerization [GO:0051289] | protein-containing complex [GO:0032991] | identical protein binding [GO:0042802]; N-acetylgalactosamine-6-phosphate deacetylase activity [GO:0047419]; N-acetylglucosamine-6-phosphate deacetylase activity [GO:0008448]; zinc ion binding [GO:0008270] | PF01979; | 3.20.20.140;2.30.40.10; | Metallo-dependent hydrolases superfamily, NagA family | null | null | CATALYTIC ACTIVITY: Reaction=H2O + N-acetyl-D-glucosamine 6-phosphate = acetate + D-glucosamine 6-phosphate; Xref=Rhea:RHEA:22936, ChEBI:CHEBI:15377, ChEBI:CHEBI:30089, ChEBI:CHEBI:57513, ChEBI:CHEBI:58725; EC=3.5.1.25; Evidence={ECO:0000269|PubMed:16630633, ECO:0000269|PubMed:17567047, ECO:0000269|PubMed:17567048, ECO... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.3 mM for N-acetyl-glucosamine 6-phosphate (at 30 degrees Celsius and pH 7.5) {ECO:0000269|PubMed:17567047, ECO:0000269|PubMed:4861885, ECO:0000269|PubMed:9143339}; KM=0.8 mM for N-acetyl-glucosamine 6-phosphate (at 37 degrees Celsius and pH 8.0) {ECO:0000269|PubM... | PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation; D-fructose 6-phosphate from N-acetylneuraminate: step 4/5. {ECO:0000305|PubMed:2190615}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5. {ECO:0000269|PubMed:17567047, ECO:0000269|PubMed:4861885, ECO:0000269|PubMed:9143339}; | null | FUNCTION: Involved in the first step in the biosynthesis of amino-sugar-nucleotides. Catalyzes the hydrolysis of the N-acetyl group of N-acetylglucosamine-6-phosphate (GlcNAc-6-P) to yield glucosamine 6-phosphate and acetate. In vitro, can also hydrolyze substrate analogs such as N-thioacetyl-D-glucosamine-6-phosphate,... | Escherichia coli (strain K12) |
P0AF24 | NAGD_ECOLI | MTIKNVICDIDGVLMHDNVAVPGAAEFLHGIMDKGLPLVLLTNYPSQTGQDLANRFATAGVDVPDSVFYTSAMATADFLRRQEGKKAYVVGEGALIHELYKAGFTITDVNPDFVIVGETRSYNWDMMHKAAYFVANGARFIATNPDTHGRGFYPACGALCAGIEKISGRKPFYVGKPSPWIIRAALNKMQAHSEETVIVGDNLRTDILAGFQAGLETILVLSGVSSLDDIDSMPFRPSWIYPSVAEIDVI | 3.1.3.5 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:16430214, ECO:0000269|PubMed:16990279}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:16430214, ECO:0000269|PubMed:16990279}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000269|PubMed:16430214, ECO:0000269|PubMed:169... | UMP catabolic process [GO:0046050] | cytosol [GO:0005829] | 5'-nucleotidase activity [GO:0008253]; alkaline phosphatase activity [GO:0004035]; magnesium ion binding [GO:0000287]; phosphatase activity [GO:0016791]; phosphoglycolate phosphatase activity [GO:0008967]; XMP 5'-nucleosidase activity [GO:0106411] | PF13344;PF13242; | 3.40.50.1000; | HAD-like hydrolase superfamily, NagD family | null | null | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + phosphate; Xref=Rhea:RHEA:12484, ChEBI:CHEBI:15377, ChEBI:CHEBI:18254, ChEBI:CHEBI:43474, ChEBI:CHEBI:58043; EC=3.1.3.5; Evidence={ECO:0000269|PubMed:16430214}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=160 uM for UMP (at pH 7 and at 25 degrees Celsius) {ECO:0000269|PubMed:16430214}; KM=400 uM for GMP (at pH 7 and at 25 degrees Celsius) {ECO:0000269|PubMed:16430214}; KM=840 uM for AMP (at pH 7 and at 25 degrees Celsius) {ECO:0000269|PubMed:16430214}; KM=840 uM for... | null | null | null | FUNCTION: Catalyzes the dephosphorylation of an unusually broad range of substrate including deoxyribo- and ribonucleoside tri-, di-, and monophosphates, as well as polyphosphate and glucose-1-P (Glu1P). {ECO:0000269|PubMed:16430214, ECO:0000269|PubMed:16990279}. | Escherichia coli (strain K12) |
P0AF28 | NARL_ECOLI | MSNQEPATILLIDDHPMLRTGVKQLISMAPDITVVGEASNGEQGIELAESLDPDLILLDLNMPGMNGLETLDKLREKSLSGRIVVFSVSNHEEDVVTALKRGADGYLLKDMEPEDLLKALHQAAAGEMVLSEALTPVLAASLRANRATTERDVNQLTPRERDILKLIAQGLPNKMIARRLDITESTVKVHVKHMLKKMKLKSRVEAAVWVHQERIF | null | null | nitrate assimilation [GO:0042128]; phosphorelay signal transduction system [GO:0000160]; regulation of DNA-templated transcription [GO:0006355] | cytosol [GO:0005829]; protein-DNA complex [GO:0032993] | ATP binding [GO:0005524]; DNA binding [GO:0003677]; DNA-binding transcription repressor activity [GO:0001217]; identical protein binding [GO:0042802]; transcription cis-regulatory region binding [GO:0000976] | PF00196;PF00072; | 3.40.50.2300;1.10.10.10; | null | null | null | null | null | null | null | null | FUNCTION: This protein activates the expression of the nitrate reductase (narGHJI) and formate dehydrogenase-N (fdnGHI) operons and represses the transcription of the fumarate reductase (frdABCD) operon in response to a nitrate/nitrite induction signal transmitted by either the NarX or NarQ proteins. | Escherichia coli (strain K12) |
P0AF32 | NARV_ECOLI | MIQYLNVFFYDIYPYICATVFFLGSWLRYDYGQYTWRASSSQMLDKRGMVIWSNLFHIGILGIFFGHLFGMLTPHWMYAWFLPVAAKQLMAMVLGGICGVLTLIGGAGLLWRRLTNQRVRATSTTPDIIIMSILLIQCLLGLSTIPFSAQYPDGSEMMKLVGWAQSIVTFRGGSSEMLNGVAFVFRLHLVLGMTIFLLFPFTRLVHVWSAPFEYFTRRYQIVRSRR | 1.7.5.1 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250}; Note=Binds 2 heme groups per subunit. Heme 1 is located at the cytoplasmic interface, heme 2 is located at the periplasmic interface. Electrons are transferred from the periplasmic to the cytoplasmic heme. {ECO:0000250}; | anaerobic electron transport chain [GO:0019645]; anaerobic respiration [GO:0009061]; nitrate assimilation [GO:0042128]; nitrate metabolic process [GO:0042126] | membrane [GO:0016020]; nitrate reductase complex [GO:0009325]; plasma membrane [GO:0005886] | electron transfer activity [GO:0009055]; heme binding [GO:0020037]; metal ion binding [GO:0046872]; nitrate reductase activity [GO:0008940] | PF02665; | 1.20.950.20; | null | null | SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. | CATALYTIC ACTIVITY: Reaction=a quinol + nitrate = a quinone + H2O + nitrite; Xref=Rhea:RHEA:56144, ChEBI:CHEBI:15377, ChEBI:CHEBI:16301, ChEBI:CHEBI:17632, ChEBI:CHEBI:24646, ChEBI:CHEBI:132124; EC=1.7.5.1; | null | null | null | null | FUNCTION: This is a second nitrate reductase enzyme which can substitute for the NRA enzyme and allows E.coli to use nitrate as an electron acceptor during anaerobic growth. The gamma chain is a membrane-embedded heme-iron unit resembling cytochrome b, which transfers electrons from quinones to the beta subunit. | Escherichia coli (strain K12) |
P0AF36 | ZAPB_ECOLI | MTMSLEVFEKLEAKVQQAIDTITLLQMEIEELKEKNNSLSQEVQNAQHQREELERENNHLKEQQNGWQERLQALLGRMEEV | null | null | division septum assembly [GO:0000917]; FtsZ-dependent cytokinesis [GO:0043093] | cell division site [GO:0032153]; cytosol [GO:0005829] | identical protein binding [GO:0042802] | PF06005; | 1.20.5.340; | ZapB family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18394147}. Note=Localizes to the septum at mid-cell, in a FtsZ-like pattern. | null | null | null | null | null | FUNCTION: Non-essential, abundant cell division factor that is required for proper Z-ring formation. It is recruited early to the divisome by direct interaction with FtsZ, stimulating Z-ring assembly and thereby promoting cell division earlier in the cell cycle. Its recruitment to the Z-ring requires functional FtsA or... | Escherichia coli (strain K12) |
