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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
P0ABP3 | DCUC_ECOLI | MLTFIELLIGVVVIVGVARYIIKGYSATGVLFVGGLLLLIISAIMGHKVLPSSQASTGYSATDIVEYVKILLMSRGGDLGMMIMMLCGFAAYMTHIGANDMVVKLASKPLQYINSPYLLMIAAYFVACLMSLAVSSATGLGVLLMATLFPVMVNVGISRGAAAAICASPAAIILAPTSGDVVLAAQASEMSLIDFAFKTTLPISIAAIIGMAIAHFFWQRYLDKKEHISHEMLDVSEITTTAPAFYAILPFTPIIGVLIFDGKWGPQLHIITILVICMLIASILEFLRSFNTQKVFSGLEVAYRGMADAFANVVMLLVAA... | null | null | C4-dicarboxylate transport [GO:0015740]; mixed acid fermentation [GO:0019664] | plasma membrane [GO:0005886] | succinate:fumarate antiporter activity [GO:0005469]; symporter activity [GO:0015293] | PF03606; | null | DcuC/DcuD transporter (TC 2.A.61) family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=fumarate(in) + succinate(out) = fumarate(out) + succinate(in); Xref=Rhea:RHEA:29323, ChEBI:CHEBI:29806, ChEBI:CHEBI:30031; Evidence={ECO:0000269|PubMed:8955408}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29325; Evidence={ECO:0000269|PubMed:8955408}; CATALYTIC ACTIVITY: Reaction=f... | null | null | null | null | FUNCTION: Responsible for the transport of C4-dicarboxylates during anaerobic growth (PubMed:10368146, PubMed:8955408). Catalyzes the uptake of fumarate coupled to the export of succinate (PubMed:8955408). Can also catalyze the uptake of fumarate and the efflux of succinate, without exchange (PubMed:10368146, PubMed:89... | Escherichia coli (strain K12) |
P0ABP8 | DEOD_ECOLI | MATPHINAEMGDFADVVLMPGDPLRAKYIAETFLEDAREVNNVRGMLGFTGTYKGRKISVMGHGMGIPSCSIYTKELITDFGVKKIIRVGSCGAVLPHVKLRDVVIGMGACTDSKVNRIRFKDHDFAAIADFDMVRNAVDAAKALGIDARVGNLFSADLFYSPDGEMFDVMEKYGILGVEMEAAGIYGVAAEFGAKALTICTVSDHIRTHEQTTAAERQTTFNDMIKIALESVLLGDKE | 2.4.2.1 | null | DNA damage response [GO:0006974]; purine nucleoside catabolic process [GO:0006152]; purine nucleoside interconversion [GO:0019686] | cytosol [GO:0005829]; membrane [GO:0016020] | guanosine phosphorylase activity [GO:0047975]; identical protein binding [GO:0042802]; purine-nucleoside phosphorylase activity [GO:0004731] | PF01048; | 3.40.50.1580; | PNP/UDP phosphorylase family | null | null | CATALYTIC ACTIVITY: Reaction=a purine D-ribonucleoside + phosphate = a purine nucleobase + alpha-D-ribose 1-phosphate; Xref=Rhea:RHEA:19805, ChEBI:CHEBI:26386, ChEBI:CHEBI:43474, ChEBI:CHEBI:57720, ChEBI:CHEBI:142355; EC=2.4.2.1; Evidence={ECO:0000255|HAMAP-Rule:MF_01627}; CATALYTIC ACTIVITY: Reaction=a purine 2'-deoxy... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=230 uM for phosphate (at 25 degrees Celsius and pH 7) {ECO:0000269|PubMed:30337572}; KM=520 uM for phosphate (at 25 degrees Celsius and pH 5.3) {ECO:0000269|PubMed:30337572}; KM=120 uM for phosphate (at pH 7.1) {ECO:0000269|PubMed:235429}; KM=70 uM for inosine (at ... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.1 for deoxyinosine as substrate (PubMed:235429). Optimum pH is 7.5 for inosine as substrate (PubMed:235429). Optimum pH is 8.2 for hypoxanthine as substrate (PubMed:235429). {ECO:0000269|PubMed:235429}; | null | FUNCTION: Catalyzes the reversible phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate (PubMed:11786017, PubMed:21672603, PubMed:235429, PubMed:30337572). Acts on 6-amino and 6-oxopurines includi... | Escherichia coli (strain K12) |
P0ABQ0 | COABC_ECOLI | MSLAGKKIVLGVSGGIAAYKTPELVRRLRDRGADVRVAMTEAAKAFITPLSLQAVSGYPVSDSLLDPAAEAAMGHIELGKWADLVILAPATADLIARVAAGMANDLVSTICLATPAPVAVLPAMNQQMYRAAATQHNLEVLASRGLLIWGPDSGSQACGDIGPGRMLDPLTIVDMAVAHFSPVNDLKHLNIMITAGPTREPLDPVRYISNHSSGKMGFAIAAAAARRGANVTLVSGPVSLPTPPFVKRVDVMTALEMEAAVNASVQQQNIFIGCAAVADYRAATVAPEKIKKQATQGDELTIKMVKNPDIVAGVAALKDH... | 4.1.1.36; 6.3.2.5 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_02225, ECO:0000269|PubMed:11278255}; COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000255|HAMAP-Rule:MF_02225, ECO:0000269|PubMed:10922366, ECO:0000269|PubMed:11278255, ECO:0000269|PubMed:11358972}; Note=Binds 1 FMN per subu... | coenzyme A biosynthetic process [GO:0015937]; pantothenate catabolic process [GO:0015941] | cytosol [GO:0005829]; phosphopantothenoylcysteine decarboxylase complex [GO:0071513] | FMN binding [GO:0010181]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; phosphopantothenate--cysteine ligase activity [GO:0004632]; phosphopantothenoylcysteine decarboxylase activity [GO:0004633] | PF04127;PF02441; | 3.40.50.10300;3.40.50.1950; | HFCD (homo-oligomeric flavin containing Cys decarboxylase) superfamily; PPC synthetase family | null | null | CATALYTIC ACTIVITY: Reaction=H(+) + N-[(R)-4-phosphopantothenoyl]-L-cysteine = (R)-4'-phosphopantetheine + CO2; Xref=Rhea:RHEA:16793, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:59458, ChEBI:CHEBI:61723; EC=4.1.1.36; Evidence={ECO:0000255|HAMAP-Rule:MF_02225, ECO:0000269|PubMed:10922366, ECO:0000269|PubMed:113589... | null | PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 2/5. {ECO:0000255|HAMAP-Rule:MF_02225, ECO:0000269|PubMed:11278255}.; PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 3/5. {ECO:0000255|HAMAP-Rule:MF_02225, ECO:0000269|PubMed:10922366}. | null | null | FUNCTION: Catalyzes two sequential steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine (PubMed:11278255, PubMed:12140293, PubMed:14686929). In the second step the latter compound is decarboxylated to form 4'-phosphopantotheine... | Escherichia coli (strain K12) |
P0ABQ4 | DYR_ECOLI | MISLIAALAVDRVIGMENAMPWNLPADLAWFKRNTLNKPVIMGRHTWESIGRPLPGRKNIILSSQPGTDDRVTWVKSVDEAIAACGDVPEIMVIGGGRVYEQFLPKAQKLYLTHIDAEVEGDTHFPDYEPDDWESVFSEFHDADAQNSHSYCFEILERR | 1.5.1.3 | null | dihydrofolate metabolic process [GO:0046452]; folic acid metabolic process [GO:0046655]; glycine biosynthetic process [GO:0006545]; one-carbon metabolic process [GO:0006730]; response to antibiotic [GO:0046677]; response to methotrexate [GO:0031427]; response to xenobiotic stimulus [GO:0009410]; tetrahydrofolate biosyn... | cytosol [GO:0005829] | dihydrofolate reductase activity [GO:0004146]; dihydrofolic acid binding [GO:0051871]; folic acid binding [GO:0005542]; methotrexate binding [GO:0051870]; NADP binding [GO:0050661]; NADP+ binding [GO:0070401]; NADPH binding [GO:0070402] | PF00186; | 3.40.430.10; | Dihydrofolate reductase family | null | null | CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000255|PROSITE-ProRule:PRU00660, ECO:0000269|PubMed:16510443}; | null | PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. | null | null | FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. | Escherichia coli (strain K12) |
P0ABR9 | MHPB_ECOLI | MHAYLHCLSHSPLVGYVDPAQEVLDEVNGVIASARERIAAFSPELVVLFAPDHYNGFFYDVMPPFCLGVGATAIGDFGSAAGELPVPVELAEACAHAVMKSGIDLAVSYCMQVDHGFAQPLEFLLGGLDKVPVLPVFINGVATPLPGFQRTRMLGEAIGRFTSTLNKRVLFLGSGGLSHQPPVPELAKADAHMRDRLLGSGKDLPASERELRQQRVISAAEKFVEDQRTLHPLNPIWDNQFMTLLEQGRIQELDAVSNEELSAIAGKSTHEIKTWVAAFAAISAFGNWRSEGRYYRPIPEWIAGFGSLSARTEN | 1.13.11.16 | null | 3-(3-hydroxy)phenylpropionate catabolic process [GO:0019622]; 3-phenylpropionate catabolic process [GO:0019380]; phenylpropanoid catabolic process [GO:0046271] | null | 3-carboxyethylcatechol 2,3-dioxygenase activity [GO:0047070]; ferrous iron binding [GO:0008198] | PF02900; | 3.40.830.10; | LigB/MhpB extradiol dioxygenase family | null | null | CATALYTIC ACTIVITY: Reaction=3-(2,3-dihydroxyphenyl)propanoate + O2 = (2Z,4E)-2-hydroxy-6-oxonona-2,4-dienedioate + H(+); Xref=Rhea:RHEA:23840, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:46951, ChEBI:CHEBI:66887; EC=1.13.11.16; Evidence={ECO:0000269|PubMed:8399388, ECO:0000269|PubMed:8752345}; CATALYTIC ACTIVITY... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=26 uM for 2,3-dihydroxyphenylpropionic acid (at 20 degrees Celsius and pH 8) {ECO:0000269|PubMed:8399388, ECO:0000269|PubMed:8752345}; KM=36 uM for 2,3-dihydroxycinnamic acid (at 20 degrees Celsius and pH 8) {ECO:0000269|PubMed:8752345}; KM=37 uM for methyl-2,3-dih... | PATHWAY: Aromatic compound metabolism; 3-phenylpropanoate degradation. | null | null | FUNCTION: Catalyzes the non-heme iron(II)-dependent oxidative cleavage of 2,3-dihydroxyphenylpropionic acid and 2,3-dihydroxicinnamic acid into 2-hydroxy-6-ketononadienedioate and 2-hydroxy-6-ketononatrienedioate, respectively. {ECO:0000269|PubMed:8399388, ECO:0000269|PubMed:8752345}. | Escherichia coli (strain K12) |
P0ABS1 | DKSA_ECOLI | MQEGQNRKTSSLSILAIAGVEPYQEKPGEEYMNEAQLAHFRRILEAWRNQLRDEVDRTVTHMQDEAANFPDPVDRAAQEEEFSLELRNRDRERKLIKKIEKTLKKVEDEDFGYCESCGVEIGIRRLEARPTADLCIDCKTLAEIREKQMAG | null | null | double-strand break repair [GO:0006302]; regulation of gene expression [GO:0010468] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | guanosine tetraphosphate binding [GO:0097216]; zinc ion binding [GO:0008270] | PF21157;PF01258; | 1.20.120.910; | DksA family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00926, ECO:0000269|PubMed:16858726}. | null | null | null | null | null | FUNCTION: Transcription factor that acts by binding directly to the RNA polymerase (RNAP). Required for negative regulation of rRNA expression and positive regulation of several amino acid biosynthesis promoters. Also required for regulation of fis expression. Binding to RNAP disrupts interaction of RNAP with DNA, inhi... | Escherichia coli (strain K12) |
P0ABS5 | DNAG_ECOLI | MAGRIPRVFINDLLARTDIVDLIDARVKLKKQGKNFHACCPFHNEKTPSFTVNGEKQFYHCFGCGAHGNAIDFLMNYDKLEFVETVEELAAMHNLEVPFEAGSGPSQIERHQRQTLYQLMDGLNTFYQQSLQQPVATSARQYLEKRGLSHEVIARFAIGFAPPGWDNVLKRFGGNPENRQSLIDAGMLVTNDQGRSYDRFRERVMFPIRDKRGRVIGFGGRVLGNDTPKYLNSPETDIFHKGRQLYGLYEAQQDNAEPNRLLVVEGYMDVVALAQYGINYAVASLGTSTTADHIQLLFRATNNVICCYDGDRAGRDAAWR... | 2.7.7.101 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_00974, ECO:0000269|PubMed:1511009, ECO:0000269|PubMed:8679581}; Note=Binds 1 zinc ion per monomer. {ECO:0000255|HAMAP-Rule:MF_00974, ECO:0000269|PubMed:1511009, ECO:0000269|PubMed:8679581}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; ... | DNA replication, synthesis of RNA primer [GO:0006269]; DNA unwinding involved in DNA replication [GO:0006268]; replication fork processing [GO:0031297] | cytoplasm [GO:0005737]; DNA-directed RNA polymerase complex [GO:0000428]; DnaB-DnaG complex [GO:1990156]; primosome complex [GO:1990077]; replisome [GO:0030894] | DNA binding [GO:0003677]; DNA primase activity [GO:0003896]; zinc ion binding [GO:0008270] | PF10410;PF08278;PF08275;PF13155;PF01807; | 3.40.1360.10;3.90.980.10;1.20.50.20;3.90.580.10; | DnaG primase family | null | null | CATALYTIC ACTIVITY: Reaction=ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.; EC=2.7.7.101; Evidence={ECO:0000255|HAMAP-Rule:MF_00974, ECO:0000269|PubMed:1511009, ECO:0000269|PubMed:340457}; | null | null | null | null | FUNCTION: RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. {ECO:0000255|HAMAP-Rule:MF_00974, ECO:0000269|PubMed:1511009, ECO:0000269|PubMed:340457}. | Escherichia coli (strain K12) |
P0ABT2 | DPS_ECOLI | MSTAKLVKSKATNLLYTRNDVSDSEKKATVELLNRQVIQFIDLSLITKQAHWNMRGANFIAVHEMLDGFRTALIDHLDTMAERAVQLGGVALGTTQVINSKTPLKSYPLDIHNVQDHLKELADRYAIVANDVRKAIGEAKDDDTADILTAASRDLDKFLWFIESNIE | 1.16.-.- | null | chromosome condensation [GO:0030261]; intracellular iron ion homeostasis [GO:0006879]; negative regulation of DNA-templated DNA replication initiation [GO:0032297]; response to starvation [GO:0042594] | cytoplasm [GO:0005737]; DnaA-Dps complex [GO:1990084]; membrane [GO:0016020]; nucleoid [GO:0009295] | DNA binding [GO:0003677]; ferric iron binding [GO:0008199]; identical protein binding [GO:0042802]; oxidoreductase activity, acting on metal ions [GO:0016722] | PF00210; | 1.20.1260.10; | Dps family | null | SUBCELLULAR LOCATION: Cytoplasm, nucleoid. | CATALYTIC ACTIVITY: Reaction=2 Fe(2+) + 2 H(+) + H2O2 = 2 Fe(3+) + 2 H2O; Xref=Rhea:RHEA:48712, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16240, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; | null | null | null | null | FUNCTION: During stationary phase, binds the chromosome non-specifically, forming a highly ordered and stable dps-DNA co-crystal within which chromosomal DNA is condensed and protected from diverse damages. It protects DNA from oxidative damage by sequestering intracellular Fe(2+) ion and storing it in the form of Fe(3... | Escherichia coli (strain K12) |
P0ABU0 | MENB_ECOLI | MIYPDEAMLYAPVEWHDCSEGFEDIRYEKSTDGIAKITINRPQVRNAFRPLTVKEMIQALADARYDDNIGVIILTGAGDKAFCSGGDQKVRGDYGGYKDDSGVHHLNVLDFQRQIRTCPKPVVAMVAGYSIGGGHVLHMMCDLTIAADNAIFGQTGPKVGSFDGGWGASYMARIVGQKKAREIWFLCRQYDAKQALDMGLVNTVVPLADLEKETVRWCREMLQNSPMALRCLKAALNADCDGQAGLQELAGNATMLFYMTEEGQEGRNAFNQKRQPDFSKFKRNP | 4.1.3.36 | COFACTOR: Name=hydrogencarbonate; Xref=ChEBI:CHEBI:17544; Evidence={ECO:0000255|HAMAP-Rule:MF_01934, ECO:0000269|PubMed:20643650, ECO:0000305|PubMed:22606952}; Note=The hydrogencarbonate anion plays the same catalytic role (proton acceptor) as the side-chain carboxylate group of the essential 'Asp-185' found in actinob... | menaquinone biosynthetic process [GO:0009234] | cytosol [GO:0005829] | 1,4-dihydroxy-2-naphthoyl-CoA synthase activity [GO:0008935]; bicarbonate binding [GO:0071890] | PF00378; | 1.10.12.10; | Enoyl-CoA hydratase/isomerase family, MenB subfamily | null | null | CATALYTIC ACTIVITY: Reaction=2-succinylbenzoyl-CoA + H(+) = 1,4-dihydroxy-2-naphthoyl-CoA + H2O; Xref=Rhea:RHEA:26562, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57364, ChEBI:CHEBI:58897; EC=4.1.3.36; Evidence={ECO:0000255|HAMAP-Rule:MF_01934, ECO:0000269|PubMed:20643650, ECO:0000269|PubMed:21830810, ECO:0000269... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=26 uM for o-succinylbenzoyl-CoA {ECO:0000269|PubMed:21830810}; KM=2.8 uM for o-succinylbenzoyl-CoA {ECO:0000269|PubMed:23658663}; Note=kcat is 620 sec(-1) with o-succinylbenzoyl-CoA as substrate (PubMed:21830810). kcat is 1.24 min(-1) with o-succinylbenzoyl-CoA as ... | PATHWAY: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 6/7. {ECO:0000255|HAMAP-Rule:MF_01934}.; PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01934}. | null | null | FUNCTION: Converts o-succinylbenzoyl-CoA (OSB-CoA) to 1,4-dihydroxy-2-naphthoyl-CoA (DHNA-CoA). {ECO:0000255|HAMAP-Rule:MF_01934, ECO:0000269|PubMed:1091286, ECO:0000269|PubMed:20643650, ECO:0000269|PubMed:21830810, ECO:0000269|PubMed:23658663}. | Escherichia coli (strain K12) |
P0ABU2 | YCHF_ECOLI | MGFKCGIVGLPNVGKSTLFNALTKAGIEAANFPFCTIEPNTGVVPMPDPRLDQLAEIVKPQRTLPTTMEFVDIAGLVKGASKGEGLGNQFLTNIRETEAIGHVVRCFENDNIIHVSGKVNPADDIEVINTELALADLDTCERAIHRVQKKAKGGDKDAKAELAVLEKCLPQLENAGMLRALDLSAEEKAAIRYLSFLTLKPTMYIANVNEDGFENNPYLDQVREIAAKEGSVVVPVCAAVEADIAELDDEERDEFMQELGLEEPGLNRVIRAGYKLLNLQTYFTAGVKEVRAWTIPVGATAPQAAGKIHTDFEKGFIRAQ... | null | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; | response to oxidative stress [GO:0006979] | cytoplasm [GO:0005737] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; enzyme inhibitor activity [GO:0004857]; GTP binding [GO:0005525]; metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803]; ribosomal large subunit binding [GO:0043023]; ribosome binding [GO:0043022] | PF01926;PF06071; | 3.10.20.30;3.40.50.300;1.10.150.300; | TRAFAC class OBG-HflX-like GTPase superfamily, OBG GTPase family, YchF/OLA1 subfamily | null | null | null | null | null | null | null | FUNCTION: ATPase that binds to both the 70S ribosome and the 50S ribosomal subunit in a nucleotide-independent manner. Does not hydrolyze GTP. {ECO:0000255|HAMAP-Rule:MF_00944, ECO:0000269|PubMed:21527254}. | Escherichia coli (strain K12) |
P0ABU7 | EXBB_ECOLI | MGNNLMQTDLSVWGMYQHADIVVKCVMIGLILASVVTWAIFFSKSVEFFNQKRRLKREQQLLAEARSLNQANDIAADFGSKSLSLHLLNEAQNELELSEGSDDNEGIKERTSFRLERRVAAVGRQMGRGNGYLATIGAISPFVGLFGTVWGIMNSFIGIAQTQTTNLAVVAPGIAEALLATAIGLVAAIPAVVIYNVFARQIGGFKAMLGDVAAQVLLLQSRDLDLEASAAAHPVRVAQKLRAG | null | null | bacteriocin transport [GO:0043213]; cobalamin transport [GO:0015889]; intracellular iron ion homeostasis [GO:0006879]; intracellular monoatomic cation homeostasis [GO:0030003]; protein import [GO:0017038]; protein stabilization [GO:0050821] | cell outer membrane [GO:0009279]; membrane [GO:0016020]; plasma membrane [GO:0005886]; plasma membrane protein complex [GO:0098797]; transmembrane transporter complex [GO:1902495] | energy transducer activity [GO:0031992]; identical protein binding [GO:0042802]; transmembrane transporter activity [GO:0022857] | PF01618; | null | ExbB/TolQ family | null | SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. | null | null | null | null | null | FUNCTION: Involved in the TonB-dependent energy-dependent transport of various receptor-bound substrates. Protects ExbD from proteolytic degradation and functionally stabilizes TonB. | Escherichia coli (strain K12) |
P0ABU9 | TOLQ_ECOLI | MTDMNILDLFLKASLLVKLIMLILIGFSIASWAIIIQRTRILNAAAREAEAFEDKFWSGIELSRLYQESQGKRDNLTGSEQIFYSGFKEFVRLHRANSHAPEAVVEGASRAMRISMNRELENLETHIPFLGTVGSISPYIGLFGTVWGIMHAFIALGAVKQATLQMVAPGIAEALIATAIGLFAAIPAVMAYNRLNQRVNKLELNYDNFMEEFTAILHRQAFTVSESNKG | null | null | bacteriocin transport [GO:0043213]; cell cycle [GO:0007049]; cell division [GO:0051301]; protein import [GO:0017038]; regulation of membrane invagination [GO:1905153] | cell division site [GO:0032153]; cell envelope [GO:0030313]; membrane [GO:0016020]; plasma membrane [GO:0005886] | null | PF01618; | null | ExbB/TolQ family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_02202, ECO:0000269|PubMed:8300535, ECO:0000269|PubMed:8331075}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_02202, ECO:0000269|PubMed:8300535, ECO:0000305|PubMed:8331075}. Note=Accumulates at cell constriction sites. Recruitment to the divi... | null | null | null | null | null | FUNCTION: Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity (PubMed:1683466, PubMed:17233825). Required, with TolR, for the proton motive force-dependent activation of TolA and for TolA-Pal interaction (PubMed:117... | Escherichia coli (strain K12) |
P0ABV2 | EXBD_ECOLI | MAMHLNENLDDNGEMHDINVTPFIDVMLVLLIIFMVAAPLATVDVKVNLPASTSTPQPRPEKPVYLSVKADNSMFIGNDPVTDETMITALNALTEGKKDTTIFFRADKTVDYETLMKVMDTLHQAGYLKIGLVGEETAKAK | null | null | bacteriocin transport [GO:0043213]; cobalamin transport [GO:0015889]; intracellular iron ion homeostasis [GO:0006879]; intracellular monoatomic cation homeostasis [GO:0030003]; protein stabilization [GO:0050821]; protein transport [GO:0015031] | cell outer membrane [GO:0009279]; membrane [GO:0016020]; plasma membrane [GO:0005886]; plasma membrane protein complex [GO:0098797]; transmembrane transporter complex [GO:1902495] | energy transducer activity [GO:0031992]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]; transmembrane transporter activity [GO:0022857] | PF02472; | 3.30.420.270; | ExbD/TolR family | null | SUBCELLULAR LOCATION: Cell inner membrane; Single-pass type II membrane protein. | null | null | null | null | null | FUNCTION: Involved in the TonB-dependent energy-dependent transport of various receptor-bound substrates. | Escherichia coli (strain K12) |
P0ABV6 | TOLR_ECOLI | MARARGRGRRDLKSEINIVPLLDVLLVLLLIFMATAPIITQSVEVDLPDATESQAVSSNDNPPVIVEVSGIGQYTVVVEKDRLERLPPEQVVAEVSSRFKANPKTVFLIGGAKDVPYDEIIKALNLLHSAGVKSVGLMTQPI | null | null | bacteriocin transport [GO:0043213]; cell cycle [GO:0007049]; cell division [GO:0051301]; protein transport [GO:0015031]; regulation of membrane invagination [GO:1905153] | cell division site [GO:0032153]; membrane [GO:0016020]; plasma membrane [GO:0005886] | transmembrane transporter activity [GO:0022857] | PF02472; | 3.30.420.270; | ExbD/TolR family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_02203, ECO:0000269|PubMed:8331075, ECO:0000269|PubMed:8376353}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_02203, ECO:0000269|PubMed:8376353, ECO:0000305|PubMed:8331075}. Note=Accumulates at cell constriction sites. Recruitment to the div... | null | null | null | null | null | FUNCTION: Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity (PubMed:1683466, PubMed:17233825). Required, with TolQ, for the proton motive force-dependent activation of TolA and for TolA-Pal interaction (PubMed:117... | Escherichia coli (strain K12) |
P0ABZ1 | FLIG_ECOLI | MSNLTGTDKSVILLMTIGEDRAAEVFKHLSQREVQTLSAAMANVTQISNKQLTDVLAEFEQEAEQFAALNINANDYLRSVLVKALGEERAASLLEDILETRDTASGIETLNFMEPQSAADLIRDEHPQIIATILVHLKRAQAADILALFDERLRHDVMLRIATFGGVQPAALAELTEVLNGLLDGQNLKRSKMGGVRTAAEIINLMKTQQEEAVITAVREFDGELAQKIIDEMFLFENLVDVDDRSIQRLLQEVDSESLLIALKGAEQPLREKFLRNMSQRAADILRDDLANRGPVRLSQVENEQKAILLIVRRLAETGE... | null | null | bacterial-type flagellum assembly [GO:0044780]; bacterial-type flagellum-dependent cell motility [GO:0071973]; bacterial-type flagellum-dependent swimming motility [GO:0071977]; chemotaxis [GO:0006935] | bacterial-type flagellum [GO:0009288]; bacterial-type flagellum basal body, C ring [GO:0009433]; bacterial-type flagellum rotor complex [GO:0120107]; plasma membrane [GO:0005886] | cytoskeletal motor activity [GO:0003774]; identical protein binding [GO:0042802] | PF01706;PF14841;PF14842; | 1.10.220.30; | FliG family | null | SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. Bacterial flagellum basal body. | null | null | null | null | null | FUNCTION: FliG is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation. | Escherichia coli (strain K12) |
P0ABZ6 | SURA_ECOLI | MKNWKTLLLGIAMIANTSFAAPQVVDKVAAVVNNGVVLESDVDGLMQSVKLNAAQARQQLPDDATLRHQIMERLIMDQIILQMGQKMGVKISDEQLDQAIANIAKQNNMTLDQMRSRLAYDGLNYNTYRNQIRKEMIISEVRNNEVRRRITILPQEVESLAQQVGNQNDASTELNLSHILIPLPENPTSDQVNEAESQARAIVDQARNGADFGKLAIAHSADQQALNGGQMGWGRIQELPGIFAQALSTAKKGDIVGPIRSGVGFHILKVNDLRGESKNISVTEVHARHILLKPSPIMTDEQARVKLEQIAADIKSGKTT... | 5.2.1.8 | null | chaperone-mediated protein folding [GO:0061077]; Gram-negative-bacterium-type cell outer membrane assembly [GO:0043165]; maintenance of stationary phase [GO:0060274]; maintenance of unfolded protein [GO:0036506]; protein folding [GO:0006457]; protein stabilization [GO:0050821] | outer membrane-bounded periplasmic space [GO:0030288] | peptide binding [GO:0042277]; peptidyl-prolyl cis-trans isomerase activity [GO:0003755]; unfolded protein binding [GO:0051082] | PF00639;PF13616;PF09312; | 3.10.50.40;1.10.4030.10; | null | null | SUBCELLULAR LOCATION: Periplasm. Note=Is capable of associating with the outer membrane. | 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:8985185}; | null | null | null | null | FUNCTION: Chaperone involved in the correct folding and assembly of outer membrane proteins, such as OmpA, OmpF and LamB (PubMed:8985185). Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins (PubMed:8985185). May... | Escherichia coli (strain K12) |
P0AC00 | FRLB_ECOLI | MLDIDKSTVDFLVTENMVQEVEKVLSHDVPLVHAIVEEMVKRDIDRIYFVACGSPLNAAQTAKHLADRFSDLQVYAISGWEFCDNTPYRLDDRCAVIGVSDYGKTEEVIKALELGRACGALTAAFTKRADSPITSAAEFSIDYQADCIWEIHLLLCYSVVLEMITRLAPNAEIGKIKNDLKQLPNALGHLVRTWEEKGRQLGELASQWPMIYTVAAGPLRPLGYKEGIVTLMEFTWTHGCVIESGEFRHGPLEIVEPGVPFLFLLGNDESRHTTERAINFVKQRTDNVIVIDYAEISQGLHPWLAPFLMFVPMEWLCYYL... | 3.5.-.- | null | fructose 6-phosphate metabolic process [GO:0006002]; protein N-linked glycosylation [GO:0006487]; UDP-N-acetylglucosamine metabolic process [GO:0006047] | null | carbohydrate derivative binding [GO:0097367]; glutamine-fructose-6-phosphate transaminase (isomerizing) activity [GO:0004360]; hydro-lyase activity [GO:0016836]; hydrolase activity [GO:0016787]; identical protein binding [GO:0042802] | PF01380; | null | null | null | null | CATALYTIC ACTIVITY: Reaction=H2O + N(6)-(6-phospho-D-fructosyl)-L-lysine = D-glucose 6-phosphate + L-lysine; Xref=Rhea:RHEA:28382, ChEBI:CHEBI:15377, ChEBI:CHEBI:32551, ChEBI:CHEBI:61392, ChEBI:CHEBI:61548; Evidence={ECO:0000269|PubMed:12147680}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.4 mM for fructoselysine 6-phosphate {ECO:0000269|PubMed:12147680}; | PATHWAY: Carbohydrate metabolism; fructoselysine degradation; D-glucose 6-phosphate and lysine from fructoselysine: step 2/2. {ECO:0000269|PubMed:14641112, ECO:0000305|PubMed:12147680}. | null | null | FUNCTION: Catalyzes the reversible conversion of fructoselysine 6-phosphate to glucose 6-phosphate and lysine (PubMed:12147680). Functions in a fructoselysine degradation pathway that allows E.coli to grow on fructoselysine or psicoselysine (PubMed:14641112). {ECO:0000269|PubMed:12147680, ECO:0000269|PubMed:14641112}. | Escherichia coli (strain K12) |
P0AC02 | BAMD_ECOLI | MTRMKYLVAAATLSLFLAGCSGSKEEVPDNPPNEIYATAQQKLQDGNWRQAITQLEALDNRYPFGPYSQQVQLDLIYAYYKNADLPLAQAAIDRFIRLNPTHPNIDYVMYMRGLTNMALDDSALQGFFGVDRSDRDPQHARAAFSDFSKLVRGYPNSQYTTDATKRLVFLKDRLAKYEYSVAEYYTERGAWVAVVNRVEGMLRDYPDTQATRDALPLMENAYRQMQMNAQAEKVAKIIAANSSNT | null | null | Gram-negative-bacterium-type cell outer membrane assembly [GO:0043165]; protein insertion into membrane [GO:0051205] | Bam protein complex [GO:1990063]; cell outer membrane [GO:0009279]; membrane [GO:0016020] | null | PF13525; | 1.25.40.10; | BamD family | null | SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-Rule:MF_00922, ECO:0000269|PubMed:16079137, ECO:0000269|PubMed:26900875, ECO:0000269|PubMed:26901871}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_00922, ECO:0000269|PubMed:16079137, ECO:0000269|PubMed:27686148}. | null | null | null | null | null | FUNCTION: Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamA, the core component of the assembly machinery. Probably involved in transient protein interactions. Efficient substrate folding and ins... | Escherichia coli (strain K12) |
P0AC13 | DHPS_ECOLI | MKLFAQGTSLDLSHPHVMGILNVTPDSFSDGGTHNSLIDAVKHANLMINAGATIIDVGGESTRPGAAEVSVEEELQRVIPVVEAIAQRFEVWISVDTSKPEVIRESAKVGAHIINDIRSLSEPGALEAAAETGLPVCLMHMQGNPKTMQEAPKYDDVFAEVNRYFIEQIARCEQAGIAKEKLLLDPGFGFGKNLSHNYSLLARLAEFHHFNLPLLVGMSRKSMIGQLLNVGPSERLSGSLACAVIAAMQGAHIIRVHDVKETVEAMRVVEATLSAKENKRYE | 2.5.1.15 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:4304228}; Note=Magnesium is required for activity, even if it seems to interact primarily with the substrate. {ECO:0000269|PubMed:4304228, ECO:0000305}; | folic acid biosynthetic process [GO:0046656]; response to xenobiotic stimulus [GO:0009410]; tetrahydrofolate biosynthetic process [GO:0046654] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | dihydropteroate synthase activity [GO:0004156]; metal ion binding [GO:0046872] | PF00809; | 3.20.20.20; | DHPS family | null | null | CATALYTIC ACTIVITY: Reaction=(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate = 7,8-dihydropteroate + diphosphate; Xref=Rhea:RHEA:19949, ChEBI:CHEBI:17836, ChEBI:CHEBI:17839, ChEBI:CHEBI:33019, ChEBI:CHEBI:72950; EC=2.5.1.15; Evidence={ECO:0000269|PubMed:368012, ECO:0000269|PubMed:4304228}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.5 uM for 4-aminobenzoate {ECO:0000269|PubMed:4304228}; | PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5. {ECO:0000269|PubMed:4304228}; | null | FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000269|PubMed:368012}. | Escherichia coli (strain K12) |
P0AC16 | FOLB_ECOLI | MDIVFIEQLSVITTIGVYDWEQTIEQKLVFDIEMAWDNRKAAKSDDVADCLSYADIAETVVSHVEGARFALVERVAEEVAELLLARFNSPWVRIKLSKPGAVARAANVGVIIERGNNLKENN | 4.1.2.25; 5.1.99.8 | null | folic acid biosynthetic process [GO:0046656]; tetrahydrofolate biosynthetic process [GO:0046654] | cytoplasm [GO:0005737] | dihydroneopterin aldolase activity [GO:0004150]; identical protein binding [GO:0042802]; isomerase activity [GO:0016853] | PF02152; | 3.30.1130.10; | DHNA family | null | null | CATALYTIC ACTIVITY: Reaction=7,8-dihydroneopterin = 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde; Xref=Rhea:RHEA:10540, ChEBI:CHEBI:17001, ChEBI:CHEBI:17071, ChEBI:CHEBI:44841; EC=4.1.2.25; Evidence={ECO:0000269|PubMed:9651328}; CATALYTIC ACTIVITY: Reaction=7,8-dihydroneopterin = 7,8-dihydromonapterin; Xref=Rhea:... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=64 uM for 7,8-dihydroneopterin in aldolase reaction {ECO:0000269|PubMed:9651328}; KM=45 uM for 7,8-dihydroneopterin in epimerase reaction {ECO:0000269|PubMed:9651328}; KM=36 uM for 7,8-dihydromonapterin in aldolase reaction {ECO:0000269|PubMed:9651328}; KM=57 uM fo... | PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 3/4. | null | null | FUNCTION: Catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin. Can use L-threo-dihydroneopterin and D-erythro-dihydroneopterin as substrates for the formation of 6-hydroxymethyldihydropterin, but it can also catalyze the epimerization of carbon 2' of dihydroneopterin to dihydromonapter... | Escherichia coli (strain K12) |