P0AF52 | GHXP_ECOLI | MSTPSARTGGSLDAWFKISQRGSTVRQEVVAGLTTFLAMVYSVIVVPGMLGKAGFPPAAVFVATCLVAGLGSIVMGLWANLPLAIGCAISLTAFTAFSLVLGQHISVPVALGAVFLMGVLFTVISATGIRSWILRNLPHGVAHGTGIGIGLFLLLIAANGVGLVIKNPLDGLPVALGDFATFPVIMSLVGLAVIIGLEKLKVPGGILLTIIGISIVGLIFDPNVHFSGVFAMPSLSDENGNSLIGSLDIMGALNPVVLPSVLALVMTAVFDATGTIRAVAGQANLLDKDGQIIDGGKALTTDSMSSVFSGLVGAAPAAVY... | null | null | guanine import across plasma membrane [GO:0098710]; hypoxanthine transport [GO:0035344] | plasma membrane [GO:0005886] | guanine transmembrane transporter activity [GO:0015208] | PF00860; | null | Nucleobase:cation symporter-2 (NCS2) (TC 2.A.40) family, Azg-like subfamily | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:24214977}; Multi-pass membrane protein {ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:24214977}. | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.6 uM for guanine {ECO:0000269|PubMed:24214977}; KM=11.2 uM for hypoxanthine {ECO:0000269|PubMed:24214977}; Vmax=4 nmol/min/mg enzyme with guanine as substrate {ECO:0000269|PubMed:24214977}; Vmax=2.7 nmol/min/mg enzyme with hypoxanthine as substrate {ECO:0000269|P... | null | null | null | FUNCTION: High-affinity transporter for guanine and hypoxanthine. {ECO:0000269|PubMed:24214977}. | Escherichia coli (strain K12) |
P0AF61 | GHOS_ECOLI | MEGKNKFNTYVVSFDYPSSYSSVFLRLRSLMYDMNFSSIVADEYGIPRQLNENSFAITTSLAASEIEDLIRLKCLDLPDIDFDLNIMTVDDYFRQFYK | 3.1.-.- | null | null | null | RNA endonuclease activity [GO:0004521] | PF11080; | 3.30.70.2360; | null | PTM: Unlike other TA proteinaceous antitoxins, this protein is stable with and without cellular stress; its structure has been determined in the absence of GhoT toxin. {ECO:0000269|PubMed:22941047}. | null | null | null | null | null | null | FUNCTION: Antitoxin component of a type V toxin-antitoxin (TA) system. Neutralizes the toxic effects of toxin GhoT by digesting ghoT transcripts in a sequence-specific manner (PubMed:22941047). In concert with GhoT is involved in reducing cell growth during antibacterial stress (PubMed:24373067). Overexpression leads t... | Escherichia coli (strain K12) |
P0AF67 | TSAE_ECOLI | MMNRVIPLPDEQATLDLGERVAKACDGATVIYLYGDLGAGKTTFSRGFLQALGHQGNVKSPTYTLVEPYTLDNLMVYHFDLYRLADPEELEFMGIRDYFANDAICLVEWPQQGTGVLPDPDVEIHIDYQAQGREARVSAVSSAGELLLARLAG | null | null | maintenance of translational fidelity [GO:1990145]; tRNA threonylcarbamoyladenosine modification [GO:0002949] | cytoplasm [GO:0005737]; EKC/KEOPS complex [GO:0000408] | ADP binding [GO:0043531]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; protein kinase activity [GO:0004672] | PF02367; | 3.40.50.300; | TsaE family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19376873}. | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=169 uM for ATP {ECO:0000269|PubMed:19376873}; Note=kcat is 0.0026 sec(-1) for ATP hydrolysis.; | null | null | null | FUNCTION: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaD and TsaB. TsaE seems... | Escherichia coli (strain K12) |
P0AF90 | RRAB_ECOLI | MANPEQLEEQREETRLIIEELLEDGSDPDALYTIEHHLSADDLETLEKAAVEAFKLGYEVTDPEELEVEDGDIVICCDILSECALNADLIDAQVEQLMTLAEKFDVEYDGWGTYFEDPNGEDGDDEDFVDEDDDGVRH | null | null | mRNA catabolic process [GO:0006402]; regulation of endoribonuclease activity [GO:0060699] | cytosol [GO:0005829] | endoribonuclease inhibitor activity [GO:0060698]; enzyme binding [GO:0019899]; protein homodimerization activity [GO:0042803]; ribonuclease inhibitor activity [GO:0008428] | PF06877; | 3.30.70.970; | RraB family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01888}. | null | null | null | null | null | FUNCTION: Globally modulates RNA abundance by binding to RNase E (Rne) and regulating its endonucleolytic activity. Can modulate Rne action in a substrate-dependent manner by altering the composition of the degradosome. {ECO:0000255|HAMAP-Rule:MF_01888, ECO:0000269|PubMed:16771842, ECO:0000269|PubMed:18510556}. | Escherichia coli (strain K12) |
P0AF93 | RIDA_ECOLI | MSKTIATENAPAAIGPYVQGVDLGNMIITSGQIPVNPKTGEVPADVAAQARQSLDNVKAIVEAAGLKVGDIVKTTVFVKDLNDFATVNATYEAFFTEHNATFPARSCVEVARLPKDVKIEIEAIAVRR | 3.5.99.10 | null | amino acid biosynthetic process [GO:0008652]; isoleucine biosynthetic process [GO:0009097]; organonitrogen compound catabolic process [GO:1901565]; protein homotrimerization [GO:0070207]; response to toxic substance [GO:0009636] | cytosol [GO:0005829]; membrane [GO:0016020]; protein-containing complex [GO:0032991] | 2-iminobutanoate deaminase activity [GO:0120242]; 2-iminopropanoate deaminase activity [GO:0120243]; deaminase activity [GO:0019239]; identical protein binding [GO:0042802]; unfolded protein binding [GO:0051082] | PF01042; | 3.30.1330.40; | RutC family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=2-iminobutanoate + H2O = 2-oxobutanoate + NH4(+); Xref=Rhea:RHEA:39975, ChEBI:CHEBI:15377, ChEBI:CHEBI:16763, ChEBI:CHEBI:28938, ChEBI:CHEBI:76545; EC=3.5.99.10; Evidence={ECO:0000250|UniProtKB:Q7CP78}; CATALYTIC ACTIVITY: Reaction=2-iminopropanoate + H2O = NH4(+) + pyruvate; Xref=Rhea:RHEA... | null | PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-oxobutanoate from L-threonine. {ECO:0000250|UniProtKB:Q7CP78}. | null | null | FUNCTION: Accelerates the release of ammonia from reactive enamine/imine intermediates of the PLP-dependent threonine dehydratase (IlvA) in the low water environment of the cell. It catalyzes the deamination of enamine/imine intermediates to yield 2-ketobutyrate and ammonia. It is required for the detoxification of rea... | Escherichia coli (strain K12) |
P0AFA2 | NARX_ECOLI | MLKRCLSPLTLVNQVALIVLLSTAIGLAGMAVSGWLVQGVQGSAHAINKAGSLRMQSYRLLAAVPLSEKDKPLIKEMEQTAFSAELTRAAERDGQLAQLQGLQDYWRNELIPALMRAQNRETVSADVSQFVAGLDQLVSGFDRTTEMRIETVVLVHRVMAVFMALLLVFTIIWLRARLLQPWRQLLAMASAVSHRDFTQRANISGRNEMAMLGTALNNMSAELAESYAVLEQRVQEKTAGLEHKNQILSFLWQANRRLHSRAPLCERLSPVLNGLQNLTLLRDIELRVYDTDDEENHQEFTCQPDMTCDDKGCQLCPRGV... | 2.7.13.3 | null | cellular response to nitrate [GO:0071249]; cellular response to nitrite [GO:0071250]; DNA damage response [GO:0006974]; nitrate assimilation [GO:0042128]; signal transduction [GO:0007165] | outer membrane-bounded periplasmic space [GO:0030288]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; phosphoprotein phosphatase activity [GO:0004721]; phosphorelay sensor kinase activity [GO:0000155]; protein homodimerization activity [GO:0042803] | PF00672;PF02518;PF07730;PF13675; | 1.20.5.1930;6.10.340.10;1.20.120.960;3.30.565.10; | null | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000269|PubMed:15919996}. | CATALYTIC ACTIVITY: Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.; EC=2.7.13.3; | null | null | null | null | FUNCTION: Acts as a sensor for nitrate/nitrite and transduces signal of nitrate availability to the NarL protein and of both nitrate/nitrite to the NarP protein. NarX probably activates NarL and NarP by phosphorylation in the presence of nitrate. NarX also plays a negative role in controlling NarL activity, probably th... | Escherichia coli (strain K12) |