P0AC19 | FOLX_ECOLI | MAQPAAIIRIKNLRLRTFIGIKEEEINNRQDIVINVTIHYPADKARTSEDINDALNYRTVTKNIIQHVENNRFSLLEKLTQDVLDIAREHHWVTYAEVEIDKLHALRYADSVSMTLSWQR | 5.1.99.7 | null | folic acid-containing compound metabolic process [GO:0006760]; pteridine-containing compound biosynthetic process [GO:0042559] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | dihydroneopterin aldolase activity [GO:0004150]; dihydroneopterin triphosphate 2'-epimerase activity [GO:0008719]; identical protein binding [GO:0042802] | PF02152; | 3.30.1130.10; | DHNA family | null | null | CATALYTIC ACTIVITY: Reaction=7,8-dihydroneopterin 3'-triphosphate = 7,8-dihydromonapterin 3'-triphosphate; Xref=Rhea:RHEA:28346, ChEBI:CHEBI:58462, ChEBI:CHEBI:61186; EC=5.1.99.7; Evidence={ECO:0000269|PubMed:9182560, ECO:0000269|PubMed:9651328}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=13 uM for 7,8-dihydroneopterin triphosphate {ECO:0000269|PubMed:9651328}; KM=149 uM for 7,8-dihydroneopterin {ECO:0000269|PubMed:9651328}; KM=66 uM for 7,8-dihydromonapterin {ECO:0000269|PubMed:9651328}; Vmax=480 umol/h/mg enzyme for the epimerization of 7,8-dihydr... | null | null | null | FUNCTION: Catalyzes the epimerization of carbon 2' of the side chain of 7,8-dihydroneopterin triphosphate (H2NTP) to form 7,8-dihydromonapterin triphosphate (H2MTP) (PubMed:9182560, PubMed:9651328). Is required for tetrahydromonapterin biosynthesis, a major pterin in E.coli (PubMed:19897652). {ECO:0000269|PubMed:198976... | Escherichia coli (strain K12) |
P0AC23 | FOCA_ECOLI | MKADNPFDLLLPAAMAKVAEEAGVYKATKHPLKTFYLAITAGVFISIAFVFYITATTGTGTMPFGMAKLVGGICFSLGLILCVVCGADLFTSTVLIVVAKASGRITWGQLAKNWLNVYFGNLVGALLFVLLMWLSGEYMTANGQWGLNVLQTADHKVHHTFIEAVCLGILANLMVCLAVWMSYSGRSLMDKAFIMVLPVAMFVASGFEHSIANMFMIPMGIVIRDFASPEFWTAVGSAPENFSHLTVMNFITDNLIPVTIGNIIGGGLLVGLTYWVIYLRENDHH | null | null | formate transport [GO:0015724]; mixed acid fermentation [GO:0019664]; response to acidic pH [GO:0010447] | plasma membrane [GO:0005886] | formate transmembrane transporter activity [GO:0015499]; identical protein binding [GO:0042802] | PF01226; | 1.20.1080.10; | FNT transporter (TC 2.A.44) family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:20041954, ECO:0000269|PubMed:24659605, ECO:0000269|PubMed:33169422}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P0AC25}. | CATALYTIC ACTIVITY: Reaction=formate(in) = formate(out); Xref=Rhea:RHEA:29679, ChEBI:CHEBI:15740; Evidence={ECO:0000269|PubMed:24659605, ECO:0000269|PubMed:30247527, ECO:0000269|PubMed:35084298, ECO:0000305|PubMed:23335413, ECO:0000305|PubMed:8022272}; | null | null | null | null | FUNCTION: Involved in the bidirectional transport of formate during mixed-acid fermentation (PubMed:23335413, PubMed:24659605, PubMed:30247527, PubMed:33169422, PubMed:35084298, PubMed:35377837, PubMed:35390794, PubMed:8022272). Functions to maintain relatively constant intracellular formate levels during growth, using... | Escherichia coli (strain K12) |
P0AC25 | FOCA_ECO57 | MKADNPFDLLLPAAMAKVAEEAGVYKATKHPLKTFYLAITAGVFISIAFVFYITATTGTGTMPFGMAKLVGGICFSLGLILCVVCGADLFTSTVLIVVAKASGRITWGQLAKNWLNVYFGNLVGALLFVLLMWLSGEYMTANGQWGLNVLQTADHKVHHTFIEAVCLGILANLMVCLAVWMSYSGRSLMDKAFIMVLPVAMFVASGFEHSIANMFMIPMGIVIRDFASPEFWTAVGSAPENFSHLTVMNFITDNLIPVTIGNIIGGGLLVGLTYWVIYLRENDHH | null | null | null | plasma membrane [GO:0005886] | formate transmembrane transporter activity [GO:0015499]; identical protein binding [GO:0042802] | PF01226; | 1.20.1080.10; | FNT transporter (TC 2.A.44) family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:19940917}; Multi-pass membrane protein {ECO:0000269|PubMed:19940917}. | CATALYTIC ACTIVITY: Reaction=formate(in) = formate(out); Xref=Rhea:RHEA:29679, ChEBI:CHEBI:15740; Evidence={ECO:0000269|PubMed:19940917}; | null | null | null | null | FUNCTION: Involved in the bidirectional transport of formate during mixed-acid fermentation (PubMed:19940917). Functions to maintain relatively constant intracellular formate levels during growth, using different mechanisms for efflux and uptake of the anion (By similarity). Is impermeable to water (PubMed:19940917). {... | Escherichia coli O157:H7 |
P0AC30 | FTSX_ECOLI | MNKRDAINHIRQFGGRLDRFRKSVGGSGDGGRNAPKRAKSSPKPVNRKTNVFNEQVRYAFHGALQDLKSKPFATFLTVMVIAISLTLPSVCYMVYKNVNQAATQYYPSPQITVYLQKTLDDDAAAGVVAQLQAEQGVEKVNYLSREDALGEFRNWSGFGGALDMLEENPLPAVAVVIPKLDFQGTESLNTLRDRITQINGIDEVRMDDSWFARLAALTGLVGRVSAMIGVLMVAAVFLVIGNSVRLSIFARRDSINVQKLIGATDGFILRPFLYGGALLGFSGALLSLILSEILVLRLSSAVAEVAQVFGTKFDINGLSF... | null | null | cell division [GO:0051301]; division septum assembly [GO:0000917]; FtsZ-dependent cytokinesis [GO:0043093]; peptidoglycan turnover [GO:0009254]; positive regulation of cell division [GO:0051781] | ATPase complex [GO:1904949]; cell division site [GO:0032153]; division septum [GO:0000935]; divisome complex [GO:1990586]; Gram-negative-bacterium-type cell wall [GO:0009276]; plasma membrane [GO:0005886]; plasma membrane protein complex [GO:0098797] | null | PF02687;PF18075; | 3.30.70.3040; | ABC-4 integral membrane protein family, FtsX subfamily | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:10048040, ECO:0000269|PubMed:14729705, ECO:0000269|PubMed:3323846}; Multi-pass membrane protein {ECO:0000269|PubMed:10048040, ECO:0000269|PubMed:14729705, ECO:0000269|PubMed:3323846}. Note=Localizes to the septal ring at the later stages of cell growth and r... | null | null | null | null | null | FUNCTION: Part of the ABC transporter FtsEX involved in cellular division. Important for assembly or stability of the septal ring. Encoded in an operon consisting of genes ftsY, ftsE and ftsX. {ECO:0000269|PubMed:10048040, ECO:0000269|PubMed:14729705}. | Escherichia coli (strain K12) |
P0AC33 | FUMA_ECOLI | MSNKPFHYQAPFPLKKDDTEYYLLTSEHVSVSEFEGQEILKVAPEALTLLARQAFHDASFMLRPAHQQQVADILRDPEASENDKYVALQFLRNSDIAAKGVLPTCQDTGTAIIVGKKGQRVWTGGGDEAALARGVYNTYIEDNLRYSQNAPLDMYKEVNTGTNLPAQIDLYAVDGDEYKFLCIAKGGGSANKTYLYQETKALLTPGKLKNYLVEKMRTLGTAACPPYHIAFVIGGTSAETNLKTVKLASAKYYDELPTEGNEHGQAFRDVELEKELLIEAQNLGLGAQFGGKYFAHDIRVIRLPRHGASCPVGMGVSCSA... | 4.2.1.2; 5.3.2.2 | COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000269|PubMed:1329945, ECO:0000269|PubMed:23405168}; Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000269|PubMed:1329945, ECO:0000269|PubMed:23405168}; | tricarboxylic acid cycle [GO:0006099] | cytosol [GO:0005829] | 4 iron, 4 sulfur cluster binding [GO:0051539]; fumarate hydratase activity [GO:0004333]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; oxaloacetate tautomerase activity [GO:0050163]; protein homodimerization activity [GO:0042803] | PF05681;PF05683; | 3.20.130.10; | Class-I fumarase family | null | null | CATALYTIC ACTIVITY: Reaction=(S)-malate = fumarate + H2O; Xref=Rhea:RHEA:12460, ChEBI:CHEBI:15377, ChEBI:CHEBI:15589, ChEBI:CHEBI:29806; EC=4.2.1.2; Evidence={ECO:0000269|PubMed:1329945, ECO:0000269|PubMed:23405168, ECO:0000269|PubMed:8422384}; CATALYTIC ACTIVITY: Reaction=oxaloacetate = enol-oxaloacetate; Xref=Rhea:RH... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.7 mM for (S)-malate {ECO:0000269|PubMed:1329945, ECO:0000269|PubMed:23405168}; KM=0.6 mM for fumarate {ECO:0000269|PubMed:8422384}; KM=0.46 mM for fumarate {ECO:0000269|PubMed:23405168}; KM=0.8 mM for D-tartrate {ECO:0000269|PubMed:23405168}; KM=0.1 mM for enol-o... | PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; (S)-malate from fumarate: step 1/1. {ECO:0000303|PubMed:1329945, ECO:0000303|PubMed:3282546}. | null | null | FUNCTION: Catalyzes the reversible hydration of fumarate to (S)-malate. Functions as an aerobic enzyme in the direction of malate formation as part of the citric acid cycle. Accounts for about 80% of the fumarase activity when the bacteria grow aerobically. To a lesser extent, also displays D-tartrate dehydratase activ... | Escherichia coli (strain K12) |
P0AC38 | ASPA_ECOLI | MSNNIRIEEDLLGTREVPADAYYGVHTLRAIENFYISNNKISDIPEFVRGMVMVKKAAAMANKELQTIPKSVANAIIAACDEVLNNGKCMDQFPVDVYQGGAGTSVNMNTNEVLANIGLELMGHQKGEYQYLNPNDHVNKCQSTNDAYPTGFRIAVYSSLIKLVDAINQLREGFERKAVEFQDILKMGRTQLQDAVPMTLGQEFRAFSILLKEEVKNIQRTAELLLEVNLGATAIGTGLNTPKEYSPLAVKKLAEVTGFPCVPAEDLIEATSDCGAYVMVHGALKRLAVKMSKICNDLRLLSSGPRAGLNEINLPELQAG... | 4.3.1.1 | null | aspartate catabolic process [GO:0006533]; aspartate metabolic process [GO:0006531]; glutamate catabolic process [GO:0006538]; nitrogen utilization [GO:0019740]; protein homotetramerization [GO:0051289]; tricarboxylic acid cycle [GO:0006099] | cytosol [GO:0005829]; membrane [GO:0016020] | aspartate ammonia-lyase activity [GO:0008797]; identical protein binding [GO:0042802] | PF10415;PF00206; | 1.10.40.30;1.20.200.10;1.10.275.10; | Class-II fumarase/aspartase family, Aspartase subfamily | null | null | CATALYTIC ACTIVITY: Reaction=L-aspartate = fumarate + NH4(+); Xref=Rhea:RHEA:16601, ChEBI:CHEBI:28938, ChEBI:CHEBI:29806, ChEBI:CHEBI:29991; EC=4.3.1.1; Evidence={ECO:0000269|PubMed:1897995, ECO:0000269|PubMed:2853974, ECO:0000269|PubMed:33012071, ECO:0000269|PubMed:4584395, ECO:0000269|PubMed:8047016, ECO:0000269|PubM... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1 mM for L-aspartate {ECO:0000269|PubMed:4584395}; KM=1.8 mM for L-aspartate {ECO:0000269|PubMed:9230046}; KM=4.3 mM for L-aspartate {ECO:0000269|PubMed:8119980}; KM=20 mM for NH(4)(+) {ECO:0000269|PubMed:4584395}; KM=5 mM for NH(2)OH {ECO:0000269|PubMed:4584395}; ... | PATHWAY: Amino-acid metabolism. {ECO:0000305|PubMed:33012071}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.7 (PubMed:4584395). For deamination reaction, shows maximum velocity at pH 7.3 for the metal ion-independent activity, and at pH 9 for the metal-activated activity (PubMed:1897995). {ECO:0000269|PubMed:1897995, ECO:0000269|PubMed:4584395}; | null | FUNCTION: Catalyzes the reversible conversion of L-aspartate to fumarate and ammonia (PubMed:1897995, PubMed:2853974, PubMed:33012071, PubMed:4584395, PubMed:8047016, PubMed:8119980). In the reverse reaction, consumption of fumarate is observed in the presence of not only NH4(+), but also hydroxylamine (NH(2)OH) (PubMe... | Escherichia coli (strain K12) |
P0AC41 | SDHA_ECOLI | MKLPVREFDAVVIGAGGAGMRAALQISQSGQTCALLSKVFPTRSHTVSAQGGITVALGNTHEDNWEWHMYDTVKGSDYIGDQDAIEYMCKTGPEAILELEHMGLPFSRLDDGRIYQRPFGGQSKNFGGEQAARTAAAADRTGHALLHTLYQQNLKNHTTIFSEWYALDLVKNQDGAVVGCTALCIETGEVVYFKARATVLATGGAGRIYQSTTNAHINTGDGVGMAIRAGVPVQDMEMWQFHPTGIAGAGVLVTEGCRGEGGYLLNKHGERFMERYAPNAKDLAGRDVVARSIMIEIREGRGCDGPWGPHAKLKLDHLGK... | 1.3.5.1 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:12560550, ECO:0000269|PubMed:16407191, ECO:0000269|PubMed:19710024}; Note=Flavinylated by SdhE, about 5% flavinylation occurs in the absence of SdhE. {ECO:0000269|PubMed:26644464}; | aerobic electron transport chain [GO:0019646]; aerobic respiration [GO:0009060]; anaerobic respiration [GO:0009061]; tricarboxylic acid cycle [GO:0006099] | membrane [GO:0016020]; plasma membrane [GO:0005886]; plasma membrane succinate dehydrogenase complex [GO:0045282]; succinate dehydrogenase complex [GO:0045281] | electron transfer activity [GO:0009055]; flavin adenine dinucleotide binding [GO:0050660]; succinate dehydrogenase (quinone) activity [GO:0008177]; succinate dehydrogenase activity [GO:0000104] | PF00890;PF02910; | 3.50.50.60;1.20.58.100;4.10.80.40;3.90.700.10; | FAD-dependent oxidoreductase 2 family, FRD/SDH subfamily | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:12560550, ECO:0000269|PubMed:16079137}; Peripheral membrane protein {ECO:0000269|PubMed:12560550, ECO:0000269|PubMed:16079137}; Cytoplasmic side {ECO:0000269|PubMed:12560550, ECO:0000269|PubMed:16079137}. | CATALYTIC ACTIVITY: Reaction=a quinone + succinate = a quinol + fumarate; Xref=Rhea:RHEA:40523, ChEBI:CHEBI:24646, ChEBI:CHEBI:29806, ChEBI:CHEBI:30031, ChEBI:CHEBI:132124; EC=1.3.5.1; Evidence={ECO:0000305|PubMed:19710024}; | null | PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; fumarate from succinate (bacterial route): step 1/1. {ECO:0000305|PubMed:19710024}. | null | null | FUNCTION: Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; the fumarate reductase is used in anaerobic growth, and the succinate dehydrogenase is used in aerobic growth. {ECO:0000269|PubMed:24374335, ECO:0000305|PubMed:12560550, ECO:000030... | Escherichia coli (strain K12) |
P0AC44 | DHSD_ECOLI | MVSNASALGRNGVHDFILVRATAIVLTLYIIYMVGFFATSGELTYEVWIGFFASAFTKVFTLLALFSILIHAWIGMWQVLTDYVKPLALRLMLQLVIVVALVVYVIYGFVVVWGV | null | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Note=The heme is bound between the two transmembrane subunits.; | aerobic electron transport chain [GO:0019646]; aerobic respiration [GO:0009060]; cytochrome complex assembly [GO:0017004]; tricarboxylic acid cycle [GO:0006099] | membrane [GO:0016020]; plasma membrane [GO:0005886]; succinate dehydrogenase complex [GO:0045281] | electron transfer activity [GO:0009055]; heme binding [GO:0020037]; metal ion binding [GO:0046872]; oxidoreductase activity, acting on the CH-CH group of donors [GO:0016627] | PF01127; | 1.20.1300.10; | null | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000269|PubMed:15919996}. | null | null | PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle. | null | null | FUNCTION: Membrane-anchoring subunit of succinate dehydrogenase (SDH). | Escherichia coli (strain K12) |
P0AC47 | FRDB_ECOLI | MAEMKNLKIEVVRYNPEVDTAPHSAFYEVPYDATTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNNVPKLACKTFLRDYTDGMKVEALANFPIERDLVVDMTHFIESLEAIKPYIIGNSRTADQGTNIQTPAQMAKYHQFSGCINCGLCYAACPQFGLNPEFIGPAAITLAHRYNEDSRDHGKKERMAQLNSQNGVWSCTFVGYCSEVCPKHVDPAAAIQQGKVESSKDFLIATLKPR | 1.3.5.1 | COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000269|PubMed:10373108}; Note=Binds 1 [2Fe-2S] cluster. {ECO:0000269|PubMed:10373108}; COFACTOR: Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137; Evidence={ECO:0000269|PubMed:10373108}; Note=Binds 1 [3Fe-4S] cluster. {ECO:0000269|PubMed:10373108}; C... | anaerobic electron transport chain [GO:0019645]; anaerobic respiration [GO:0009061]; bacterial-type flagellum assembly [GO:0044780]; fermentation [GO:0006113]; tricarboxylic acid cycle [GO:0006099] | cytosol [GO:0005829]; membrane [GO:0016020]; plasma membrane fumarate reductase complex [GO:0045284] | 2 iron, 2 sulfur cluster binding [GO:0051537]; 3 iron, 4 sulfur cluster binding [GO:0051538]; 4 iron, 4 sulfur cluster binding [GO:0051539]; electron transfer activity [GO:0009055]; iron-sulfur cluster binding [GO:0051536]; metal ion binding [GO:0046872]; succinate dehydrogenase (quinone) activity [GO:0008177] | PF13085;PF13237; | 3.10.20.30;1.10.1060.10; | Succinate dehydrogenase/fumarate reductase iron-sulfur protein family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305|PubMed:10373108}; Peripheral membrane protein {ECO:0000305|PubMed:10373108}; Cytoplasmic side {ECO:0000305|PubMed:10373108}. | CATALYTIC ACTIVITY: Reaction=a quinone + succinate = a quinol + fumarate; Xref=Rhea:RHEA:40523, ChEBI:CHEBI:24646, ChEBI:CHEBI:29806, ChEBI:CHEBI:30031, ChEBI:CHEBI:132124; EC=1.3.5.1; Evidence={ECO:0000269|PubMed:11850430}; CATALYTIC ACTIVITY: Reaction=a menaquinone + succinate = a menaquinol + fumarate; Xref=Rhea:RHE... | null | null | null | null | FUNCTION: Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; fumarate reductase is used during anaerobic growth, and succinate dehydrogenase is used during aerobic growth. The QFR enzyme complex binds 2 quinones in or near the membrane; 1 ne... | Escherichia coli (strain K12) |
P0AC53 | G6PD_ECOLI | MAVTQTAQACDLVIFGAKGDLARRKLLPSLYQLEKAGQLNPDTRIIGVGRADWDKAAYTKVVREALETFMKETIDEGLWDTLSARLDFCNLDVNDTAAFSRLGAMLDQKNRITINYFAMPPSTFGAICKGLGEAKLNAKPARVVMEKPLGTSLATSQEINDQVGEYFEECQVYRIDHYLGKETVLNLLALRFANSLFVNNWDNRTIDHVEITVAEEVGIEGRWGYFDKAGQMRDMIQNHLLQILCMIAMSPPSDLSADSIRDEKVKVLKSLRRIDRSNVREKTVRGQYTAGFAQGKKVPGYLEEEGANKSSNTETFVAIR... | 1.1.1.49 | null | glucose metabolic process [GO:0006006]; pentose-phosphate shunt [GO:0006098]; pentose-phosphate shunt, oxidative branch [GO:0009051]; quorum sensing [GO:0009372] | cytosol [GO:0005829] | glucose-6-phosphate dehydrogenase activity [GO:0004345]; identical protein binding [GO:0042802]; NADP binding [GO:0050661] | PF02781;PF00479; | 3.40.50.720; | Glucose-6-phosphate dehydrogenase family | PTM: Probably processed by the ClpPX protease to generate the extracellular death factor (EDF). It is thought that processing produces Asn-Asn-Trp-Asp-Asn which is amidated to generate Asn-Asn-Trp-Asn-Asn (Probable). {ECO:0000305|PubMed:17962566}. | null | CATALYTIC ACTIVITY: Reaction=D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-lactone + H(+) + NADPH; Xref=Rhea:RHEA:15841, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:57955, ChEBI:CHEBI:58349, ChEBI:CHEBI:61548; EC=1.1.1.49; Evidence={ECO:0000255|HAMAP-Rule:MF_00966}; | null | PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 1/3. {ECO:0000255|HAMAP-Rule:MF_00966, ECO:0000269|PubMed:15113569}. | null | null | FUNCTION: Catalyzes the oxidation of glucose 6-phosphate to 6-phosphogluconolactone. {ECO:0000255|HAMAP-Rule:MF_00966, ECO:0000269|PubMed:15113569, ECO:0000269|PubMed:17962566}.; FUNCTION: Probable source of extracellular death factor (EDF, sequence Asn-Asn-Trp-Asn-Asn, NNWNN) following processing and amidation. This p... | Escherichia coli (strain K12) |
P0AC55 | GLNK_ECOLI | MKLVTVIIKPFKLEDVREALSSIGIQGLTVTEVKGFGRQKGHAELYRGAEYSVNFLPKVKIDVAIADDQLDEVIDIVSKAAYTGKIGDGKIFVAELQRVIRIRTGEADEAAL | null | null | positive regulation of nitrogen utilization [GO:0045848]; regulation of nitrogen utilization [GO:0006808] | cytosol [GO:0005829]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; enzyme regulator activity [GO:0030234]; identical protein binding [GO:0042802] | PF00543; | 3.30.70.120; | P(II) protein family | PTM: Uridylylated/deuridylylated by GlnD (PubMed:11847102, PubMed:8843440). Fully uridylylated in nitrogen-limited conditions and deuridylylated when extracellular ammonium increases (PubMed:11847102, PubMed:20639578). Uridylylation abrogates binding to AmtB (PubMed:11847102, PubMed:16864585). {ECO:0000269|PubMed:11847... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11847102, ECO:0000269|PubMed:14668330, ECO:0000269|PubMed:16864585}. Cell inner membrane {ECO:0000269|PubMed:11847102, ECO:0000269|PubMed:14668330, ECO:0000269|PubMed:16864585}. Note=During nitrogen limitation, GlnK is predominantly in its fully uridylylated state in ... | null | null | null | null | null | FUNCTION: Involved in the regulation of nitrogen metabolism (PubMed:10760266, PubMed:11847102, PubMed:12366843, PubMed:14668330, PubMed:28538158, PubMed:8843440). Regulates the activity of its targets by protein-protein interaction in response to the nitrogen status of the cell (PubMed:10760266, PubMed:11847102, PubMed... | Escherichia coli (strain K12) |
P0AC69 | GLRX4_ECOLI | MSTTIEKIQRQIAENPILLYMKGSPKLPSCGFSAQAVQALAACGERFAYVDILQNPDIRAELPKYANWPTFPQLWVDGELVGGCDIVIEMYQRGELQQLIKETAAKYKSEEPDAE | null | null | cell redox homeostasis [GO:0045454]; intracellular iron ion homeostasis [GO:0006879]; iron-sulfur cluster assembly [GO:0016226] | cytosol [GO:0005829]; iron-sulfur cluster assembly complex [GO:1990229] | 2 iron, 2 sulfur cluster binding [GO:0051537]; disulfide oxidoreductase activity [GO:0015036]; metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803] | PF00462; | 3.40.30.10; | Glutaredoxin family, Monothiol subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15833738}. | null | null | null | null | null | FUNCTION: Monothiol glutaredoxin involved in the biogenesis of iron-sulfur clusters. {ECO:0000305}. | Escherichia coli (strain K12) |
P0AC75 | KDTA_ECOLI | MLELLYTALLYLIQPLIWIRLWVRGRKAPAYRKRWGERYGFYRHPLKPGGIMLHSVSVGETLAAIPLVRALRHRYPDLPITVTTMTPTGSERVQSAFGKDVQHVYLPYDLPDALNRFLNKVDPKLVLIMETELWPNLIAALHKRKIPLVIANARLSARSAAGYAKLGKFVRRLLRRITLIAAQNEEDGARFVALGAKNNQVTVTGSLKFDISVTPQLAAKAVTLRRQWAPHRPVWIATSTHEGEESVVIAAHQALLQQFPNLLLILVPRHPERFPDAINLVRQAGLSYITRSSGEVPSTSTQVVVGDTMGELMLLYGIAD... | 2.4.99.12; 2.4.99.13 | null | Kdo2-lipid A biosynthetic process [GO:0036104]; lipid A biosynthetic process [GO:0009245]; lipopolysaccharide core region biosynthetic process [GO:0009244] | membrane [GO:0016020]; plasma membrane [GO:0005886] | Kdo transferase activity [GO:0043842]; transferase activity [GO:0016740] | PF00534;PF04413; | 3.40.50.11720;3.40.50.2000; | Glycosyltransferase group 1 family, Glycosyltransferase 30 subfamily | PTM: Degraded by the protease FtsH; therefore FtsH regulates the addition of the sugar moiety to the LPS and thus the maturation of the LPS precursor. {ECO:0000269|PubMed:18776015}. | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305|PubMed:1577828}; Single-pass membrane protein {ECO:0000305|PubMed:1577828}; Cytoplasmic side {ECO:0000305|PubMed:1577828}. | CATALYTIC ACTIVITY: Reaction=CMP-3-deoxy-beta-D-manno-octulosonate + lipid IVA (E. coli) = alpha-Kdo-(2->6)-lipid IVA (E. coli) + CMP + H(+); Xref=Rhea:RHEA:28066, ChEBI:CHEBI:15378, ChEBI:CHEBI:58603, ChEBI:CHEBI:60364, ChEBI:CHEBI:60377, ChEBI:CHEBI:85987; EC=2.4.99.12; Evidence={ECO:0000269|PubMed:10951204, ECO:0000... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=52 uM for lipid IV(A) (at pH 8) {ECO:0000269|PubMed:1577828}; KM=88 uM for CMP-Kdo (at pH 8) {ECO:0000269|PubMed:1577828}; Vmax=18 umol/min/mg enzyme (at pH 8) {ECO:0000269|PubMed:1577828}; | PATHWAY: Glycolipid biosynthesis; KDO(2)-lipid A biosynthesis; KDO(2)-lipid A from CMP-3-deoxy-D-manno-octulosonate and lipid IV(A): step 1/4. {ECO:0000269|PubMed:1577828}.; PATHWAY: Glycolipid biosynthesis; KDO(2)-lipid A biosynthesis; KDO(2)-lipid A from CMP-3-deoxy-D-manno-octulosonate and lipid IV(A): step 2/4. {EC... | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7. {ECO:0000269|PubMed:1577828}; | null | FUNCTION: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of two 3-deoxy-D-manno-octulosonate (Kdo) residues from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A. {ECO:0000269|PubMed:10951204, ECO:0000269|PubMed:1577828}. | Escherichia coli (strain K12) |
P0AC78 | WECA_ECOLI | MNLLTVSTDLISIFLFTTLFLFFARKVAKKVGLVDKPNFRKRHQGLIPLVGGISVYAGICFTFGIVDYYIPHASLYLACAGVLVFIGALDDRFDISVKIRATIQAAVGIVMMVFGKLYLSSLGYIFGSWEMVLGPFGYFLTLFAVWAAINAFNMVDGIDGLLGGLSCVSFAAIGMILWFDGQTSLAIWCFAMIAAILPYIMLNLGILGRRYKVFMGDAGSTLIGFTVIWILLETTQGKTHPISPVTALWIIAIPLMDMVAIMYRRLRKGMSPFSPDRQHIHHLIMRAGFTSRQAFVLITLAAALLASIGVLAEYSHFVPE... | 2.7.8.33 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_02030, ECO:0000269|PubMed:17237164}; COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP-Rule:MF_02030, ECO:0000269|PubMed:17237164}; | cell wall macromolecule biosynthetic process [GO:0044038]; cell wall organization [GO:0071555]; enterobacterial common antigen biosynthetic process [GO:0009246]; lipopolysaccharide biosynthetic process [GO:0009103]; O antigen biosynthetic process [GO:0009243] | Gram-negative-bacterium-type cell wall [GO:0009276]; membrane [GO:0016020]; plasma membrane [GO:0005886] | glycosyltransferase activity [GO:0016757]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; manganese ion binding [GO:0030145]; phospho-N-acetylmuramoyl-pentapeptide-transferase activity [GO:0008963]; phosphotransferase activity, for other substituted phosphate groups [GO:0016780]; UDP-N-acet... | PF00953; | null | Glycosyltransferase 4 family, WecA subfamily | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_02030, ECO:0000269|PubMed:11700352, ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:17237164}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_02030}. Note=Localizes to discrete regions in the plasma membrane. {ECO:0000269|PubMed:17237164}. | CATALYTIC ACTIVITY: Reaction=di-trans,octa-cis-undecaprenyl phosphate + UDP-N-acetyl-alpha-D-glucosamine = N-acetyl-alpha-D-glucosaminyl-di-trans,octa-cis-undecaprenyl diphosphate + UMP; Xref=Rhea:RHEA:28090, ChEBI:CHEBI:57705, ChEBI:CHEBI:57865, ChEBI:CHEBI:60392, ChEBI:CHEBI:62959; EC=2.7.8.33; Evidence={ECO:0000255|... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5.6 uM for UDP-GlcNAc {ECO:0000269|PubMed:9134438}; KM=0.12 uM for UDP-GlcNAc (in the presence of Mg(2+)) {ECO:0000269|PubMed:17237164}; KM=0.19 uM for UDP-GlcNAc (in the presence of Mn(2+)) {ECO:0000269|PubMed:17237164}; KM=1.7 mM for Mg(2+) {ECO:0000269|PubMed:17... | PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen biosynthesis. {ECO:0000255|HAMAP-Rule:MF_02030, ECO:0000269|PubMed:11700352}.; PATHWAY: Bacterial outer membrane biogenesis; enterobacterial common antigen biosynthesis. {ECO:0000255|HAMAP-Rule:MF_02030, ECO:0000269|PubMed:1730666}. | null | null | FUNCTION: Catalyzes the transfer of the GlcNAc-1-phosphate moiety from UDP-GlcNAc onto the carrier lipid undecaprenyl phosphate (C55-P), yielding GlcNAc-pyrophosphoryl-undecaprenyl (GlcNAc-PP-C55). It is the first lipid-linked intermediate involved in enterobacterial common antigen (ECA) synthesis, and an acceptor for ... | Escherichia coli (strain K12) |
P0AC81 | LGUL_ECOLI | MRLLHTMLRVGDLQRSIDFYTKVLGMKLLRTSENPEYKYSLAFVGYGPETEEAVIELTYNWGVDKYELGTAYGHIALSVDNAAEACEKIRQNGGNVTREAGPVKGGTTVIAFVEDPDGYKIELIEEKDAGRGLGN | 4.4.1.5 | COFACTOR: Name=Ni(2+); Xref=ChEBI:CHEBI:49786; Evidence={ECO:0000269|PubMed:10913283}; Note=Binds 1 nickel ion per subunit. In the homodimer, two nickel ions are bound between subunits. Is not active with zinc ions. {ECO:0000269|PubMed:10913283}; | methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione [GO:0019243]; response to toxic substance [GO:0009636] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | lactoylglutathione lyase activity [GO:0004462]; nickel cation binding [GO:0016151]; protein homodimerization activity [GO:0042803] | PF00903; | 3.10.180.10; | Glyoxalase I family | null | null | CATALYTIC ACTIVITY: Reaction=(R)-S-lactoylglutathione = glutathione + methylglyoxal; Xref=Rhea:RHEA:19069, ChEBI:CHEBI:17158, ChEBI:CHEBI:57474, ChEBI:CHEBI:57925; EC=4.4.1.5; Evidence={ECO:0000269|PubMed:10913283}; | null | PATHWAY: Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 1/2. {ECO:0000269|PubMed:25670698}. | null | null | FUNCTION: Catalyzes the isomerization of the hemithioacetal formed spontaneously from methylglyoxal and glutathione, to S-lactoylglutathione, which is then hydrolyzed by a type II glyoxalase (GloB or GloC). Is involved in methylglyoxal (MG) detoxification (Probable) (PubMed:10913283). Involved in resistance to hypochlo... | Escherichia coli (strain K12) |