P0AFA7 | NHAB_ECOLI | MEISWGRALWRNFLGQSPDWYKLALIIFLIVNPLIFLISPFVAGWLLVAEFIFTLAMALKCYPLLPGGLLAIEAVFIGMTSAEHVREEVAANLEVLLLLMFMVAGIYFMKQLLLFIFTRLLLSIRSKMLLSLSFCVAAAFLSAFLDALTVVAVVISVAVGFYGIYHRVASSRTEDTDLQDDSHIDKHYKVVLEQFRGFLRSLMMHAGVGTALGGVMTMVGEPQNLIIAKAAGWHFGDFFLRMSPVTVPVLICGLLTCLLVEKLRWFGYGETLPEKVREVLQQFDDQSRHQRTRQDKIRLIVQAIIGVWLVTALALHLAEV... | null | null | response to lithium ion [GO:0010226] | plasma membrane [GO:0005886] | sodium:proton antiporter activity [GO:0015385] | PF06450; | null | NhaB Na(+)/H(+) (TC 2.A.34) antiporter family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_01599, ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01599}. | CATALYTIC ACTIVITY: Reaction=3 H(+)(out) + 2 Na(+)(in) = 3 H(+)(in) + 2 Na(+)(out); Xref=Rhea:RHEA:29247, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101; Evidence={ECO:0000255|HAMAP-Rule:MF_01599, ECO:0000269|PubMed:7929345}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29248; Evidence={ECO:0000255|HAMAP-Rule:MF_01599, E... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=16.66 mM for Na(+) (at pH 7.2) {ECO:0000269|PubMed:7929345}; KM=3.44 mM for Na(+) (at pH 7.6) {ECO:0000269|PubMed:7929345}; KM=1.53 mM for Na(+) (at pH 8.5) {ECO:0000269|PubMed:7929345}; KM=0.73 mM for Na(+) {ECO:0000269|PubMed:8019504}; KM=0.63 mM for Li(+) {ECO:0... | null | null | null | FUNCTION: Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons (PubMed:1317851, PubMed:7929345, PubMed:8019504, PubMed:8093613). Catalyzes the exchange of 3 H(+) per 2 Na(+) (PubMed:7929345). Can also transport lithium (PubMed:8019504). Essential for regulation of intracellular pH under alkaline ... | Escherichia coli (strain K12) |
P0AFB1 | NLPI_ECOLI | MKPFLRWCFVATALTLAGCSNTSWRKSEVLAVPLQPTLQQEVILARMEQILASRALTDDERAQLLYERGVLYDSLGLRALARNDFSQALAIRPDMPEVFNYLGIYLTQAGNFDAAYEAFDSVLELDPTYNYAHLNRGIALYYGGRDKLAQDDLLAFYQDDPNDPFRSLWLYLAEQKLDEKQAKEVLKQHFEKSDKEQWGWNIVEFYLGNISEQTLMERLKADATDNTSLAEHLSETNFYLGKYYLSLGDLDSATALFKLAVANNVHNFVEHRYALLELSLLGQDQDDLAESDQQ | null | null | cell cycle [GO:0007049]; cell division [GO:0051301]; peptidoglycan metabolic process [GO:0000270]; receptor-mediated virion attachment to host cell [GO:0046813] | cell outer membrane [GO:0009279]; plasma membrane [GO:0005886] | protein homodimerization activity [GO:0042803]; protein-macromolecule adaptor activity [GO:0030674] | PF13432; | 1.25.40.10; | null | null | SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. | null | null | null | null | null | FUNCTION: May be involved in cell division. May play a role in bacterial septation or regulation of cell wall degradation during cell division. Negatively controls the production of extracellular DNA (eDNA). {ECO:0000269|PubMed:10400590, ECO:0000269|PubMed:20833130}. | Escherichia coli (strain K12) |
P0AFB5 | NTRB_ECOLI | MATGTQPDAGQILNSLINSILLIDDNLAIHYANPAAQQLLAQSSRKLFGTPLPELLSYFSLNIELMQESLEAGQGFTDNEVTLVIDGRSHILSVTAQRMPDGMILLEMAPMDNQRRLSQEQLQHAQQVAARDLVRGLAHEIKNPLGGLRGAAQLLSKALPDPSLLEYTKVIIEQADRLRNLVDRLLGPQLPGTRVTESIHKVAERVVTLVSMELPDNVRLIRDYDPSLPELAHDPDQIEQVLLNIVRNALQALGPEGGEIILRTRTAFQLTLHGERYRLAARIDVEDNGPGIPPHLQDTLFYPMVSGREGGTGLGLSIAR... | 2.7.13.3; 3.1.3.- | null | nitrogen fixation [GO:0009399]; regulation of DNA-templated transcription [GO:0006355]; regulation of nitrogen compound metabolic process [GO:0051171]; signal transduction involved in regulation of gene expression [GO:0023019] | cytoplasm [GO:0005737] | ATP binding [GO:0005524]; identical protein binding [GO:0042802]; phosphoprotein phosphatase activity [GO:0004721]; phosphorelay sensor kinase activity [GO:0000155]; phosphotransferase activity, carboxyl group as acceptor [GO:0016774]; protein histidine kinase activity [GO:0004673]; protein homodimerization activity [G... | PF02518;PF00512;PF00989; | 1.10.287.130;3.30.565.10;3.30.450.20; | null | PTM: Autophosphorylated. {ECO:0000269|PubMed:10074086, ECO:0000269|PubMed:2016302, ECO:0000269|PubMed:2574599}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:15157101}. | CATALYTIC ACTIVITY: Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.; EC=2.7.13.3; Evidence={ECO:0000269|PubMed:10074086, ECO:0000269|PubMed:2574599}; | null | null | null | null | FUNCTION: Member of the two-component regulatory system NtrB/NtrC, which controls expression of the nitrogen-regulated (ntr) genes in response to nitrogen limitation. Under conditions of nitrogen limitation, NtrB autophosphorylates and transfers the phosphoryl group to NtrC. In the presence of nitrogen, acts as a phosp... | Escherichia coli (strain K12) |
P0AFB8 | NTRC_ECOLI | MQRGIVWVVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHSDLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAISHYQEQQQPRNVQLNGPTTDIIGEAPAMQDVFRIIGRLSRSSISVLINGESGTGKELVAHALHRHSPRAKAPFIALNMAAIPKDLIESELFGHEKGAFTGANTIRQGRFEQADGGTLFLDEIGDMPLDVQTRLLRVLADGQFYRVGGYAPVKVDVRIIAATHQNLEQRVQEGKFREDLFHRLNVIRVHLPPLRERREDIPR... | null | null | nitrogen fixation [GO:0009399]; regulation of DNA-templated transcription [GO:0006355]; regulation of nitrogen utilization [GO:0006808] | cytosol [GO:0005829] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; phosphorelay response regulator activity [GO:0000156]; sequence-specific DNA binding [GO:0043565] | PF02954;PF00072;PF00158; | 1.10.8.60;3.40.50.2300;1.10.10.60;3.40.50.300; | null | PTM: Phosphorylated and dephosphorylated by NtrB (PubMed:2574599, PubMed:2874557). Phosphorylation induces strong cooperative binding to DNA (PubMed:1350679). {ECO:0000269|PubMed:1350679, ECO:0000269|PubMed:2574599, ECO:0000269|PubMed:2874557}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | null | null | null | null | null | FUNCTION: Member of the two-component regulatory system NtrB/NtrC, which controls expression of the nitrogen-regulated (ntr) genes in response to nitrogen limitation. Phosphorylated NtrC binds directly to DNA and stimulates the formation of open promoter-sigma54-RNA polymerase complexes (PubMed:1350679, PubMed:2574599,... | Escherichia coli (strain K12) |
P0AFC0 | NUDB_ECOLI | MKDKVYKRPVSILVVIYAQDTKRVLMLQRRDDPDFWQSVTGSVEEGETAPQAAMREVKEEVTIDVVAEQLTLIDCQRTVEFEIFSHLRHRYAPGVTRNTESWFCLALPHERQIVFTEHLAYKWLDAPAAAALTKSWSNRQAIEQFVINAA | 3.6.1.67 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:8798731}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:8798731}; | folic acid biosynthetic process [GO:0046656]; tetrahydrofolate biosynthetic process [GO:0046654] | null | dATP diphosphatase activity [GO:0008828]; dihydroneopterin triphosphate pyrophosphohydrolase activity [GO:0019177]; magnesium ion binding [GO:0000287]; metal ion binding [GO:0046872] | PF00293; | 3.90.79.10; | Nudix hydrolase family | null | null | CATALYTIC ACTIVITY: Reaction=7,8-dihydroneopterin 3'-triphosphate + H2O = 7,8-dihydroneopterin 3'-phosphate + diphosphate + H(+); Xref=Rhea:RHEA:25302, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:58462, ChEBI:CHEBI:58762; EC=3.6.1.67; Evidence={ECO:0000269|PubMed:8798731}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.27 mM for dihydroneopterin triphosphate {ECO:0000269|PubMed:17698004, ECO:0000269|PubMed:8798731}; KM=0.79 mM for dATP {ECO:0000269|PubMed:17698004, ECO:0000269|PubMed:8798731}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5-9. {ECO:0000269|PubMed:17698004, ECO:0000269|PubMed:8798731}; | null | FUNCTION: Catalyzes the hydrolysis of dihydroneopterin triphosphate to dihydroneopterin monophosphate and pyrophosphate. Required for efficient folate biosynthesis. Can also hydrolyze nucleoside triphosphates with a preference for dATP. {ECO:0000269|PubMed:17698004, ECO:0000269|PubMed:8798731}. | Escherichia coli (strain K12) |