P0AC84 | GLO2_ECOLI | MNLNSIPAFDDNYIWVLNDEAGRCLIVDPGDAEPVLNAIAANNWQPEAIFLTHHHHDHVGGVKELVEKFPQIVVYGPQETQDKGTTQVVKDGETAFVLGHEFSVIATPGHTLGHICYFSKPYLFCGDTLFSGGCGRLFEGTASQMYQSLKKLSALPDDTLVCCAHEYTLSNMKFALSILPHDLSINDYYRKVKELRAKNQITLPVILKNERQINVFLRTEDIDLINVINEETLLQQPEERFAWLRSKKDRF | 3.1.2.6 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:17196158, ECO:0000305|PubMed:25670698}; Note=Binds 2 Zn(2+) ions per subunit. Mn(2+) and Co(2+) can substitute for zinc in reconstitution experiments. {ECO:0000269|PubMed:17196158}; | methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione [GO:0019243]; response to heat [GO:0009408]; response to toxic substance [GO:0009636] | null | hydroxyacylglutathione hydrolase activity [GO:0004416]; zinc ion binding [GO:0008270] | PF16123;PF00753; | 3.60.15.10; | Metallo-beta-lactamase superfamily, Glyoxalase II family | null | null | CATALYTIC ACTIVITY: Reaction=an S-(2-hydroxyacyl)glutathione + H2O = a 2-hydroxy carboxylate + glutathione + H(+); Xref=Rhea:RHEA:21864, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57925, ChEBI:CHEBI:58896, ChEBI:CHEBI:71261; EC=3.1.2.6; Evidence={ECO:0000269|PubMed:17196158, ECO:0000269|PubMed:25670698}; CATALYT... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=184 uM for (R)-S-lactoylglutathione {ECO:0000269|PubMed:17196158}; KM=0.5 mM for (R)-S-lactoylglutathione {ECO:0000269|PubMed:25670698}; Vmax=112 umol/min/mg enzyme for the hydrolysis of (R)-S-lactoylglutathione {ECO:0000269|PubMed:17196158}; Note=kcat is 53 sec(-1... | PATHWAY: Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 2/2. {ECO:0000269|PubMed:25670698}. | null | null | FUNCTION: Type II glyoxalase that catalyzes the hydrolysis of (R)-S-lactoylglutathione to (R)-lactate and glutathione (PubMed:17196158, PubMed:25670698). Is more efficient than the isozyme GloC, and plays a major contribution to methylglyoxal (MG) detoxification in E.coli (PubMed:25670698). The two isoenzymes have addi... | Escherichia coli (strain K12) |
P0AC88 | GM4D_ECOLI | MSKVALITGVTGQDGSYLAEFLLEKGYEVHGIKRRASSFNTERVDHIYQDPHTCNPKFHLHYGDLSDTSNLTRILREVQPDEVYNLGAMSHVAVSFESPEYTADVDAMGTLRLLEAIRFLGLEKKTRFYQASTSELYGLVQEIPQKETTPFYPRSPYAVAKLYAYWITVNYRESYGMYACNGILFNHESPRRGETFVTRKITRAIANIAQGLESCLYLGNMDSLRDWGHAKDYVKMQWMMLQQEQPEDFVIATGVQYSVRQFVEMAAAQLGIKLRFEGTGVEEKGIVVSVTGHDAPGVKPGDVIIAVDPRYFRPAEVETL... | 4.2.1.47 | COFACTOR: Name=NADP(+); Xref=ChEBI:CHEBI:58349; Evidence={ECO:0000255|HAMAP-Rule:MF_00955, ECO:0000269|PubMed:10673432, ECO:0000269|PubMed:9257704}; | 'de novo' GDP-L-fucose biosynthetic process [GO:0042351]; colanic acid biosynthetic process [GO:0009242]; GDP-mannose metabolic process [GO:0019673] | cytoplasm [GO:0005737] | GDP-mannose 4,6-dehydratase activity [GO:0008446]; NADP+ binding [GO:0070401]; protein homodimerization activity [GO:0042803] | PF16363; | 3.40.50.720;3.90.25.10; | NAD(P)-dependent epimerase/dehydratase family, GDP-mannose 4,6-dehydratase subfamily | null | null | CATALYTIC ACTIVITY: Reaction=GDP-alpha-D-mannose = GDP-4-dehydro-alpha-D-rhamnose + H2O; Xref=Rhea:RHEA:23820, ChEBI:CHEBI:15377, ChEBI:CHEBI:57527, ChEBI:CHEBI:57964; EC=4.2.1.47; Evidence={ECO:0000255|HAMAP-Rule:MF_00955, ECO:0000269|PubMed:9257704}; | null | PATHWAY: Nucleotide-sugar biosynthesis; GDP-L-fucose biosynthesis via de novo pathway; GDP-L-fucose from GDP-alpha-D-mannose: step 1/2. {ECO:0000269|PubMed:9257704}.; PATHWAY: Exopolysaccharide biosynthesis; colanic acid biosynthesis. {ECO:0000269|PubMed:9257704}. | null | null | FUNCTION: Catalyzes the conversion of GDP-D-mannose to GDP-4-dehydro-6-deoxy-D-mannose. {ECO:0000255|HAMAP-Rule:MF_00955, ECO:0000269|PubMed:9257704}. | Escherichia coli (strain K12) |
P0AC98 | SATP_ECOLI | MGNTKLANPAPLGLMGFGMTTILLNLHNVGYFALDGIILAMGIFYGGIAQIFAGLLEYKKGNTFGLTAFTSYGSFWLTLVAILLMPKLGLTDAPNAQFLGVYLGLWGVFTLFMFFGTLKGARVLQFVFFSLTVLFALLAIGNIAGNAAIIHFAGWIGLICGASAIYLAMGEVLNEQFGRTVLPIGESH | null | null | acetate transmembrane transport [GO:0035433]; nitrogen compound transport [GO:0071705]; succinate transmembrane transport [GO:0071422] | plasma membrane [GO:0005886] | acetate:proton symporter activity [GO:0015360] | PF01184; | null | Acetate uptake transporter (AceTr) (TC 2.A.96) family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000269|PubMed:15919996}. | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.24 mM for acetic acid {ECO:0000269|PubMed:23844911}; KM=1.18 mM for succinic acid {ECO:0000269|PubMed:23844911}; Vmax=8.72 nmol/min/mg enzyme with acetic acid as substrate {ECO:0000269|PubMed:23844911}; Vmax=10.05 nmol/min/mg enzyme with succinic acid as substrat... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0. {ECO:0000269|PubMed:23844911}; | null | FUNCTION: Uptake of acetate and succinate. Transport is energetically dependent on the protonmotive force. {ECO:0000269|PubMed:23844911}. | Escherichia coli (strain K12) |
P0ACB0 | DNAB_ECOLI | MAGNKPFNKQQAEPRERDPQVAGLKVPPHSIEAEQSVLGGLMLDNERWDDVAERVVADDFYTRPHRHIFTEMARLQESGSPIDLITLAESLERQGQLDSVGGFAYLAELSKNTPSAANISAYADIVRERAVVREMISVANEIAEAGFDPQGRTSEDLLDLAESRVFKIAESRANKDEGPKNIADVLDATVARIEQLFQQPHDGVTGVNTGYDDLNKKTAGLQPSDLIIVAARPSMGKTTFAMNLVENAAMLQDKPVLIFSLEMPSEQIMMRSLASLSRVDQTKIRTGQLDDEDWARISGTMGILLEKRNIYIDDSSGLTP... | 3.6.4.12 | null | DNA duplex unwinding [GO:0032508]; DNA replication [GO:0006260]; DNA replication initiation [GO:0006270]; DNA replication, synthesis of RNA primer [GO:0006269]; DNA unwinding involved in DNA replication [GO:0006268]; replication fork processing [GO:0031297]; response to ionizing radiation [GO:0010212] | cytosol [GO:0005829]; DNA helicase complex [GO:0033202]; DnaB-DnaC complex [GO:1990100]; DnaB-DnaC-DnaT-PriA-PriB complex [GO:1990158]; DnaB-DnaC-DnaT-PriA-PriC complex [GO:1990159]; DnaB-DnaC-Rep-PriC complex [GO:1990160]; DnaB-DnaG complex [GO:1990156]; primosome complex [GO:1990077]; replisome [GO:0030894] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; DNA helicase activity [GO:0003678]; helicase activity [GO:0004386]; identical protein binding [GO:0042802] | PF00772;PF03796; | 3.40.50.300; | Helicase family, DnaB subfamily | null | null | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; | null | null | null | null | FUNCTION: Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity and contains distinct active sites for ATP binding, DNA binding, and interaction with DnaC protein, primase, and other prepriming proteins.; FUNCTION: Deletion or mutations in this gene were sele... | Escherichia coli (strain K12) |
P0ACB2 | HEM2_ECOLI | MTDLIQRPRRLRKSPALRAMFEETTLSLNDLVLPIFVEEEIDDYKAVEAMPGVMRIPEKHLAREIERIANAGIRSVMTFGISHHTDETGSDAWREDGLVARMSRICKQTVPEMIVMSDTCFCEYTSHGHCGVLCEHGVDNDATLENLGKQAVVAAAAGADFIAPSAAMDGQVQAIRQALDAAGFKDTAIMSYSTKFASSFYGPFREAAGSALKGDRKSYQMNPMNRREAIRESLLDEAQGADCLMVKPAGAYLDIVRELRERTELPIGAYQVSGEYAMIKFAALAGAIDEEKVVLESLGSIKRAGADLIFSYFALDLAEK... | 4.2.1.24 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:10194344, ECO:0000269|PubMed:11444968, ECO:0000269|PubMed:11909869, ECO:0000269|PubMed:7592604, ECO:0000269|PubMed:8439296}; Note=Binds 1 zinc ion per monomer. {ECO:0000269|PubMed:10194344, ECO:0000269|PubMed:11444968, ECO:0000269|PubMed:119098... | heme biosynthetic process [GO:0006783]; protoporphyrinogen IX biosynthetic process [GO:0006782] | cytosol [GO:0005829] | magnesium ion binding [GO:0000287]; porphobilinogen synthase activity [GO:0004655]; zinc ion binding [GO:0008270] | PF00490; | 3.20.20.70; | ALAD family | null | null | CATALYTIC ACTIVITY: Reaction=2 5-aminolevulinate = H(+) + 2 H2O + porphobilinogen; Xref=Rhea:RHEA:24064, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58126, ChEBI:CHEBI:356416; EC=4.2.1.24; Evidence={ECO:0000305|PubMed:8439296}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=800 uM for 5-aminolevulinic acid {ECO:0000269|PubMed:8439296}; | PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5. {ECO:0000269|PubMed:8439296}; | null | FUNCTION: Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen. | Escherichia coli (strain K12) |
P0ACB4 | HEMG_ECOLI | MKTLILFSTRDGQTREIASYLASELKELGIQADVANVHRIEEPQWENYDRVVIGASIRYGHYHSAFQEFVKKHATRLNSMPSAFYSVNLVARKPEKRTPQTNSYARKFLMNSQWRPDRCAVIAGALRYPRYRWYDRFMIKLIMKMSGGETDTRKEVVYTDWEQVANFAREIAHLTDKPTLK | 1.3.5.3 | COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000255|HAMAP-Rule:MF_00853, ECO:0000269|PubMed:20484676, ECO:0000305|PubMed:19583219}; Note=Binds 1 FMN non-covalently per subunit. {ECO:0000255|HAMAP-Rule:MF_00853, ECO:0000269|PubMed:20484676}; | heme B biosynthetic process [GO:0006785]; heme biosynthetic process [GO:0006783]; porphyrin-containing compound biosynthetic process [GO:0006779]; protoporphyrinogen IX biosynthetic process [GO:0006782] | membrane [GO:0016020]; plasma membrane [GO:0005886] | electron transfer activity [GO:0009055]; FMN binding [GO:0010181]; menaquinone-dependent protoporphyrinogen oxidase activity [GO:0070819]; oxygen-dependent protoporphyrinogen oxidase activity [GO:0004729] | PF12724; | 3.40.50.360; | HemG family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_00853, ECO:0000305|PubMed:20484676}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_00853, ECO:0000305|PubMed:20484676}. | CATALYTIC ACTIVITY: Reaction=3 a menaquinone + protoporphyrinogen IX = 3 a menaquinol + protoporphyrin IX; Xref=Rhea:RHEA:27409, Rhea:RHEA-COMP:9537, Rhea:RHEA-COMP:9539, ChEBI:CHEBI:16374, ChEBI:CHEBI:18151, ChEBI:CHEBI:57306, ChEBI:CHEBI:57307; EC=1.3.5.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00853, ECO:0000269|PubMed... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=7 uM for protoporphyrinogen IX {ECO:0000269|PubMed:19583219}; KM=3.76 uM for menadione (a soluble menaquinone analog) {ECO:0000269|PubMed:19583219}; KM=17.3 uM for menaquinone {ECO:0000269|PubMed:20484676}; Vmax=960 umol/h/mg enzyme {ECO:0000269|PubMed:20484676}; N... | PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; protoporphyrin-IX from protoporphyrinogen-IX: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00853, ECO:0000305|PubMed:19583219, ECO:0000305|PubMed:7916647}. | null | null | FUNCTION: Catalyzes the 6-electron oxidation of protoporphyrinogen IX to form protoporphyrin IX; under anaerobic conditions uses menaquinone as an electron acceptor, under aerobic condition uses ubiquinone as an electron acceptor. {ECO:0000255|HAMAP-Rule:MF_00853}.; FUNCTION: Anaerobically in vitro transfers electrons ... | Escherichia coli (strain K12) |
P0ACC1 | PRMC_ECOLI | MEYQHWLREAISQLQASESPRRDAEILLEHVTGRGRTFILAFGETQLTDEQCQQLDALLTRRRDGEPIAHLTGVREFWSLPLFVSPATLIPRPDTECLVEQALARLPEQPCRILDLGTGTGAIALALASERPDCEIIAVDRMPDAVSLAQRNAQHLAIKNIHILQSDWFSALAGQQFAMIVSNPPYIDEQDPHLQQGDVRFEPLTALVAADSGMADIVHIIEQSRNALVSGGFLLLEHGWQQGEAVRQAFILAGYHDVETCRDYGDNERVTLGRYYQ | 2.1.1.297 | null | peptidyl-glutamine methylation [GO:0018364]; protein methylation [GO:0006479]; regulation of gene expression [GO:0010468]; translational termination [GO:0006415] | null | nucleic acid binding [GO:0003676]; protein methyltransferase activity [GO:0008276]; protein-(glutamine-N5) methyltransferase activity [GO:0102559]; protein-glutamine N-methyltransferase activity [GO:0036009]; S-adenosylmethionine-dependent methyltransferase activity [GO:0008757] | PF05175;PF17827; | 1.10.8.10;3.40.50.150; | Protein N5-glutamine methyltransferase family, PrmC subfamily | null | null | CATALYTIC ACTIVITY: Reaction=L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:42896, Rhea:RHEA-COMP:10271, Rhea:RHEA-COMP:10272, ChEBI:CHEBI:15378, ChEBI:CHEBI:30011, ChEBI:CHEBI:57856, ChEB... | null | null | null | null | FUNCTION: Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif, i.e. on 'Gln-235' in RF1 and on 'Gln-252' in RF2. {ECO:0000269|PubMed:11805295, ECO:0000269|PubMed:11847124, ECO:0000269|PubMed:16364916}. | Escherichia coli (strain K12) |
P0ACC3 | ERPA_ECOLI | MSDDVALPLEFTDAAANKVKSLIADEDNPNLKLRVYITGGGCSGFQYGFTFDDQVNEGDMTIEKQGVGLVVDPMSLQYLVGGSVDYTEGLEGSRFIVTNPNAKSTCGCGSSFSI | null | COFACTOR: Name=iron-sulfur cluster; Xref=ChEBI:CHEBI:30408; Evidence={ECO:0000269|PubMed:17698959}; Note=Binds 1 iron-sulfur cluster per subunit. A study found 40-50% as [2Fe-2S] clusters, 15-25% as [4Fe-4S] clusters and the rest as paramagnetic iron. {ECO:0000269|PubMed:17698959}; | aerobic respiration [GO:0009060]; anaerobic respiration [GO:0009061]; iron-sulfur cluster assembly [GO:0016226]; protein maturation [GO:0051604]; protein maturation by [4Fe-4S] cluster transfer [GO:0106035] | cytosol [GO:0005829] | 2 iron, 2 sulfur cluster binding [GO:0051537]; 4 iron, 4 sulfur cluster binding [GO:0051539]; iron ion binding [GO:0005506] | PF01521; | 2.60.300.12; | HesB/IscA family | null | null | null | null | null | null | null | FUNCTION: Probably involved in the insertion of Fe-S clusters into apoproteins in vivo including IspG and/or IspH. Essential for growth under aerobic conditions and for anaerobic respiration but not for fermentation. In vitro it binds Fe-S clusters and transfers them to apo-IspG, which is involved in quinone biosynthes... | Escherichia coli (strain K12) |
P0ACC7 | GLMU_ECOLI | MLNNAMSVVILAAGKGTRMYSDLPKVLHTLAGKAMVQHVIDAANELGAAHVHLVYGHGGDLLKQALKDDNLNWVLQAEQLGTGHAMQQAAPFFADDEDILMLYGDVPLISVETLQRLRDAKPQGGIGLLTVKLDDPTGYGRITRENGKVTGIVEHKDATDEQRQIQEINTGILIANGADMKRWLAKLTNNNAQGEYYITDIIALAYQEGREIVAVHPQRLSEVEGVNNRLQLSRLERVYQSEQAEKLLLAGVMLRDPARFDLRGTLTHGRDVEIDTNVIIEGNVTLGHRVKIGTGCVIKNSVIGDDCEISPYTVVEDANL... | 2.3.1.157; 2.7.7.23 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:17473010}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000269|PubMed:11329257}; Note=Binds 1 Mg(2+) ion per subunit (PubMed:17473010). Can also use Co(2+) ion to a lesser extent (PubMed:11329257). {ECO:0000269|PubMed:11329257, ECO:00002... | cell morphogenesis [GO:0000902]; cell wall organization [GO:0071555]; lipid A biosynthetic process [GO:0009245]; peptidoglycan biosynthetic process [GO:0009252]; regulation of cell shape [GO:0008360]; UDP-N-acetylglucosamine biosynthetic process [GO:0006048] | cytosol [GO:0005829] | glucosamine-1-phosphate N-acetyltransferase activity [GO:0019134]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; UDP-N-acetylglucosamine diphosphorylase activity [GO:0003977] | PF00132;PF12804; | 2.160.10.10; | N-acetylglucosamine-1-phosphate uridyltransferase family; Transferase hexapeptide repeat family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01631, ECO:0000269|PubMed:10428949}. | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate; Xref=Rhea:RHEA:13725, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57776, ChEBI:CHEBI:58516; EC=2.3.1.157; Evidence={ECO:0000255|HAMAP-Rule:MF_01631, ECO:0000269|Pub... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.018 mM for N-acetylglucosamine 1-phosphate {ECO:0000269|PubMed:8083170, ECO:0000269|PubMed:8555230, ECO:0000269|PubMed:9733680}; KM=0.07 mM for alpha-D-glucosamine 1-phosphate {ECO:0000269|PubMed:10428949}; KM=0.1 mM for UTP {ECO:0000269|PubMed:10428949}; KM=0.15... | PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II): step 2/2. {ECO:0000255|HAMAP-Rule:MF_01631}.; PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; UDP-N-acet... | null | null | FUNCTION: Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is ... | Escherichia coli (strain K12) |
P0ACD4 | ISCU_ECOLI | MAYSEKVIDHYENPRNVGSFDNNDENVGSGMVGAPACGDVMKLQIKVNDEGIIEDARFKTYGCGSAIASSSLVTEWVKGKSLDEAQAIKNTDIAEELELPPVKIHCSILAEDAIKAAIADYKSKREAK | null | null | intracellular iron ion homeostasis [GO:0006879]; iron-sulfur cluster assembly [GO:0016226]; L-cysteine catabolic process [GO:0019448] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; IscS-IscU complex [GO:1990330] | 2 iron, 2 sulfur cluster binding [GO:0051537]; 4 iron, 4 sulfur cluster binding [GO:0051539]; copper ion binding [GO:0005507]; ferrous iron binding [GO:0008198]; identical protein binding [GO:0042802]; zinc ion binding [GO:0008270] | PF01592; | 3.90.1010.10; | NifU family | null | null | null | null | null | null | null | FUNCTION: A scaffold on which IscS assembles Fe-S clusters. Exists as 2 interconverting forms, a structured (S) and disordered (D) form. The D-state is the preferred substrate for IscS. Converts to the S-state when an Fe-S cluster is assembled, which helps it dissociate from IscS to transfer the Fe-S to an acceptor. It... | Escherichia coli (strain K12) |
P0ACD8 | MBHL_ECOLI | MSTQYETQGYTINNAGRRLVVDPITRIEGHMRCEVNINDQNVITNAVSCGTMFRGLEIILQGRDPRDAWAFVERICGVCTGVHALASVYAIEDAIGIKVPDNANIIRNIMLATLWCHDHLVHFYQLAGMDWIDVLDALKADPRKTSELAQSLSSWPKSSPGYFFDVQNRLKKFVEGGQLGIFRNGYWGHPQYKLPPEANLMGFAHYLEALDFQREIVKIHAVFGGKNPHPNWIVGGMPCAINIDESGAVGAVNMERLNLVQSIITRTADFINNVMIPDALAIGQFNKPWSEIGTGLSDKCVLSYGAFPDIANDFGEKSLL... | 1.12.99.6 | COFACTOR: Name=Ni(2+); Xref=ChEBI:CHEBI:49786; Evidence={ECO:0000250}; Note=Binds 1 nickel ion per subunit. {ECO:0000250}; | anaerobic electron transport chain [GO:0019645]; anaerobic respiration [GO:0009061]; cellular response to starvation [GO:0009267]; fermentation [GO:0006113]; hydrogen metabolic process [GO:1902421] | [Ni-Fe] hydrogenase complex [GO:0044569]; membrane [GO:0016020]; outer membrane-bounded periplasmic space [GO:0030288]; periplasmic side of plasma membrane [GO:0098567] | electron transfer activity [GO:0009055]; ferredoxin hydrogenase activity [GO:0008901]; hydrogenase (acceptor) activity [GO:0033748]; nickel cation binding [GO:0016151] | PF00374; | 1.10.645.10; | [NiFe]/[NiFeSe] hydrogenase large subunit family | null | SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. | CATALYTIC ACTIVITY: Reaction=A + H2 = AH2; Xref=Rhea:RHEA:12116, ChEBI:CHEBI:13193, ChEBI:CHEBI:17499, ChEBI:CHEBI:18276; EC=1.12.99.6; | null | null | null | null | FUNCTION: This is one of three E.coli hydrogenases synthesized in response to different physiological conditions. HYD1 is believed to have a role in hydrogen cycling during fermentative growth. | Escherichia coli (strain K12) |
P0ACE0 | MBHM_ECOLI | MSQRITIDPVTRIEGHLRIDCEIENGVVSKAWASGTMWRGMEEIVKNRDPRDAWMIVQRICGVCTTTHALSSVRAAESALNIDVPVNAQYIRNIILAAHTTHDHIVHFYQLSALDWVDITSALQADPTKASEMLKGVSTWHLNSPEEFTKVQNKIKDLVASGQLGIFANGYWGHPAMKLPPEVNLIAVAHYLQALECQRDANRVVALLGGKTPHIQNLAVGGVANPINLDGLGVLNLERLMYIKSFIDKLSDFVEQVYKVDTAVIAAFYPEWLTRGKGAVNYLSVPEFPTDSKNGSFLFPGGYIENADLSSYRPITSHSD... | 1.12.99.6 | COFACTOR: Name=Ni(2+); Xref=ChEBI:CHEBI:49786; Evidence={ECO:0000250}; Note=Binds 1 nickel ion per subunit. {ECO:0000250}; | null | plasma membrane [GO:0005886] | ferredoxin hydrogenase activity [GO:0008901]; hydrogenase (acceptor) activity [GO:0033748]; nickel cation binding [GO:0016151] | PF00374; | 1.10.645.10; | [NiFe]/[NiFeSe] hydrogenase large subunit family | null | SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. | CATALYTIC ACTIVITY: Reaction=A + H2 = AH2; Xref=Rhea:RHEA:12116, ChEBI:CHEBI:13193, ChEBI:CHEBI:17499, ChEBI:CHEBI:18276; EC=1.12.99.6; | null | null | null | null | FUNCTION: This is one of three E.coli hydrogenases synthesized in response to different physiological conditions. HYD2 is involved in hydrogen uptake. | Escherichia coli (strain K12) |
P0ACE3 | HHA_ECOLI | MSEKPLTKTDYLMRLRRCQTIDTLERVIEKNKYELSDNELAVFYSAADHRLAELTMNKLYDKIPSSVWKFIR | null | null | regulation of DNA-templated transcription [GO:0006355]; regulation of gene expression [GO:0010468] | cytosol [GO:0005829]; H-NS-Hha complex [GO:0097495]; transcription regulator complex [GO:0005667] | DNA binding [GO:0003677] | PF05321; | 1.20.1280.40; | Hha/YmoA/Cnu family | null | null | null | null | null | null | null | FUNCTION: Down-regulates hemolysin (hly) expression in complex with H-NS (PubMed:10778755, PubMed:11790731, PubMed:1956303, PubMed:21600204). Stimulates transposition events in vivo (PubMed:8145648). Modifies the set of genes regulated by H-NS; Hha and Cnu (YdgT) increase the number of genes DNA bound by H-NS/StpA and ... | Escherichia coli (strain K12) |
P0ACE7 | HINT_ECOLI | MAEETIFSKIIRREIPSDIVYQDDLVTAFRDISPQAPTHILIIPNILIPTVNDVSAEHEQALGRMITVAAKIAEQEGIAEDGYRLIMNTNRHGGQEVYHIHMHLLGGRPLGPMLAHKGL | 3.9.1.- | null | D-alanine catabolic process [GO:0055130] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | adenosine 5'-monophosphoramidase activity [GO:0043530]; nucleotide binding [GO:0000166]; protein homodimerization activity [GO:0042803] | PF01230; | 3.30.428.10; | HINT family | null | null | null | null | null | null | null | FUNCTION: Hydrolyzes purine nucleotide phosphoramidates, including adenosine 5'monophosphoramidate (AMP-NH2), adenosine 5'monophosphomorpholidate (AMP-morpholidate), guanosine 5'monophosphomorpholidate (GMP-morpholidate) and tryptamine 5'guanosine monophosphate (TpGd) (PubMed:15703176, PubMed:20934431). Hydrolyzes lysy... | Escherichia coli (strain K12) |
P0ACF0 | DBHA_ECOLI | MNKTQLIDVIAEKAELSKTQAKAALESTLAAITESLKEGDAVQLVGFGTFKVNHRAERTGRNPQTGKEIKIAAANVPAFVSGKALKDAVK | null | null | bacterial nucleoid packaging [GO:0036386]; chromosome condensation [GO:0030261]; DNA damage response [GO:0006974]; DNA repair [GO:0006281]; DNA replication initiation [GO:0006270]; DNA-templated transcription [GO:0006351] | cytosol [GO:0005829]; DnaA-HU complex [GO:1990103]; HU-DNA complex [GO:1990178]; membrane [GO:0016020] | DNA binding [GO:0003677]; identical protein binding [GO:0042802]; structural constituent of chromatin [GO:0030527] | PF00216; | 4.10.520.10; | Bacterial histone-like protein family | null | SUBCELLULAR LOCATION: Cytoplasm, nucleoid {ECO:0000269|PubMed:21903814}. Note=Scattered throughout the nucleoid (PubMed:21903814). {ECO:0000269|PubMed:21903814}. | null | null | null | null | null | FUNCTION: Histone-like DNA-binding protein which is capable of wrapping DNA to stabilize it, and thus to prevent its denaturation under extreme environmental conditions. {ECO:0000305|PubMed:24916461}. | Escherichia coli (strain K12) |
P0ACF4 | DBHB_ECOLI | MNKSQLIDKIAAGADISKAAAGRALDAIIASVTESLKEGDDVALVGFGTFAVKERAARTGRNPQTGKEITIAAAKVPSFRAGKALKDAVN | null | null | bacterial nucleoid packaging [GO:0036386]; chromosome condensation [GO:0030261]; DNA repair [GO:0006281]; DNA replication initiation [GO:0006270]; DNA-templated transcription [GO:0006351] | cytosol [GO:0005829]; DnaA-HU complex [GO:1990103]; HU-DNA complex [GO:1990178] | DNA binding [GO:0003677]; identical protein binding [GO:0042802]; structural constituent of chromatin [GO:0030527] | PF00216; | 4.10.520.10; | Bacterial histone-like protein family | null | null | null | null | null | null | null | FUNCTION: Histone-like DNA-binding protein which is capable of wrapping DNA to stabilize it, and thus to prevent its denaturation under extreme environmental conditions. {ECO:0000305|PubMed:24916461}. | Escherichia coli (strain K12) |
P0ACF8 | HNS_ECOLI | MSEALKILNNIRTLRAQARECTLETLEEMLEKLEVVVNERREEESAAAAEVEERTRKLQQYREMLIADGIDPNELLNSLAAVKSGTKAKRAQRPAKYSYVDENGETKTWTGQGRTPAVIKKAMDEQGKSLDDFLIKQ | null | null | bacterial nucleoid packaging [GO:0036386]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of single-species biofilm formation on inanimate substrate [GO:1900232]; regulation of DNA-templated transcription [GO:0006355]; regulation of translation [GO:0006417] | cytosol [GO:0005829]; H-NS complex [GO:1990121]; H-NS-Cnu complex [GO:0036411]; H-NS-Hha complex [GO:0097495]; membrane [GO:0016020]; protein-DNA complex [GO:0032993]; transcription regulator complex [GO:0005667] | bent DNA binding [GO:0003681]; DNA-binding transcription repressor activity [GO:0001217]; identical protein binding [GO:0042802]; minor groove of adenine-thymine-rich DNA binding [GO:0003680]; protein dimerization activity [GO:0046983]; RNA binding [GO:0003723]; structural constituent of chromatin [GO:0030527]; transcr... | PF00816; | 1.10.287.1050;4.10.430.10; | Histone-like protein H-NS family | PTM: 2-hydroxyisobutyrylated by TmcA on Lys-121. {ECO:0000269|PubMed:34903851}.; PTM: Cells (strain MRE-600) in mid-exponential phase have three 15.5 kDa proteins with 3 different isoelectric points; the major form (H1a, pI 7.5) rises in concentration during growth while the 2 minor forms (H1b, pI about 7.2 and H1c, pI... | SUBCELLULAR LOCATION: Cytoplasm, nucleoid {ECO:0000269|PubMed:21903814, ECO:0000269|PubMed:333393}. Note=Forms 2 compact clusters per chromosome, located at one-quarter and three-quarter positions on the cell's long axis: 2 H-NS-repressed genes were closely associated with H-NS clusters while a non-H-NS-repressed gene ... | null | null | null | null | null | FUNCTION: A DNA-binding protein implicated in transcriptional repression (silencing) (PubMed:16963779, PubMed:17046956, PubMed:2128918, PubMed:23543115, PubMed:333393, PubMed:8890170, PubMed:8913298, PubMed:9398522). Also involved in bacterial chromosome organization and compaction (PubMed:10982869, PubMed:21903814, Pu... | Escherichia coli (strain K12) |
P0ACG1 | STPA_ECOLI | MSVMLQSLNNIRTLRAMAREFSIDVLEEMLEKFRVVTKERREEEEQQQRELAERQEKISTWLELMKADGINPEELLGNSSAAAPRAGKKRQPRPAKYKFTDVNGETKTWTGQGRTPKPIAQALAEGKSLDDFLI | null | null | null | cytosol [GO:0005829]; nucleoid [GO:0009295]; protein-DNA complex [GO:0032993] | bent DNA binding [GO:0003681]; DNA binding [GO:0003677]; DNA-binding transcription repressor activity [GO:0001217]; minor groove of adenine-thymine-rich DNA binding [GO:0003680]; protein dimerization activity [GO:0046983]; RNA binding [GO:0003723]; structural constituent of chromatin [GO:0030527]; transcription cis-reg... | PF00816; | 1.10.287.1050;4.10.430.10; | Histone-like protein H-NS family | null | SUBCELLULAR LOCATION: Cytoplasm, nucleoid {ECO:0000269|PubMed:21903814}. Note=Scattered throughout the nucleoid (PubMed:21903814). {ECO:0000269|PubMed:21903814}. | null | null | null | null | null | FUNCTION: A DNA-binding protein that acts in a fashion similar to H-NS protein upon overexpression, represses a number of genes including the cryptic blg operon, hns, papB and the proU locus (PubMed:8890170). A subset of H-NS/StpA-regulated genes also require Hha for repression; Hha and Cnu (YdgT) increases the number ... | Escherichia coli (strain K12) |
P0ACG8 | HSLR_ECOLI | MKEKPAVEVRLDKWLWAARFYKTRALAREMIEGGKVHYNGQRSKPSKIVELNATLTLRQGNDERTVIVKAITEQRRPASEAALLYEETAESVEKREKMALARKLNALTMPHPDRRPDKKERRDLLRFKHGDSE | null | null | cellular response to heat [GO:0034605]; response to heat [GO:0009408] | cytosol [GO:0005829] | DNA binding [GO:0003677]; ribosomal large subunit binding [GO:0043023]; single-stranded RNA binding [GO:0003727] | PF01479; | 3.10.290.10; | HSP15 family | null | null | null | null | null | null | null | FUNCTION: Involved in the recycling of free 50S ribosomal subunits that still carry a nascent chain. Binds RNA more specifically than DNA. Binds with very high affinity to the free 50S ribosomal subunit. Does not bind it when it is part of the 70S ribosome. | Escherichia coli (strain K12) |
P0ACJ0 | LRP_ECOLI | MVDSKKRPGKDLDRIDRNILNELQKDGRISNVELSKRVGLSPTPCLERVRRLERQGFIQGYTALLNPHYLDASLLVFVEITLNRGAPDVFEQFNTAVQKLEEIQECHLVSGDFDYLLKTRVPDMSAYRKLLGETLLRLPGVNDTRTYVVMEEVKQSNRLVIKTR | null | null | alanine catabolic process [GO:0006524]; negative regulation of DNA-templated transcription [GO:0045892]; regulation of DNA-templated transcription [GO:0006355]; response to leucine [GO:0043201] | cytosol [GO:0005829]; protein-DNA complex [GO:0032993] | DNA-binding transcription activator activity [GO:0001216]; DNA-binding transcription repressor activity [GO:0001217]; identical protein binding [GO:0042802]; sequence-specific DNA binding [GO:0043565]; transcription cis-regulatory region binding [GO:0000976] | PF01037;PF13412; | 3.30.70.920;1.10.10.10; | null | null | null | null | null | null | null | null | FUNCTION: Mediates a global response to leucine. Exogenous leucine affects the expression of a number of different operons; lrp mediates this effect for at least some of these operons. For example it is regulator of the branched-chain amino acid transport genes. | Escherichia coli (strain K12) |