P0AFC3 | NUOA_ECOLI | MSMSTSTEVIAHHWAFAIFLIVAIGLCCLMLVGGWFLGGRARARSKNVPFESGIDSVGSARLRLSAKFYLVAMFFVIFDVEALYLFAWSTSIRESGWVGFVEAAIFIFVLLAGLVYLVRIGALDWTPARSRRERMNPETNSIANRQR | 7.1.1.- | null | respiratory electron transport chain [GO:0022904] | membrane [GO:0016020]; NADH dehydrogenase complex [GO:0030964]; plasma membrane [GO:0005886]; plasma membrane respiratory chain complex I [GO:0045272]; respiratory chain complex I [GO:0045271] | NADH dehydrogenase (ubiquinone) activity [GO:0008137]; quinone binding [GO:0048038] | PF00507; | 1.20.58.1610; | Complex I subunit 3 family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_01394, ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01394, ECO:0000269|PubMed:15919996}. | CATALYTIC ACTIVITY: Reaction=a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+); Xref=Rhea:RHEA:57888, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124; Evidence={ECO:0000255|HAMAP-Rule:MF_01394}; | null | null | null | null | FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ... | Escherichia coli (strain K12) |
P0AFC7 | NUOB_ECOLI | MDYTLTRIDPNGENDRYPLQKQEIVTDPLEQEVNKNVFMGKLNDMVNWGRKNSIWPYNFGLSCCYVEMVTSFTAVHDVARFGAEVLRASPRQADLMVVAGTCFTKMAPVIQRLYDQMLEPKWVISMGACANSGGMYDIYSVVQGVDKFIPVDVYIPGCPPRPEAYMQALMLLQESIGKERRPLSWVVGDQGVYRANMQSERERKRGERIAVTNLRTPDEI | 7.1.1.- | COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000255|HAMAP-Rule:MF_01356}; Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255|HAMAP-Rule:MF_01356}; | aerobic respiration [GO:0009060]; electron transport coupled proton transport [GO:0015990]; respiratory electron transport chain [GO:0022904] | membrane [GO:0016020]; NADH dehydrogenase complex [GO:0030964]; plasma membrane [GO:0005886]; plasma membrane respiratory chain complex I [GO:0045272]; respiratory chain complex I [GO:0045271] | 4 iron, 4 sulfur cluster binding [GO:0051539]; iron ion binding [GO:0005506]; NADH dehydrogenase (ubiquinone) activity [GO:0008137]; quinone binding [GO:0048038] | PF01058; | 3.40.50.12280; | Complex I 20 kDa subunit family | null | SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. | CATALYTIC ACTIVITY: Reaction=a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+); Xref=Rhea:RHEA:57888, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124; Evidence={ECO:0000255|HAMAP-Rule:MF_01356}; | null | null | null | null | FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are transl... | Escherichia coli (strain K12) |
P0AFD1 | NUOE_ECOLI | MHENQQPQTEAFELSAAEREAIEHEMHHYEDPRAASIEALKIVQKQRGWVPDGAIHAIADVLGIPASDVEGVATFYSQIFRQPVGRHVIRYCDSVVCHINGYQGIQAALEKKLNIKPGQTTFDGRFTLLPTCCLGNCDKGPNMMIDEDTHAHLTPEAIPELLERYK | 7.1.1.- | COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000305}; Note=Binds 1 [2Fe-2S] cluster. {ECO:0000305}; | respiratory electron transport chain [GO:0022904]; transmembrane transport [GO:0055085] | membrane [GO:0016020]; NADH dehydrogenase complex [GO:0030964]; plasma membrane [GO:0005886]; plasma membrane respiratory chain complex I [GO:0045272]; respiratory chain complex I [GO:0045271] | 2 iron, 2 sulfur cluster binding [GO:0051537]; metal ion binding [GO:0046872]; NADH dehydrogenase activity [GO:0003954]; quinone binding [GO:0048038] | PF01257; | 3.40.30.10;1.10.10.1590; | Complex I 24 kDa subunit family | null | null | CATALYTIC ACTIVITY: Reaction=a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+); Xref=Rhea:RHEA:57888, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124; | null | null | null | null | FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ... | Escherichia coli (strain K12) |
P0AFD4 | NUOH_ECOLI | MSWISPELIEILLTILKAVVILLVVVTCGAFMSFGERRLLGLFQNRYGPNRVGWGGSLQLVADMIKMFFKEDWIPKFSDRVIFTLAPMIAFTSLLLAFAIVPVSPGWVVADLNIGILFFLMMAGLAVYAVLFAGWSSNNKYSLLGAMRASAQTLSYEVFLGLSLMGVVAQAGSFNMTDIVNSQAHVWNVIPQFFGFITFAIAGVAVCHRHPFDQPEAEQELADGYHIEYSGMKFGLFFVGEYIGIVTISALMVTLFFGGWQGPLLPPFIWFALKTAFFMMMFILIRASLPRPRYDQVMSFGWKICLPLTLINLLVTAAVI... | 7.1.1.- | null | aerobic respiration [GO:0009060]; respiratory electron transport chain [GO:0022904]; transmembrane transport [GO:0055085] | membrane [GO:0016020]; NADH dehydrogenase complex [GO:0030964]; plasma membrane [GO:0005886]; plasma membrane respiratory chain complex I [GO:0045272]; respiratory chain complex I [GO:0045271] | NADH dehydrogenase activity [GO:0003954]; oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor [GO:0016655]; quinone binding [GO:0048038] | PF00146; | null | Complex I subunit 1 family | null | SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. | CATALYTIC ACTIVITY: Reaction=a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+); Xref=Rhea:RHEA:57888, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124; | null | null | null | null | FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ... | Escherichia coli (strain K12) |
P0AFD6 | NUOI_ECOLI | MTLKELLVGFGTQVRSIWMIGLHAFAKRETRMYPEEPVYLPPRYRGRIVLTRDPDGEERCVACNLCAVACPVGCISLQKAETKDGRWYPEFFRINFSRCIFCGLCEEACPTTAIQLTPDFEMGEYKRQDLVYEKEDLLISGPGKYPEYNFYRMAGMAIDGKDKGEAENEAKPIDVKSLLP | 7.1.1.- | COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250}; Note=Binds 2 [4Fe-4S] clusters per subunit. {ECO:0000250}; | aerobic respiration [GO:0009060]; respiratory electron transport chain [GO:0022904] | membrane [GO:0016020]; NADH dehydrogenase complex [GO:0030964]; plasma membrane [GO:0005886]; plasma membrane respiratory chain complex I [GO:0045272]; respiratory chain complex I [GO:0045271] | 4 iron, 4 sulfur cluster binding [GO:0051539]; iron ion binding [GO:0005506]; NADH dehydrogenase (quinone) activity [GO:0050136]; quinone binding [GO:0048038] | PF12838; | 3.30.70.3270; | Complex I 23 kDa subunit family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+); Xref=Rhea:RHEA:57888, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124; | null | null | null | null | FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ... | Escherichia coli (strain K12) |
P0AFE0 | NUOJ_ECOLI | MEFAFYICGLIAILATLRVITHTNPVHALLYLIISLLAISGVFFSLGAYFAGALEIIVYAGAIMVLFVFVVMMLNLGGSEIEQERQWLKPQVWIGPAILSAIMLVVIVYAILGVNDQGIDGTPISAKAVGITLFGPYVLAVELASMLLLAGLVVAFHVGREERAGEVLSNRKDDSAKRKTEEHA | 7.1.1.- | null | respiratory electron transport chain [GO:0022904] | membrane [GO:0016020]; NADH dehydrogenase complex [GO:0030964]; plasma membrane [GO:0005886]; plasma membrane respiratory chain complex I [GO:0045272]; respiratory chain complex I [GO:0045271] | NADH dehydrogenase (ubiquinone) activity [GO:0008137]; quinone binding [GO:0048038] | PF00499; | 1.20.120.1200; | Complex I subunit 6 family | null | SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. | CATALYTIC ACTIVITY: Reaction=a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+); Xref=Rhea:RHEA:57888, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124; | null | null | null | null | FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ... | Escherichia coli (strain K12) |
P0AFE4 | NUOK_ECOLI | MIPLQHGLILAAILFVLGLTGLVIRRNLLFMLIGLEIMINASALAFVVAGSYWGQTDGQVMYILAISLAAAEASIGLALLLQLHRRRQNLNIDSVSEMRG | 7.1.1.- | null | ATP synthesis coupled electron transport [GO:0042773]; respiratory electron transport chain [GO:0022904] | membrane [GO:0016020]; NADH dehydrogenase complex [GO:0030964]; plasma membrane [GO:0005886]; plasma membrane respiratory chain complex I [GO:0045272]; respiratory chain complex I [GO:0045271] | NADH dehydrogenase (ubiquinone) activity [GO:0008137]; quinone binding [GO:0048038] | PF00420; | 1.10.287.3510; | Complex I subunit 4L family | null | SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. | CATALYTIC ACTIVITY: Reaction=a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+); Xref=Rhea:RHEA:57888, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124; Evidence={ECO:0000255|HAMAP-Rule:MF_01456}; | null | null | null | null | FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ... | Escherichia coli (strain K12) |
P0AFE8 | NUOM_ECOLI | MLLPWLILIPFIGGFLCWQTERFGVKVPRWIALITMGLTLALSLQLWLQGGYSLTQSAGIPQWQSEFDMPWIPRFGISIHLAIDGLSLLMVVLTGLLGVLAVLCSWKEIEKYQGFFHLNLMWILGGVIGVFLAIDMFLFFFFWEMMLVPMYFLIALWGHKASDGKTRITAATKFFIYTQASGLVMLIAILALVFVHYNATGVWTFNYEELLNTPMSSGVEYLLMLGFFIAFAVKMPVVPLHGWLPDAHSQAPTAGSVDLAGILLKTAAYGLLRFSLPLFPNASAEFAPIAMWLGVIGIFYGAWMAFAQTDIKRLIAYTSV... | 7.1.1.- | null | aerobic respiration [GO:0009060]; ATP synthesis coupled electron transport [GO:0042773]; electron transport coupled proton transport [GO:0015990]; respiratory electron transport chain [GO:0022904] | membrane [GO:0016020]; NADH dehydrogenase complex [GO:0030964]; plasma membrane [GO:0005886]; plasma membrane respiratory chain complex I [GO:0045272]; respiratory chain complex I [GO:0045271] | NADH dehydrogenase (ubiquinone) activity [GO:0008137]; ubiquinone binding [GO:0048039] | PF00361; | null | Complex I subunit 4 family | null | SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. | CATALYTIC ACTIVITY: Reaction=a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+); Xref=Rhea:RHEA:57888, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124; | null | null | null | null | FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ... | Escherichia coli (strain K12) |
P0AFF0 | NUON_ECOLI | MTITPQNLIALLPLLIVGLTVVVVMLSIAWRRNHFLNATLSVIGLNAALVSLWFVGQAGAMDVTPLMRVDGFAMLYTGLVLLASLATCTFAYPWLEGYNDNKDEFYLLVLIAALGGILLANANHLASLFLGIELISLPLFGLVGYAFRQKRSLEASIKYTILSAAASSFLLFGMALVYAQSGDLSFVALGKNLGDGMLNEPLLLAGFGLMIVGLGFKLSLVPFHLWTPDVYQGAPAPVSTFLATASKIAIFGVVMRLFLYAPVGDSEAIRVVLAIIAFASIIFGNLMALSQTNIKRLLGYSSISHLGYLLVALIALQTGE... | 7.1.1.- | null | aerobic respiration [GO:0009060]; ATP synthesis coupled electron transport [GO:0042773]; electron transport coupled proton transport [GO:0015990]; respiratory electron transport chain [GO:0022904] | membrane [GO:0016020]; NADH dehydrogenase complex [GO:0030964]; plasma membrane [GO:0005886]; plasma membrane respiratory chain complex I [GO:0045272]; respiratory chain complex I [GO:0045271] | NADH dehydrogenase (ubiquinone) activity [GO:0008137]; quinone binding [GO:0048038] | PF00361; | null | Complex I subunit 2 family | null | SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. | CATALYTIC ACTIVITY: Reaction=a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+); Xref=Rhea:RHEA:57888, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124; Evidence={ECO:0000255|HAMAP-Rule:MF_00445}; | null | null | null | null | FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ... | Escherichia coli (strain K12) |
P0AFF2 | NUPC_ECOLI | MDRVLHFVLALAVVAILALLVSSDRKKIRIRYVIQLLVIEVLLAWFFLNSDVGLGFVKGFSEMFEKLLGFANEGTNFVFGSMNDQGLAFFFLKVLCPIVFISALIGILQHIRVLPVIIRAIGFLLSKVNGMGKLESFNAVSSLILGQSENFIAYKDILGKISRNRMYTMAATAMSTVSMSIVGAYMTMLEPKYVVAALVLNMFSTFIVLSLINPYRVDASEENIQMSNLHEGQSFFEMLGEYILAGFKVAIIVAAMLIGFIALIAALNALFATVTGWFGYSISFQGILGYIFYPIAWVMGVPSSEALQVGSIMATKLVSN... | null | null | nucleoside transmembrane transport [GO:1901642] | plasma membrane [GO:0005886] | cytidine transmembrane transporter activity [GO:0015212]; nucleoside:proton symporter activity [GO:0015506]; uridine transmembrane transporter activity [GO:0015213] | PF07670;PF07662;PF01773; | null | Concentrative nucleoside transporter (CNT) (TC 2.A.41) family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:8022285}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=adenosine(in) + H(+)(in) = adenosine(out) + H(+)(out); Xref=Rhea:RHEA:29987, ChEBI:CHEBI:15378, ChEBI:CHEBI:16335; Evidence={ECO:0000269|PubMed:14668133}; CATALYTIC ACTIVITY: Reaction=H(+)(in) + uridine(in) = H(+)(out) + uridine(out); Xref=Rhea:RHEA:29951, ChEBI:CHEBI:15378, ChEBI:CHEBI:167... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.6 uM for uridine (at pH 5.5) {ECO:0000269|PubMed:14668133}; KM=10 uM for uridine (at pH 6.5) {ECO:0000269|PubMed:14668133}; KM=15 uM for uridine (at pH 7.5) {ECO:0000269|PubMed:14668133}; KM=44 uM for uridine (at pH 8.5) {ECO:0000269|PubMed:14668133}; KM=1.6 uM f... | null | null | null | FUNCTION: Nucleoside transport protein that can transport adenosine, uridine, thymidine, cytidine and deoxycytidine (PubMed:11466294, PubMed:14668133, PubMed:15678184, PubMed:374403). Shows weak activity with inosine and xanthosine (PubMed:11466294, PubMed:14668133). Transport is driven by a proton motive force (PubMed... | Escherichia coli (strain K12) |
P0AFF4 | NUPG_ECOLI | MNLKLQLKILSFLQFCLWGSWLTTLGSYMFVTLKFDGASIGAVYSSLGIAAVFMPALLGIVADKWLSAKWVYAICHTIGAITLFMAAQVTTPEAMFLVILINSFAYMPTLGLINTISYYRLQNAGMDIVTDFPPIRIWGTIGFIMAMWVVSLSGFELSHMQLYIGAALSAILVLFTLTLPHIPVAKQQANQSWTTLLGLDAFALFKNKRMAIFFIFSMLLGAELQITNMFGNTFLHSFDKDPMFASSFIVQHASIIMSISQISETLFILTIPFFLSRYGIKNVMMISIVAWILRFALFAYGDPTPFGTVLLVLSMIVYGC... | null | null | adenosine transport [GO:0032238]; nucleoside transmembrane transport [GO:1901642]; organic substance transport [GO:0071702]; purine nucleoside transmembrane transport [GO:0015860]; pyrimidine nucleoside transport [GO:0015864]; uridine transport [GO:0015862] | plasma membrane [GO:0005886] | cytidine transmembrane transporter activity [GO:0015212]; nucleoside:proton symporter activity [GO:0015506]; pyrimidine nucleoside transmembrane transporter activity [GO:0015214]; uridine transmembrane transporter activity [GO:0015213] | PF03825; | 1.20.1250.20; | Major facilitator superfamily, Nucleoside:H(+) symporter (NHS) (TC 2.A.1.10) family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_02049, ECO:0000269|PubMed:15513740, ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:3311747, ECO:0000269|PubMed:33640454}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_02049, ECO:0000269|PubMed:33640454}. | CATALYTIC ACTIVITY: Reaction=adenosine(in) + H(+)(in) = adenosine(out) + H(+)(out); Xref=Rhea:RHEA:29987, ChEBI:CHEBI:15378, ChEBI:CHEBI:16335; Evidence={ECO:0000269|PubMed:15513740, ECO:0000269|PubMed:374403}; CATALYTIC ACTIVITY: Reaction=H(+)(in) + uridine(in) = H(+)(out) + uridine(out); Xref=Rhea:RHEA:29951, ChEBI:C... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=23.6 uM for uridine {ECO:0000269|PubMed:15513740}; KM=20.6 uM for adenosine {ECO:0000269|PubMed:15513740}; Vmax=67.2 nmol/min/mg enzyme with uridine as substrate {ECO:0000269|PubMed:15513740}; Vmax=56.8 nmol/min/mg enzyme with adenosine as substrate {ECO:0000269|Pu... | null | null | null | FUNCTION: Broad-specificity transporter of purine and pyrimidine nucleosides (PubMed:11466294, PubMed:15513740, PubMed:15678184, PubMed:3311747, PubMed:374403). Can transport adenosine, uridine, thymidine, cytidine, deoxycytidine, guanosine and inosine (PubMed:11466294, PubMed:15513740, PubMed:15678184, PubMed:3311747,... | Escherichia coli (strain K12) |