P0ACJ8 | CRP_ECOLI | MVLGKPQTDPTLEWFLSHCHIHKYPSKSTLIHQGEKAETLYYIVKGSVAVLIKDEEGKEMILSYLNQGDFIGELGLFEEGQERSAWVRAKTACEVAEISYKKFRQLIQVNPDILMRLSAQMARRLQVTSEKVGNLAFLDVTGRIAQTLLNLAKQPDAMTHPDGMQIKITRQEIGQIVGCSRETVGRILKMLEDQNLISAHGKTIVVYGTR | null | null | carbon catabolite repression of transcription [GO:0045013]; DNA-templated transcription [GO:0006351]; negative regulation of DNA-templated transcription [GO:0045892]; positive regulation of DNA-templated transcription [GO:0045893] | cytosol [GO:0005829]; protein-DNA complex [GO:0032993] | cAMP binding [GO:0030552]; DNA binding, bending [GO:0008301]; DNA-binding transcription factor activity [GO:0003700]; identical protein binding [GO:0042802]; minor groove of adenine-thymine-rich DNA binding [GO:0003680]; sequence-specific DNA binding [GO:0043565] | PF00027;PF13545; | 2.60.120.10;1.10.10.10; | null | null | null | null | null | null | null | null | FUNCTION: A global transcription regulator, which plays a major role in carbon catabolite repression (CCR) as well as other processes. Binds cyclic AMP (cAMP) which allosterically activates DNA binding (to consensus sequence 5'-AAATGTGATCTAGATCACATTT-3') to directly regulate the transcription of about 300 genes in abou... | Escherichia coli (strain K12) |
P0ACN4 | ALLR_ECOLI | MTEVRRRGRPGQAEPVAQKGAQALERGIAILQYLEKSGGSSSVSDISLNLDLPLSTTFRLLKVLQAADFVYQDSQLGWWHIGLGVFNVGAAYIHNRDVLSVAGPFMRRLMLLSGETVNVAIRNGNEAVLIGQLECKSMVRMCAPLGSRLPLHASGAGKALLYPLAEEELMSIILQTGLQQFTPTTLVDMPTLLKDLEQARELGYTVDKEEHVVGLNCIASAIYDDVGSVVAAISISGPSSRLTEDRFVSQGELVRDTARDISTALGLKAHP | null | null | DNA damage response [GO:0006974]; negative regulation of DNA-templated transcription [GO:0045892] | cytosol [GO:0005829] | DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; identical protein binding [GO:0042802] | PF09339;PF01614; | 3.30.450.40;1.10.10.10; | null | null | null | null | null | null | null | null | FUNCTION: Negative regulator of allantoin and glyoxylate utilization operons. Binds to the gcl promoter and to the allS-allA intergenic region. Binding to DNA is abolished by glyoxylate. {ECO:0000269|PubMed:10601204, ECO:0000269|PubMed:12460564, ECO:0000269|PubMed:16546208}. | Escherichia coli (strain K12) |
P0ACP7 | PURR_ECOLI | MATIKDVAKRANVSTTTVSHVINKTRFVAEETRNAVWAAIKELHYSPSAVARSLKVNHTKSIGLLATSSEAAYFAEIIEAVEKNCFQKGYTLILGNAWNNLEKQRAYLSMMAQKRVDGLLVMCSEYPEPLLAMLEEYRHIPMVVMDWGEAKADFTDAVIDNAFEGGYMAGRYLIERGHREIGVIPGPLERNTGAGRLAGFMKAMEEAMIKVPESWIVQGDFEPESGYRAMQQILSQPHRPTAVFCGGDIMAMGALCAADEMGLRVPQDVSLIGYDNVRNARYFTPALTTIHQPKDSLGETAFNMLLDRIVNKREEPQSIE... | null | null | negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of purine nucleotide biosynthetic process [GO:1900372]; purine nucleotide biosynthetic process [GO:0006164]; regulation of DNA-templated transcription [GO:0006355] | cytosol [GO:0005829] | DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription repressor activity [GO:0001217]; guanine binding [GO:0002057]; protein homodimerization activity [GO:0042803]; transcription cis-regulatory region binding [GO:0000976] | PF00356;PF13377; | 3.40.50.2300;1.10.260.40; | null | null | null | null | null | PATHWAY: Purine metabolism; purine nucleotide biosynthesis [regulation]. | null | null | FUNCTION: Is the main repressor of the genes involved in the de novo synthesis of purine nucleotides, regulating purB, purC, purEK, purF, purHD, purL, purMN and guaBA expression. In addition, it participates in the regulation or coregulation of genes involved in de novo pyrimidine nucleotide biosynthesis, salvage and u... | Escherichia coli (strain K12) |
P0ACQ4 | OXYR_ECOLI | MNIRDLEYLVALAEHRHFRRAADSCHVSQPTLSGQIRKLEDELGVMLLERTSRKVLFTQAGMLLVDQARTVLREVKVLKEMASQQGETMSGPLHIGLIPTVGPYLLPHIIPMLHQTFPKLEMYLHEAQTHQLLAQLDSGKLDCVILALVKESEAFIEVPLFDEPMLLAIYEDHPWANRECVPMADLAGEKLLMLEDGHCLRDQAMGFCFEAGADEDTHFRATSLETLRNMVAAGSGITLLPALAVPPERKRDGVVYLPCIKPEPRRTIGLVYRPGSPLRSRYEQLAEAIRARMDGHFDKVLKQAV | null | null | DNA damage response [GO:0006974]; regulation of DNA-templated transcription [GO:0006355]; regulation of DNA-templated transcription initiation [GO:2000142]; response to nitrosative stress [GO:0051409]; response to oxidative stress [GO:0006979] | cytosol [GO:0005829]; protein-DNA complex [GO:0032993] | cis-regulatory region sequence-specific DNA binding [GO:0000987]; DNA-binding transcription factor activity [GO:0003700] | PF00126;PF03466; | 3.40.190.10;1.10.10.10; | LysR transcriptional regulatory family | PTM: Disulfide bond formation between Cys-199 and Cys-208 significantly rearranges the secondary structure of the protein and activates it (PubMed:11301006). The reduced and oxidized homodimers have different forms which may alter oligomerization and interaction with DNA (PubMed:11301006). {ECO:0000269|PubMed:11301006,... | null | null | null | null | null | null | FUNCTION: Hydrogen peroxide (H2O2) sensor. Activates the expression of a regulon of H2O2-inducible genes such as katG, gor, ahpC, ahpF, oxyS (a regulatory RNA), dps, fur and grxA in response to H2O2. Represses transcription of phage Mu mom gene in a methylation-sensitive manner; MomR binds to the mom promoter when it i... | Escherichia coli (strain K12) |
P0ACV0 | LPXL_ECOLI | MTNLPKFSTALLHPRYWLTWLGIGVLWLVVQLPYPVIYRLGCGLGKLALRFMKRRAKIVHRNLELCFPEMSEQERRKMVVKNFESVGMGLMETGMAWFWPDRRIARWTEVIGMEHIRDVQAQKRGILLVGIHFLTLELGARQFGMQEPGIGVYRPNDNPLIDWLQTWGRLRSNKSMLDRKDLKGMIKALKKGEVVWYAPDHDYGPRSSVFVPLFAVEQAATTTGTWMLARMSGACLVPFVPRRKPDGKGYQLIMLPPECSPPLDDAETTAAWMNKVVEKCIMMAPEQYMWLHRRFKTRPEGVPSRY | 2.3.1.241 | null | Kdo2-lipid A biosynthetic process [GO:0036104]; lipid A biosynthetic process [GO:0009245]; lipopolysaccharide biosynthetic process [GO:0009103] | membrane [GO:0016020]; plasma membrane [GO:0005886] | lauroyltransferase activity [GO:0008913]; transferase activity [GO:0016740] | PF03279; | null | LpxL/LpxM/LpxP family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_01942, ECO:0000269|PubMed:1846149, ECO:0000269|PubMed:18656959, ECO:0000269|PubMed:8662613}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01942}. | CATALYTIC ACTIVITY: Reaction=alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA (E. coli) + dodecanoyl-[ACP] = alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-(dodecanoyl)-lipid IVA (E. coli) + holo-[ACP]; Xref=Rhea:RHEA:28442, Rhea:RHEA-COMP:9644, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:60365, ChEBI:CHEBI:61524, ChEBI:CHEBI:64479, ChEBI:CHEBI:65... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=7 uM for lauroyl-ACP {ECO:0000269|PubMed:18656959}; KM=15 uM for Kdo(2)-lipid IV(A) {ECO:0000269|PubMed:18656959}; Vmax=95 umol/min/mg enzyme toward lauroyl-ACP {ECO:0000269|PubMed:18656959}; Vmax=221 umol/min/mg enzyme toward Kdo(2)-lipid IV(A) {ECO:0000269|PubMed... | PATHWAY: Glycolipid biosynthesis; KDO(2)-lipid A biosynthesis; KDO(2)-lipid A from CMP-3-deoxy-D-manno-octulosonate and lipid IV(A): step 3/4. {ECO:0000255|HAMAP-Rule:MF_01942, ECO:0000269|PubMed:18656959, ECO:0000269|PubMed:2203778, ECO:0000269|PubMed:8662613}.; PATHWAY: Bacterial outer membrane biogenesis; lipopolysa... | null | null | FUNCTION: Catalyzes the transfer of laurate from lauroyl-[acyl-carrier-protein] (ACP) to Kdo(2)-lipid IV(A) to form Kdo(2)-(lauroyl)-lipid IV(A). Has 10 fold selectivity for lauroyl-ACP over myristoyl-ACP. In vitro, can also catalyze a slow second acylation reaction leading to the formation of Kdo(2)-(dilauroyl)-lipid ... | Escherichia coli (strain K12) |
P0ACV6 | MPAA_ECOLI | MTVTRPRAERGAFPPGTEHYGRSLLGAPLIWFPAPAASRESGLILAGTHGDENSSVVTLSCALRTLTPSLRRHHVVLCVNPDGCQLGLRANANGVDLNRNFPAANWKEGETVYRWNSAAEERDVVLLTGDKPGSEPETQALCQLIHRIQPAWVVSFHDPLACIEDPRHSELGEWLAQAFELPLVTSVGYETPGSFGSWCADLNLHCITAEFPPISSDEASEKYLFAMANLLRWHPKDAIRPS | 3.4.17.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_02211, ECO:0000269|PubMed:22970852}; Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_02211, ECO:0000269|PubMed:22970852}; | cell wall macromolecule catabolic process [GO:0016998]; cell wall organization [GO:0071555]; glycopeptide catabolic process [GO:0009050]; peptidoglycan catabolic process [GO:0009253]; proteolysis [GO:0006508] | cytoplasm [GO:0005737] | amidase activity [GO:0004040]; murein tripeptide carboxypeptidase activity [GO:0061473]; protein homodimerization activity [GO:0042803]; zinc ion binding [GO:0008270] | PF00246; | 3.40.630.10; | Peptidase M14 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02211, ECO:0000305|PubMed:12511517}. | CATALYTIC ACTIVITY: Reaction=H2O + L-alanyl-gamma-D-glutamyl-meso-diaminoheptanedioate = L-alanyl-D-glutamate + meso-2,6-diaminoheptanedioate; Xref=Rhea:RHEA:28398, ChEBI:CHEBI:15377, ChEBI:CHEBI:57791, ChEBI:CHEBI:61395, ChEBI:CHEBI:61401; Evidence={ECO:0000255|HAMAP-Rule:MF_02211, ECO:0000269|PubMed:12511517, ECO:000... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.41 mM for L-alanyl-gamma-D-glutamyl-meso-diaminopimelic acid {ECO:0000269|PubMed:22970852}; Note=kcat is 38.3 sec(-1). {ECO:0000269|PubMed:22970852}; | PATHWAY: Cell wall degradation; peptidoglycan degradation. {ECO:0000255|HAMAP-Rule:MF_02211, ECO:0000305|PubMed:22970852}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|PubMed:22970852}; | null | FUNCTION: Involved in muropeptide degradation. Catalyzes the hydrolysis of the gamma-D-glutamyl-diaminopimelic acid (gamma-D-Glu-Dap) amide bond in the murein tripeptide L-alanyl-gamma-D-glutamyl-meso-diaminopimelic acid, leading to the formation of L-Ala-gamma-D-Glu and Dap (PubMed:12511517, PubMed:22970852). Has weak... | Escherichia coli (strain K12) |
P0AD14 | BTSS_ECOLI | MYDFNLVLLLLQQMCVFLVIAWLMSKTPLFIPLMQVTVRLPHKFLCYIVFSIFCIMGTWFGLHIDDSIANTRAIGAVMGGLLGGPVVGGLVGLTGGLHRYSMGGMTALSCMISTIVEGLLGGLVHSILIRRGRTDKVFNPITAGAVTFVAEMVQMLIILAIARPYEDAVRLVSNIAAPMMVTNTVGAALFMRILLDKRAMFEKYTSAFSATALKVAASTEGILRQGFNEVNSMKVAQVLYQELDIGAVAITDREKLLAFTGIGDDHHLPGKPISSTYTLKAIETGEVVYADGNEVPYRCSLHPQCKLGSTLVIPLRGENQ... | 2.7.13.3 | null | cell wall organization [GO:0071555]; response to nutrient levels [GO:0031667]; signal transduction [GO:0007165] | plasma membrane [GO:0005886] | ATP binding [GO:0005524]; monocarboxylic acid binding [GO:0033293]; phosphorelay sensor kinase activity [GO:0000155] | PF07694;PF13185;PF06580; | 3.30.450.40;3.30.565.10; | null | PTM: Autophosphorylated. {ECO:0000269|PubMed:15522865}. | 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}; | null | null | null | null | FUNCTION: Member of the two-component regulatory system BtsS/BtsR, which is part of a nutrient-sensing regulatory network composed of BtsS/BtsR, the low-affinity pyruvate signaling system YpdA/YpdB and their respective target proteins, BtsT and YhjX. Responds to depletion of nutrients, specifically serine, and the conc... | Escherichia coli (strain K12) |
P0AD49 | YFIA_ECOLI | MTMNITSKQMEITPAIRQHVADRLAKLEKWQTHLINPHIILSKEPQGFVADATINTPNGVLVASGKHEDMYTAINELINKLERQLNKLQHKGEARRAATSVKDANFVEEVEEE | null | null | dormancy process [GO:0022611]; negative regulation of translational elongation [GO:0045900]; negative regulation of translational initiation [GO:0045947]; response to cold [GO:0009409] | cytosol [GO:0005829]; cytosolic small ribosomal subunit [GO:0022627] | ribosomal small subunit binding [GO:0043024]; rRNA binding [GO:0019843] | PF02482; | 3.30.160.100; | HPF/YfiA ribosome-associated protein family, YfiA subfamily | null | null | null | null | null | null | null | FUNCTION: During stationary phase prevents 70S dimer formation, probably in order to regulate translation efficiency during transition between the exponential and the stationary phases (PubMed:16324148). During environmental stress such as cold shock or excessive cell density at stationary phase, stabilizes the 70S rib... | Escherichia coli (strain K12) |
P0AD57 | ISPB_ECOLI | MNLEKINELTAQDMAGVNAAILEQLNSDVQLINQLGYYIVSGGGKRIRPMIAVLAARAVGYEGNAHVTIAALIEFIHTATLLHDDVVDESDMRRGKATANAAFGNAASVLVGDFIYTRAFQMMTSLGSLKVLEVMSEAVNVIAEGEVLQLMNVNDPDITEENYMRVIYSKTARLFEAAAQCSGILAGCTPEEEKGLQDYGRYLGTAFQLIDDLLDYNADGEQLGKNVGDDLNEGKPTLPLLHAMHHGTPEQAQMIRTAIEQGNGRHLLEPVLEAMNACGSLEWTRQRAEEEADKAIAALQVLPDTPWREALIGLAHIAVQ... | 2.5.1.90 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250}; | isoprenoid biosynthetic process [GO:0008299]; polyprenol biosynthetic process [GO:0016094]; ubiquinone biosynthetic process [GO:0006744] | cytosol [GO:0005829] | identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; octaprenyl pyrophosphate synthase activity [GO:0106350]; prenyltransferase activity [GO:0004659]; protein homodimerization activity [GO:0042803] | PF00348; | 1.10.600.10; | FPP/GGPP synthase family | null | null | CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate + 5 isopentenyl diphosphate = all-trans-octaprenyl diphosphate + 5 diphosphate; Xref=Rhea:RHEA:27798, ChEBI:CHEBI:33019, ChEBI:CHEBI:57711, ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.90; Evidence={ECO:0000269|PubMed:8037730}; | null | null | null | null | FUNCTION: Supplies octaprenyl diphosphate, the precursor for the side chain of the isoprenoid quinones ubiquinone and menaquinone. {ECO:0000269|PubMed:8037730}. | Escherichia coli (strain K12) |
P0AD59 | IVY_ECOLI | MGRISSGGMMFKAITTVAALVIATSAMAQDDLTISSLAKGETTKAAFNQMVQGHKLPAWVMKGGTYTPAQTVTLGDETYQVMSACKPHDCGSQRIAVMWSEKSNQMTGLFSTIDEKTSQEKLTWLNVNDALSIDGKTVLFAALTGSLENHPDGFNFK | null | null | chaperone-mediated protein folding [GO:0061077] | outer membrane-bounded periplasmic space [GO:0030288] | lysozyme inhibitor activity [GO:0060241]; protein homodimerization activity [GO:0042803] | PF08816; | 3.40.1420.10; | Ivy family | null | SUBCELLULAR LOCATION: Periplasm. | null | null | null | null | null | FUNCTION: Strong inhibitor of lysozyme C. | Escherichia coli (strain K12) |