P0AFF6 | NUSA_ECOLI | MNKEILAVVEAVSNEKALPREKIFEALESALATATKKKYEQEIDVRVQIDRKSGDFDTFRRWLVVDEVTQPTKEITLEAARYEDESLNLGDYVEDQIESVTFDRITTQTAKQVIVQKVREAERAMVVDQFREHEGEIITGVVKKVNRDNISLDLGNNAEAVILREDMLPRENFRPGDRVRGVLYSVRPEARGAQLFVTRSKPEMLIELFRIEVPEIGEEVIEIKAAARDPGSRAKIAVKTNDKRIDPVGACVGMRGARVQAVSTELGGERIDIVLWDDNPAQFVINAMAPADVASIVVDEDKHTMDIAVEAGNLAQAIGR... | null | null | DNA-templated transcription termination [GO:0006353]; protein complex oligomerization [GO:0051259]; regulation of DNA-templated transcription elongation [GO:0032784]; ribosome biogenesis [GO:0042254]; transcription antitermination [GO:0031564] | cytosol [GO:0005829]; transcription elongation factor complex [GO:0008023] | bacterial-type RNA polymerase core enzyme binding [GO:0001000]; DNA-binding transcription factor activity [GO:0003700]; nucleotide binding [GO:0000166]; protein domain specific binding [GO:0019904]; RNA binding [GO:0003723] | PF14520;PF13184;PF08529;PF00575; | 3.30.300.20;1.10.150.20;2.40.50.140;3.30.1480.10; | NusA family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00945, ECO:0000269|PubMed:17272300}. Note=Colocalizes with nucleoids. | null | null | null | null | null | FUNCTION: Part of the processive rRNA transcription and antitermination complex (rrnTAC). The complex forms an RNA-chaperone ring around the RNA exit tunnel of RNA polymerase (RNAP). It supports rapid transcription and antitermination of rRNA operons, cotranscriptional rRNA folding, and annealing of distal rRNA regions... | Escherichia coli (strain K12) |
P0AFG3 | ODO1_ECOLI | MQNSALKAWLDSSYLSGANQSWIEQLYEDFLTDPDSVDANWRSTFQQLPGTGVKPDQFHSQTREYFRRLAKDASRYSSTISDPDTNVKQVKVLQLINAYRFRGHQHANLDPLGLWQQDKVADLDPSFHDLTEADFQETFNVGSFASGKETMKLGELLEALKQTYCGPIGAEYMHITSTEEKRWIQQRIESGRATFNSEEKKRFLSELTAAEGLERYLGAKFPGAKRFSLEGGDALIPMLKEMIRHAGNSGTREVVLGMAHRGRLNVLVNVLGKKPQDLFDEFAGKHKEHLGTGDVKYHMGFSSDFQTDGGLVHLALAFNP... | 1.2.4.2 | COFACTOR: Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; Evidence={ECO:0000305|PubMed:17367808}; | tricarboxylic acid cycle [GO:0006099] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; oxoglutarate dehydrogenase complex [GO:0045252] | identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; nucleotide binding [GO:0000166]; oxoglutarate dehydrogenase (succinyl-transferring) activity [GO:0004591]; thiamine pyrophosphate binding [GO:0030976] | PF16078;PF00676;PF16870;PF02779; | 3.40.50.12470;3.40.50.970;3.40.50.11610;1.10.287.1150; | Alpha-ketoglutarate dehydrogenase family | null | null | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[dihydrolipoyllysine-residue succinyltransferase] = CO2 + N(6)-[(R)-S(8)-succinyldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue succinyltransferase]; Xref=Rhea:RHEA:12188, Rhea:RHEA-COMP:10483, Rhea:RHEA-COMP:10484, ChEBI:CHEBI:15378, C... | null | null | null | null | FUNCTION: E1 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the decarboxylation of 2-oxoglutarate, the first step in the conversion of 2-oxoglutarate to succinyl-CoA and CO(2). {ECO:0000269|PubMed:17367808}. | Escherichia coli (strain K12) |
P0AFG6 | ODO2_ECOLI | MSSVDILVPDLPESVADATVATWHKKPGDAVVRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQILGRLREGNSAGKETSAKSEEKASTPAQRQQASLEEQNNDALSPAIRRLLAEHNLDASAIKGTGVGGRLTREDVEKHLAKAPAKESAPAAAAPAAQPALAARSEKRVPMTRLRKRVAERLLEAKNSTAMLTTFNEVNMKPIMDLRKQYGEAFEKRHGIRLGFMSFYVKAVVEALKRYPEVNASIDGDDVVYHNYFDVSMAVSTPRGLVTPVLRDVDTLGMADIEKKIKELAVKGRDGKLTVEDLTGGN... | 2.3.1.61 | COFACTOR: Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088; Note=Binds 1 lipoyl cofactor covalently.; | L-lysine catabolic process to acetyl-CoA via saccharopine [GO:0033512]; tricarboxylic acid cycle [GO:0006099] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; oxoglutarate dehydrogenase complex [GO:0045252] | dihydrolipoyllysine-residue succinyltransferase activity [GO:0004149]; lipoic acid binding [GO:0031405] | PF00198;PF00364;PF02817; | 2.40.50.100;3.30.559.10;4.10.320.10; | 2-oxoacid dehydrogenase family | null | null | CATALYTIC ACTIVITY: Reaction=N(6)-[(R)-dihydrolipoyl]-L-lysyl-[2-oxoglutarate dehydrogenase complex component E2] + succinyl-CoA = CoA + N(6)-[(R)-S(8)-succinyldihydrolipoyl]-L-lysyl-[2-oxoglutarate dehydrogenase complex component E2]; Xref=Rhea:RHEA:15213, Rhea:RHEA-COMP:10581, Rhea:RHEA-COMP:10582, ChEBI:CHEBI:57287,... | null | PATHWAY: Amino-acid degradation; L-lysine degradation via saccharopine pathway; glutaryl-CoA from L-lysine: step 6/6. | null | null | FUNCTION: E2 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the second step in the conversion of 2-oxoglutarate to succinyl-CoA and CO(2). {ECO:0000305|PubMed:17367808}. | Escherichia coli (strain K12) |
P0AFG8 | ODP1_ECOLI | MSERFPNDVDPIETRDWLQAIESVIREEGVERAQYLIDQLLAEARKGGVNVAAGTGISNYINTIPVEEQPEYPGNLELERRIRSAIRWNAIMTVLRASKKDLELGGHMASFQSSATIYDVCFNHFFRARNEQDGGDLVYFQGHISPGVYARAFLEGRLTQEQLDNFRQEVHGNGLSSYPHPKLMPEFWQFPTVSMGLGPIGAIYQAKFLKYLEHRGLKDTSKQTVYAFLGDGEMDEPESKGAITIATREKLDNLVFVINCNLQRLDGPVTGNGKIINELEGIFEGAGWNVIKVMWGSRWDELLRKDTSGKLIQLMNETVD... | 1.2.4.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; COFACTOR: Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; | pyruvate catabolic process [GO:0042867] | cytosol [GO:0005829]; cytosolic pyruvate dehydrogenase complex [GO:0045250]; membrane [GO:0016020]; pyruvate dehydrogenase complex [GO:0045254] | identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; molecular adaptor activity [GO:0060090]; protein homodimerization activity [GO:0042803]; pyruvate dehydrogenase (acetyl-transferring) activity [GO:0004739]; pyruvate dehydrogenase activity [GO:0004738]; small molecule binding [GO:0036094]; thia... | PF17831;PF00456; | 3.40.50.920;3.40.50.970; | null | null | null | CATALYTIC ACTIVITY: Reaction=H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + pyruvate = CO2 + N(6)-[(R)-S(8)-acetyldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase]; Xref=Rhea:RHEA:19189, Rhea:RHEA-COMP:10480, Rhea:RHEA-COMP:10481, ChEBI:CHEBI:15361, ChEBI:CHEBI:1... | null | null | null | null | FUNCTION: Component of the pyruvate dehydrogenase (PDH) complex, that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). | Escherichia coli (strain K12) |
P0AFI0 | OXC_ECOLI | MSDQLQMTDGMHIIVEALKQNNIDTIYGVVGIPVTDMARHAQAEGIRYIGFRHEQSAGYAAAASGFLTQKPGICLTVSAPGFLNGLTALANATVNGFPMIMISGSSDRAIVDLQQGDYEELDQMNAAKPYAKAAFRVNQPQDLGIALARAIRVSVSGRPGGVYLDLPANVLAATMEKDEALTTIVKVENPSPALLPCPKSVTSAISLLAKAERPLIILGKGAAYSQADEQLREFIESAQIPFLPMSMAKGILEDTHPLSAAAARSFALANADVVMLVGARLNWLLAHGKKGWAADTQFIQLDIEPQEIDSNRPIAVPVVG... | 4.1.1.8 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:20553497}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:20553497}; COFACTOR: Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; Evidence={ECO:0000269|PubMed:20553497}; Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000269|Pu... | cellular response to acidic pH [GO:0071468]; fatty acid alpha-oxidation [GO:0001561]; oxalate catabolic process [GO:0033611] | peroxisome [GO:0005777] | ADP binding [GO:0043531]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; oxalyl-CoA decarboxylase activity [GO:0008949]; thiamine pyrophosphate binding [GO:0030976] | PF02775;PF00205;PF02776; | 3.40.50.970;3.40.50.1220; | TPP enzyme family | null | null | CATALYTIC ACTIVITY: Reaction=H(+) + oxalyl-CoA = CO2 + formyl-CoA; Xref=Rhea:RHEA:19333, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57376, ChEBI:CHEBI:57388; EC=4.1.1.8; Evidence={ECO:0000269|PubMed:20553497}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.17 uM for oxalyl-CoA (with 300 uM ADP at pH 6.5 and 30 degrees Celsius) {ECO:0000269|PubMed:20553497}; KM=4.8 uM for oxalyl-CoA (at pH 6.5 and 30 degrees Celsius) {ECO:0000269|PubMed:20553497}; Note=kcat is 69.7 sec(-1) for decarboxylase activity with oxalyl-CoA ... | PATHWAY: Metabolic intermediate degradation; oxalate degradation; CO(2) and formate from oxalate: step 2/2. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is between 5.5 and 7. {ECO:0000269|PubMed:20553497}; | null | FUNCTION: Involved in the catabolism of oxalate and in the adapatation to low pH via the induction of the oxalate-dependent acid tolerance response (ATR). Catalyzes the decarboxylation of oxalyl-CoA to yield carbon dioxide and formyl-CoA. {ECO:0000269|PubMed:20553497}. | Escherichia coli (strain K12) |
P0AFI2 | PARC_ECOLI | MSDMAERLALHEFTENAYLNYSMYVIMDRALPFIGDGLKPVQRRIVYAMSELGLNASAKFKKSARTVGDVLGKYHPHGDSACYEAMVLMAQPFSYRYPLVDGQGNWGAPDDPKSFAAMRYTESRLSKYSELLLSELGQGTADWVPNFDGTLQEPKMLPARLPNILLNGTTGIAVGMATDIPPHNLREVAQAAIALIDQPKTTLDQLLDIVQGPDYPTEAEIITSRAEIRKIYENGRGSVRMRAVWKKEDGAVVISALPHQVSGARVLEQIAAQMRNKKLPMVDDLRDESDHENPTRLVIVPRSNRVDMDQVMNHLFATTD... | 5.6.2.2 | null | chromosome segregation [GO:0007059]; DNA topological change [GO:0006265]; plasmid partitioning [GO:0030541]; sister chromatid cohesion [GO:0007062] | chromosome [GO:0005694]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex [GO:0009330]; extrinsic component of plasma membrane [GO:0019897] | ATP binding [GO:0005524]; DNA binding [GO:0003677]; DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity [GO:0003918] | PF03989;PF00521; | 3.30.1360.40;2.120.10.90;3.90.199.10;1.10.268.10; | Type II topoisomerase GyrA/ParC subunit family, ParC type 1 subfamily | null | SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. | CATALYTIC ACTIVITY: Reaction=ATP-dependent breakage, passage and rejoining of double-stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000255|HAMAP-Rule:MF_00936, ECO:0000269|PubMed:12269820, ECO:0000269|PubMed:16023670, ECO:0000269|PubMed:21300644}; | null | null | null | null | FUNCTION: Topoisomerase IV is essential for chromosome segregation; it is the principal protein responsible for decatenating newly replicated chromosomes (PubMed:9334322). It relaxes supercoiled DNA (PubMed:12269820, PubMed:16023670, PubMed:21300644). MukB stimulates the relaxation activity of topoisomerase IV and also... | Escherichia coli (strain K12) |
P0AFI5 | PBP7_ECOLI | MPKFRVSLFSLALMLAVPFAPQAVAKTAAATTASQPEIASGSAMIVDLNTNKVIYSNHPDLVRPIASISKLMTAMVVLDARLPLDEKLKVDISQTPEMKGVYSRVRLNSEISRKDMLLLALMSSENRAAASLAHHYPGGYKAFIKAMNAKAKSLGMNNTRFVEPTGLSVHNVSTARDLTKLLIASKQYPLIGQLSTTREDMATFSNPTYTLPFRNTNHLVYRDNWNIQLTKTGFTNAAGHCLVMRTVINNKPVALVVMDAFGKYTHFADASRLRTWIETGKVMPVPAAALSYKKQKAAQMAAAGQTAQND | 3.4.21.- | null | cell wall organization [GO:0071555]; FtsZ-dependent cytokinesis [GO:0043093]; peptidoglycan biosynthetic process [GO:0009252]; peptidoglycan metabolic process [GO:0000270]; proteolysis [GO:0006508]; regulation of cell shape [GO:0008360]; response to xenobiotic stimulus [GO:0009410] | periplasmic space [GO:0042597]; TRAPP complex [GO:0030008] | endopeptidase activity [GO:0004175]; serine-type D-Ala-D-Ala carboxypeptidase activity [GO:0009002] | PF00768; | 3.40.710.10; | Peptidase S11 family | PTM: Pbp8 is a proteolytic product of Pbp7. | SUBCELLULAR LOCATION: Periplasm. | null | null | null | null | null | FUNCTION: Cell wall formation. May play a specialized role in remodeling the cell wall. Specifically hydrolyzes the DD-diaminopimelate-alanine bonds in high-molecular-mass murein sacculi. | Escherichia coli (strain K12) |
P0AFI7 | PDXH_ECOLI | MSDNDELQQIAHLRREYTKGGLRRRDLPADPLTLFERWLSQACEAKLADPTAMVVATVDEHGQPYQRIVLLKHYDEKGMVFYTNLGSRKAHQIENNPRVSLLFPWHTLERQVMVIGKAERLSTLEVMKYFHSRPRDSQIGAWVSKQSSRISARGILESKFLELKQKFQQGEVPLPSFWGGFRVSLEQIEFWQGGEHRLHDRFLYQRENDAWKIDRLAP | 1.4.3.5 | COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:10903950, ECO:0000269|PubMed:11453690, ECO:0000269|PubMed:11786019, ECO:0000269|PubMed:15858270, ECO:0000269|PubMed:7860596, ECO:0000269|PubMed:9693059}; Note=Binds 1 FMN per subunit. {ECO:0000269|PubMed:10903950, ECO:0000269|PubMed:11453690, ECO:... | 'de novo' pyridoxal 5'-phosphate biosynthetic process [GO:0036001]; pyridoxal phosphate biosynthetic process [GO:0042823]; pyridoxine biosynthetic process [GO:0008615] | cytosol [GO:0005829]; protein-containing complex [GO:0032991] | FMN binding [GO:0010181]; oxidoreductase activity [GO:0016491]; phosphate ion binding [GO:0042301]; protein homodimerization activity [GO:0042803]; pyridoxal phosphate binding [GO:0030170]; pyridoxamine phosphate oxidase activity [GO:0004733]; riboflavin binding [GO:1902444] | PF10590;PF01243; | null | Pyridoxamine 5'-phosphate oxidase family | null | null | CATALYTIC ACTIVITY: Reaction=H2O + O2 + pyridoxamine 5'-phosphate = H2O2 + NH4(+) + pyridoxal 5'-phosphate; Xref=Rhea:RHEA:15817, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:58451, ChEBI:CHEBI:597326; EC=1.4.3.5; Evidence={ECO:0000269|PubMed:11786019, ECO:0000269|PubMed:78605... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.3 uM for pyridoxamine 5'-phosphate {ECO:0000269|PubMed:11786019}; KM=2 uM for pyridoxine 5'-phosphate (at pH 7.6 and 37 degrees Celsius) {ECO:0000269|PubMed:7860596, ECO:0000269|PubMed:9693059}; KM=105 uM for pyridoxamine 5'-phosphate (at pH 7.6 and 37 degrees Ce... | PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1.; PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal 5'-phosphate from pyridoxine 5'-phosphate: step 1/1. | null | null | FUNCTION: Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP). {ECO:0000269|PubMed:11786019, ECO:0000269|PubMed:7860596, ECO:0000269|PubMed:9693059}. | Escherichia coli (strain K12) |
P0AFJ7 | PITA_ECOLI | MLHLFAGLDLHTGLLLLLALAFVLFYEAINGFHDTANAVATVIYTRAMRSQLAVVMAAVFNFLGVLLGGLSVAYAIVHMLPTDLLLNMGSSHGLAMVFSMLLAAIIWNLGTWYFGLPASSSHTLIGAIIGIGLTNALMTGTSVVDALNIPKVLSIFGSLIVSPIVGLVFAGGLIFLLRRYWSGTKKRARIHLTPAEREKKDGKKKPPFWTRIALILSAIGVAFSHGANDGQKGIGLVMLVLIGVAPAGFVVNMNATGYEITRTRDAINNVEAYFEQHPALLKQATGADQLVPAPEAGATQPAEFHCHPSNTINALNRLKG... | null | null | magnesium ion homeostasis [GO:0010960]; phosphate ion transmembrane transport [GO:0035435]; tellurite transport [GO:0015710] | plasma membrane [GO:0005886] | inorganic phosphate transmembrane transporter activity [GO:0005315]; solute:proton symporter activity [GO:0015295]; tellurite transmembrane transporter activity [GO:0015654]; zinc ion transmembrane transporter activity [GO:0005385] | PF01384; | null | Inorganic phosphate transporter (PiT) (TC 2.A.20) family, Pit subfamily | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:11489853, ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=H(+)(in) + phosphate(in) = H(+)(out) + phosphate(out); Xref=Rhea:RHEA:29939, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474; Evidence={ECO:0000269|PubMed:328484, ECO:0000269|PubMed:8110778, ECO:0000305|PubMed:6998957}; CATALYTIC ACTIVITY: Reaction=arsenate(in) + H(+)(in) = arsenate(out) + H(+)(out); ... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.9 uM for phosphate {ECO:0000269|PubMed:11489853}; Vmax=58 nmol/min/mg enzyme (at pH 6.6 and 1.8 mM Mg(2+)) {ECO:0000269|PubMed:11489853}; Vmax=39 nmol/min/mg enzyme (at pH 7.0 and 10.0 mM Mg(2+)) {ECO:0000269|PubMed:11489853}; | null | null | null | FUNCTION: Low-affinity inorganic phosphate transporter (PubMed:11489853, PubMed:328484, PubMed:6998957, PubMed:8110778). Mediates proton-driven uptake of soluble neutral metal phosphate (MeHP04) complexes (PubMed:8110778). It can use Mg(2+), Ca(2+), Co(2+) and Mn(2+) (PubMed:8110778). Activity impacts bacterial growth ... | Escherichia coli (strain K12) |
P0AFL3 | PPIA_ECOLI | MFKSTLAAMAAVFALSALSPAAMAAKGDPHVLLTTSAGNIELELDKQKAPVSVQNFVDYVNSGFYNNTTFHRVIPGFMIQGGGFTEQMQQKKPNPPIKNEADNGLRNTRGTIAMARTADKDSATSQFFINVADNAFLDHGQRDFGYAVFGKVVKGMDVADKISQVPTHDVGPYQNVPSKPVVILSAKVLP | 5.2.1.8 | null | protein folding [GO:0006457] | outer membrane-bounded periplasmic space [GO:0030288]; periplasmic space [GO:0042597] | peptidyl-prolyl cis-trans isomerase activity [GO:0003755] | PF00160; | 2.40.100.10; | Cyclophilin-type PPIase family | null | SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:2190212}. | CATALYTIC ACTIVITY: Reaction=[protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833, ChEBI:CHEBI:83834; EC=5.2.1.8; Evidence={ECO:0000269|PubMed:2190212}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16238;... | null | null | null | null | FUNCTION: PPIases accelerate the folding of proteins (Probable). It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (PubMed:2190212). {ECO:0000269|PubMed:2190212, ECO:0000305}. | Escherichia coli (strain K12) |
P0AFL6 | PPX_ECOLI | MPIHDKSPRPQEFAAVDLGSNSFHMVIARVVDGAMQIIGRLKQRVHLADGLGPDNMLSEEAMTRGLNCLSLFAERLQGFSPASVCIVGTHTLRQALNATDFLKRAEKVIPYPIEIISGNEEARLIFMGVEHTQPEKGRKLVIDIGGGSTELVIGENFEPILVESRRMGCVSFAQLYFPGGVINKENFQRARMAAAQKLETLTWQFRIQGWNVAMGASGTIKAAHEVLMEMGEKDGIITPERLEKLVKEVLRHRNFASLSLPGLSEERKTVFVPGLAILCGVFDALAIRELRLSDGALREGVLYEMEGRFRHQDVRSRTAS... | 3.6.1.11 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:8380170}; | polyphosphate catabolic process [GO:0006798] | plasma membrane [GO:0005886] | exopolyphosphatase activity [GO:0004309]; guanosine tetraphosphate binding [GO:0097216]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803] | PF02541;PF21447; | 3.30.420.40;3.30.70.2260;3.30.420.150;1.10.3210.10; | GppA/Ppx family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:8380170}; Peripheral membrane protein {ECO:0000305|PubMed:8380170}. | CATALYTIC ACTIVITY: Reaction=[phosphate](n) + H2O = [phosphate](n-1) + H(+) + phosphate; Xref=Rhea:RHEA:21528, Rhea:RHEA-COMP:9859, Rhea:RHEA-COMP:14279, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16838, ChEBI:CHEBI:43474; EC=3.6.1.11; Evidence={ECO:0000269|PubMed:16905100, ECO:0000269|PubMed:8380170, ECO:000026... | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8. {ECO:0000269|PubMed:8380170}; | null | FUNCTION: Degradation of inorganic polyphosphates (polyP). Releases orthophosphate processively from the ends of the polyP chain. Has a strong preference for long-chain polyphosphates and has only weak affinity for smaller size polyP of about 15 residues. {ECO:0000269|PubMed:16905100, ECO:0000269|PubMed:8380170, ECO:00... | Escherichia coli (strain K12) |
P0AFM2 | PROX_ECOLI | MRHSVLFATAFATLISTQTFAADLPGKGITVNPVQSTITEETFQTLLVSRALEKLGYTVNKPSEVDYNVGYTSLASGDATFTAVNWTPLHDNMYEAAGGDKKFYREGVFVNGAAQGYLIDKKTADQYKITNIAQLKDPKIAKLFDTNGDGKADLTGCNPGWGCEGAINHQLAAYELTNTVTHNQGNYAAMMADTISRYKEGKPVFYYTWTPYWVSNELKPGKDVVWLQVPFSALPGDKNADTKLPNGANYGFPVSTMHIVANKAWAEKNPAAAKLFAIMQLPVADINAQNAIMHDGKASEGDIQGHVDGWIKAHQQQFDG... | null | null | amino acid import across plasma membrane [GO:0089718]; cellular response to osmotic stress [GO:0071470]; glycine betaine transport [GO:0031460]; glycine import across plasma membrane [GO:1903804]; hyperosmotic response [GO:0006972] | membrane [GO:0016020]; outer membrane-bounded periplasmic space [GO:0030288]; ProVWX complex [GO:1990222] | quaternary ammonium group binding [GO:0050997]; transmembrane transporter activity [GO:0022857] | PF04069; | 3.40.190.10; | null | null | SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:3305496, ECO:0000269|PubMed:7898450}. | null | null | null | null | null | FUNCTION: Part of the ProU ABC transporter complex involved in glycine betaine and proline betaine uptake. Binds glycine betaine and proline betaine with high affinity. {ECO:0000269|PubMed:14612446, ECO:0000269|PubMed:23249124, ECO:0000269|PubMed:3305496, ECO:0000269|PubMed:7898450}. | Escherichia coli (strain K12) |
P0AFM6 | PSPA_ECOLI | MGIFSRFADIVNANINALLEKAEDPQKLVRLMIQEMEDTLVEVRSTSARALAEKKQLTRRIEQASAREVEWQEKAELALLKEREDLARAALIEKQKLTDLIKSLEHEVTLVDDTLARMKKEIGELENKLSETRARQQALMLRHQAANSSRDVRRQLDSGKLDEAMARFESFERRIDQMEAEAESHSFGKQKSLDDQFAELKADDAISEQLAQLKAKMKQDNQ | null | null | phage shock [GO:0009271]; regulation of cellular response to stress [GO:0080135]; regulation of DNA-templated transcription [GO:0006355]; response to heat [GO:0009408] | cell pole [GO:0060187]; cytosol [GO:0005829]; plasma membrane [GO:0005886]; transcription regulator complex [GO:0005667] | identical protein binding [GO:0042802]; phospholipid binding [GO:0005543] | PF04012; | null | PspA/Vipp/IM30 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19555453}. Cell inner membrane {ECO:0000269|PubMed:19555453}; Peripheral membrane protein {ECO:0000269|PubMed:19555453}; Cytoplasmic side {ECO:0000269|PubMed:19555453}. Note=Localizes at both cell poles and along the length of the cell. | null | null | null | null | null | FUNCTION: The phage shock protein (psp) operon (pspABCDE) may play a significant role in the competition for survival under nutrient- or energy-limited conditions. PspA negatively regulates expression of the pspABCDE promoter and of pspG through negative regulation of the psp-specific transcriptional activator PspF. Is... | Escherichia coli (strain K12) |
P0AFP6 | GCH1L_ECOLI | MKNTELEQLINEKLNSAAISDYAPNGLQVEGKETVQKIVTGVTASQALLDEAVRLGADAVIVHHGYFWKGESPVIRGMKRNRLKTLLANDINLYGWHLPLDAHPELGNNAQLAALLGITVMGEIEPLVPWGELTMPVPGLELASWIEARLGRKPLWCGDTGPEVVQRVAWCTGGGQSFIDSAARFGVDAFITGEVSEQTIHSAREQGLHFYAAGHHATERGGIRALSEWLNENTDLDVTFIDIPNPA | null | null | DNA repair [GO:0006281]; protein hexamerization [GO:0034214]; response to ionizing radiation [GO:0010212] | cell pole [GO:0060187]; cytoplasm [GO:0005737]; cytosol [GO:0005829] | identical protein binding [GO:0042802]; metal ion binding [GO:0046872] | PF01784; | 3.40.1390.30; | GTP cyclohydrolase I type 2/NIF3 family | null | null | null | null | null | null | null | FUNCTION: Provides significant protection from radiation damage and may be involved in the degradation of radiation-damaged nucleotides. {ECO:0000269|PubMed:25049088}. | Escherichia coli (strain K12) |
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