P0AD61 | KPYK1_ECOLI | MKKTKIVCTIGPKTESEEMLAKMLDAGMNVMRLNFSHGDYAEHGQRIQNLRNVMSKTGKTAAILLDTKGPEIRTMKLEGGNDVSLKAGQTFTFTTDKSVIGNSEMVAVTYEGFTTDLSVGNTVLVDDGLIGMEVTAIEGNKVICKVLNNGDLGENKGVNLPGVSIALPALAEKDKQDLIFGCEQGVDFVAASFIRKRSDVIEIREHLKAHGGENIHIISKIENQEGLNNFDEILEASDGIMVARGDLGVEIPVEEVIFAQKMMIEKCIRARKVVITATQMLDSMIKNPRPTRAEAGDVANAILDGTDAVMLSGESAKGKY... | 2.7.1.40 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:7011316}; COFACTOR: Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000250|UniProtKB:Q02499}; | cellular response to insulin stimulus [GO:0032869]; glycolytic process [GO:0006096]; phosphorylation [GO:0016310]; response to heat [GO:0009408] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; pyruvate kinase complex [GO:1902912] | ATP binding [GO:0005524]; identical protein binding [GO:0042802]; kinase activity [GO:0016301]; magnesium ion binding [GO:0000287]; potassium ion binding [GO:0030955]; pyruvate kinase activity [GO:0004743] | PF00224;PF02887; | 3.20.20.60;2.40.33.10;3.40.1380.20; | Pyruvate kinase family | null | null | CATALYTIC ACTIVITY: Reaction=ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate; Xref=Rhea:RHEA:18157, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58702, ChEBI:CHEBI:456216; EC=2.7.1.40; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18159; Evidence={ECO:0000269|PubMed:10751408, ECO:000030... | null | PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5. | null | null | FUNCTION: Catalyzes the formation of pyruvate in the last step of glycolysis, it is irreversible under physiological conditions. The reaction is critical for the control of metabolic flux in the second part of glycolysis. {ECO:0000305|PubMed:8591049}. | Escherichia coli (strain K12) |
P0AD64 | BLA1_KLEPN | MRYIRLCIISLLATLPLAVHASPQPLEQIKLSESQLSGRVGMIEMDLASGRTLTAWRADERFPMMSTFKVVLCGAVLARVDAGDEQLERKIHYRQQDLVDYSPVSEKHLADGMTVGELCAAAITMSDNSAANLLLATVGGPAGLTAFLRQIGDNVTRLDRWETELNEALPGDARDTTTPASMAATLRKLLTSQRLSARSQRQLLQWMVDDRVAGPLIRSVLPAGWFIADKTGAGERGARGIVALLGPNNKAERIVVIYLRDTPASMAERNQQIAGIGAALIEHWQR | 3.5.2.6 | null | beta-lactam antibiotic catabolic process [GO:0030655]; response to antibiotic [GO:0046677] | null | beta-lactamase activity [GO:0008800] | PF13354; | 3.40.710.10; | Class-A beta-lactamase family | null | null | CATALYTIC ACTIVITY: Reaction=a beta-lactam + H2O = a substituted beta-amino acid; Xref=Rhea:RHEA:20401, ChEBI:CHEBI:15377, ChEBI:CHEBI:35627, ChEBI:CHEBI:140347; EC=3.5.2.6; Evidence={ECO:0000255|PROSITE-ProRule:PRU10101, ECO:0000269|PubMed:10231522, ECO:0000269|PubMed:19351161, ECO:0000269|PubMed:22908166, ECO:0000269... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=183 uM for ampicillin (at pH 7.4 and 25 degrees Celsius) {ECO:0000269|PubMed:19351161}; KM=77 uM for piperacillin (at pH 7.4 and 25 degrees Celsius) {ECO:0000269|PubMed:19351161}; KM=75 uM for piperacillin (at pH 7.4) {ECO:0000269|PubMed:23252553}; KM=21 uM for nit... | null | null | null | FUNCTION: Broad-spectrum beta-lactamase which confers resistance to penicillins, as well as first- and third-generation cephalosporins (PubMed:10639363, PubMed:18955486, PubMed:19351161, PubMed:22908166, PubMed:23145056, PubMed:23252553). Has nitrocefin-hydrolyzing activity (PubMed:10231522, PubMed:19351161, PubMed:232... | Klebsiella pneumoniae |
P0AD65 | MRDA_ECOLI | MKLQNSFRDYTAESALFVRRALVAFLGILLLTGVLIANLYNLQIVRFTDYQTRSNENRIKLVPIAPSRGIIYDRNGIPLALNRTIYQIEMMPEKVDNVQQTLDALRSVVDLTDDDIAAFRKERARSHRFTSIPVKTNLTEVQVARFAVNQYRFPGVEVKGYKRRYYPYGSALTHVIGYVSKINDKDVERLNNDGKLANYAATHDIGKLGIERYYEDVLHGQTGYEEVEVNNRGRVIRQLKEVPPQAGHDIYLTLDLKLQQYIETLLAGSRAAVVVTDPRTGGVLALVSTPSYDPNLFVDGISSKDYSALLNDPNTPLVNR... | 3.4.16.4 | null | cell wall organization [GO:0071555]; peptidoglycan biosynthetic process [GO:0009252]; proteolysis [GO:0006508]; regulation of cell shape [GO:0008360]; response to antibiotic [GO:0046677] | outer membrane-bounded periplasmic space [GO:0030288]; plasma membrane [GO:0005886] | penicillin binding [GO:0008658]; peptidoglycan L,D-transpeptidase activity [GO:0071972]; serine-type D-Ala-D-Ala carboxypeptidase activity [GO:0009002] | PF03717;PF00905; | 3.40.710.10;3.90.1310.10; | Transpeptidase family, MrdA subfamily | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_02081, ECO:0000269|PubMed:1103132, ECO:0000269|PubMed:3009484}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_02081}. Note=Localizes preferentially in the lateral wall and at mid-cell in comparison with the old cell pole. Localization at mid... | 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; Evidence={ECO:0000255|HAMAP-Rule:MF_02081, ECO:0000269|PubMed:3009484}; | null | PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. {ECO:0000255|HAMAP-Rule:MF_02081, ECO:0000269|PubMed:3009484}. | null | null | FUNCTION: Catalyzes cross-linking of the peptidoglycan cell wall (PubMed:3009484). Responsible for the determination of the rod shape of the cell (PubMed:1103132). Is probably required for lateral peptidoglycan synthesis and maintenance of the correct diameter during lateral and centripetal growth (PubMed:12519203). {E... | Escherichia coli (strain K12) |
P0AD68 | FTSI_ECOLI | MKAAAKTQKPKRQEEHANFISWRFALLCGCILLALAFLLGRVAWLQVISPDMLVKEGDMRSLRVQQVSTSRGMITDRSGRPLAVSVPVKAIWADPKEVHDAGGISVGDRWKALANALNIPLDQLSARINANPKGRFIYLARQVNPDMADYIKKLKLPGIHLREESRRYYPSGEVTAHLIGFTNVDSQGIEGVEKSFDKWLTGQPGERIVRKDRYGRVIEDISSTDSQAAHNLALSIDERLQALVYRELNNAVAFNKAESGSAVLVDVNTGEVLAMANSPSYNPNNLSGTPKEAMRNRTITDVFEPGSTVKPMVVMTALQR... | 3.4.16.4 | null | cell division [GO:0051301]; cell wall organization [GO:0071555]; division septum assembly [GO:0000917]; FtsZ-dependent cytokinesis [GO:0043093]; peptidoglycan biosynthetic process [GO:0009252]; proteolysis [GO:0006508]; regulation of cell shape [GO:0008360]; response to xenobiotic stimulus [GO:0009410] | cell division site [GO:0032153]; divisome complex [GO:1990586]; plasma membrane [GO:0005886] | penicillin binding [GO:0008658]; peptidoglycan glycosyltransferase activity [GO:0008955]; serine-type D-Ala-D-Ala carboxypeptidase activity [GO:0009002] | PF03717;PF00905; | 1.10.150.770;3.30.450.330;3.40.710.10;3.90.1310.10; | Transpeptidase family, FtsI subfamily | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_02080, ECO:0000269|PubMed:2677607, ECO:0000269|PubMed:9614966}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_02080, ECO:0000269|PubMed:2677607, ECO:0000269|PubMed:9614966}; Periplasmic side {ECO:0000269|PubMed:2677607, ECO:0000269|PubMed:96... | 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; Evidence={ECO:0000255|HAMAP-Rule:MF_02080, ECO:0000269|PubMed:3531167, ECO:0000269|PubMed:6450748, ECO:0000269|PubMed:7030331}; | null | PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. {ECO:0000255|HAMAP-Rule:MF_02080, ECO:0000269|PubMed:6450748}. | null | null | FUNCTION: Essential cell division protein that catalyzes cross-linking of the peptidoglycan cell wall at the division septum (PubMed:1103132, PubMed:3531167, PubMed:6450748, PubMed:7030331, PubMed:9614966). Required for localization of FtsN (PubMed:9282742). {ECO:0000269|PubMed:1103132, ECO:0000269|PubMed:3531167, ECO:... | Escherichia coli (strain K12) |
P0AD70 | AMPH_ECOLI | MKRSLLFSAVLCAASLTSVHAAQPITEPEFASDIVDRYADHIFYGSGATGMALVVIDGNQRVFRSYGETRPGNNVRPQLDSVVRIASLTKLMTSEMLVKLLDQGTVKLNDPLSKYAPPGARVPTYNGTPITLVNLATHTSALPREQPGGAAHRPVFVWPTREQRWKYLSTAKLKAAPGSQAAYSNLAFDLLADALANASGKPYTQLFEEQITRPLGMKDTTYTPSPDQCRRLMVAERGASPCNNTLAAIGSGGVYSTPGDMMRWMQQYLSSDFYQRSNQADRMQTLIYQRAQFTKVIGMDVPGKADALGLGWVYMAPKEG... | 3.4.-.- | null | cell wall organization [GO:0071555]; peptidoglycan catabolic process [GO:0009253]; proteolysis [GO:0006508]; regulation of cell shape [GO:0008360] | plasma membrane [GO:0005886] | carboxypeptidase activity [GO:0004180]; endopeptidase activity [GO:0004175]; penicillin binding [GO:0008658] | PF00144; | 3.40.710.10; | Beta-lactamase family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:22001512}. | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=102 uM for D45 (at 37 degrees Celsius and pH 7.3) {ECO:0000269|PubMed:22001512}; KM=134 uM for D44 (at 37 degrees Celsius and pH 7.3) {ECO:0000269|PubMed:22001512}; KM=225 uM for M5 (at 37 degrees Celsius and pH 7.5) {ECO:0000269|PubMed:22001512}; Vmax=4.98 nmol/mi... | null | null | null | FUNCTION: Hydrolyzes the cross-linked dimers tetrapentapeptide (D45) and tetratetrapeptide (D44). Removes the terminal D-alanine from muropeptides and disaccharide pentapeptide M5 with a C-terminal D-Ala-D-Ala dipeptide. Associated with recycling and remodeling of peptidoglycan (PG). Also displays a low beta-lactamase ... | Escherichia coli (strain K12) |
P0AD99 | BRNQ_ECOLI | MTHQLRSRDIIALGFMTFALFVGAGNIIFPPMVGLQAGEHVWTAAFGFLITAVGLPVLTVVALAKVGGGVDSLSTPIGKVAGVLLATVCYLAVGPLFATPRTATVSFEVGIAPLTGDSALPLFIYSLVYFAIVILVSLYPGKLLDTVGNFLAPLKIIALVILSVAAIVWPAGSISTATEAYQNAAFSNGFVNGYLTMDTLGAMVFGIVIVNAARSRGVTEARLLTRYTVWAGLMAGVGLTLLYLALFRLGSDSASLVDQSANGAAILHAYVQHTFGGGGSFLLAALIFIACLVTAVGLTCACAEFFAQYVPLSYRTLVFI... | null | null | branched-chain amino acid transport [GO:0015803]; isoleucine transport [GO:0015818]; leucine transport [GO:0015820]; valine transport [GO:0015829] | plasma membrane [GO:0005886] | L-isoleucine transmembrane transporter activity [GO:0015188]; L-leucine transmembrane transporter activity [GO:0015190]; L-valine transmembrane transporter activity [GO:0005304] | PF05525; | null | Branched chain amino acid transporter family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Liv-II branched chain amino acid transport system, which transports leucine, valine and isoleucine. {ECO:0000269|PubMed:4590465, ECO:0000269|PubMed:4945181}. | Escherichia coli (strain K12) |
P0ADA1 | TESA_ECOLI | MMNFNNVFRWHLPFLFLVLLTFRAAAADTLLILGDSLSAGYRMSASAAWPALLNDKWQSKTSVVNASISGDTSQQGLARLPALLKQHQPRWVLVELGGNDGLRGFQPQQTEQTLRQILQDVKAANAEPLLMQIRLPANYGRRYNEAFSAIYPKLAKEFDVPLLPFFMEEVYLKPQWMQDDGIHPNRDAQPFIADWMAKQLQPLVNHDS | 3.1.1.2; 3.1.1.5; 3.1.2.14; 3.1.2.2; 3.4.21.- | null | lipid metabolic process [GO:0006629]; proteolysis [GO:0006508] | outer membrane-bounded periplasmic space [GO:0030288] | arylesterase activity [GO:0004064]; fatty acyl-[ACP] hydrolase activity [GO:0016297]; fatty acyl-CoA hydrolase activity [GO:0047617]; identical protein binding [GO:0042802]; lysophospholipase activity [GO:0004622]; peptidase activity [GO:0008233]; phosphatidyl phospholipase B activity [GO:0102545] | PF13472; | 3.40.50.1110; | 'GDSL' lipolytic enzyme family | null | SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:8098033, ECO:0000269|PubMed:8432696}. | CATALYTIC ACTIVITY: Reaction=a fatty acyl-CoA + H2O = a fatty acid + CoA + H(+); Xref=Rhea:RHEA:16781, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57287, ChEBI:CHEBI:77636; Evidence={ECO:0000269|PubMed:4554913, ECO:0000269|PubMed:9070299}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.5 uM for N-benzyloxycarbonyl-L-tyrosine-p-nitrophenyl ester {ECO:0000269|PubMed:9070299}; KM=3.8 uM for oleoyl-ACP {ECO:0000269|PubMed:4554913}; KM=4 uM for oleoyl-CoA {ECO:0000269|PubMed:4554913}; KM=4 uM for palmitoleoyl-CoA {ECO:0000269|PubMed:4554913}; KM=4.6... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5-8.4 (PubMed:12846577, PubMed:4554913, PubMed:4945109). Stable between pH 6.1 and 12, however, below pH 6.0, thioesterase rapidly loses activity (PubMed:4554913). {ECO:0000269|PubMed:12846577, ECO:0000269|PubMed:4554913, ECO:0000269|PubMed:4945109}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Protease is stable up to 50 degrees Celsius. {ECO:0000269|PubMed:4945109}; | FUNCTION: TesA is a multifunctional esterase that can act as a thioesterase, lysophospholipase and protease (PubMed:10423542, PubMed:1864840, PubMed:238979, PubMed:4554913, PubMed:4945109, PubMed:791643, PubMed:8098033, PubMed:8132479, PubMed:8432696, PubMed:9070299). TesA functions as a thioesterase specific for fatty... | Escherichia coli (strain K12) |
P0ADA2 | TESA_ECOL6 | MMNFNNVFRWHLPFLFLVLLTFRAAAADTLLILGDSLSAGYRMSASAAWPALLNDKWQSKTSVVNASISGDTSQQGLARLPALLKQHQPRWVLVELGGNDGLRGFQPQQTEQTLRQILQDVKAANAEPLLMQIRLPANYGRRYNEAFSAIYPKLAKEFDVPLLPFFMEEVYLKPQWMQDDGIHPNRDAQPFIADWMAKQLQPLVNHDS | 3.1.1.2; 3.1.1.5; 3.1.2.14; 3.1.2.2; 3.4.21.- | null | lipid metabolic process [GO:0006629]; proteolysis [GO:0006508] | periplasmic space [GO:0042597] | arylesterase activity [GO:0004064]; fatty acyl-[ACP] hydrolase activity [GO:0016297]; fatty acyl-CoA hydrolase activity [GO:0047617]; lysophospholipase activity [GO:0004622]; peptidase activity [GO:0008233]; phosphatidyl phospholipase B activity [GO:0102545] | PF13472; | 3.40.50.1110; | 'GDSL' lipolytic enzyme family | null | SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:P0ADA1}. | CATALYTIC ACTIVITY: Reaction=a fatty acyl-CoA + H2O = a fatty acid + CoA + H(+); Xref=Rhea:RHEA:16781, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57287, ChEBI:CHEBI:77636; Evidence={ECO:0000250|UniProtKB:P0ADA1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16782; Evidence={ECO:0000250... | null | null | null | null | FUNCTION: TesA is a multifunctional esterase that can act as a thioesterase, arylesterase, lysophospholipase and protease. {ECO:0000250|UniProtKB:P0ADA1}. | Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) |
P0ADA3 | NLPD_ECOLI | MSAGSPKFTVRRIAALSLVSLWLAGCSDTSNPPAPVSSVNGNAPANTNSGMLITPPPKMGTTSTAQQPQIQPVQQPQIQATQQPQIQPVQPVAQQPVQMENGRIVYNRQYGNIPKGSYSGSTYTVKKGDTLFYIAWITGNDFRDLAQRNNIQAPYALNVGQTLQVGNASGTPITGGNAITQADAAEQGVVIKPAQNSTVAVASQPTITYSESSGEQSANKMLPNNKPTATTVTAPVTVPTASTTEPTVSSTSTSTPISTWRWPTEGKVIETFGASEGGNKGIDIAGSKGQAIIATADGRVVYAGNALRGYGNLIIIKHND... | null | null | cell cycle [GO:0007049]; response to xenobiotic stimulus [GO:0009410]; septum digestion after cytokinesis [GO:0000920] | cell division site [GO:0032153]; cell outer membrane [GO:0009279]; plasma membrane [GO:0005886] | metalloendopeptidase activity [GO:0004222] | PF01476;PF01551; | 2.70.70.10;3.10.350.10; | E.coli NlpD/Haemophilus LppB family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}. Note=Localizes at the septal ring. {ECO:0000269|PubMed:19525345}. | null | null | null | null | null | FUNCTION: Activator of the cell wall hydrolase AmiC. Required for septal murein cleavage and daughter cell separation during cell division. {ECO:0000269|PubMed:19525345, ECO:0000269|PubMed:20300061}. | Escherichia coli (strain K12) |
P0ADC1 | LPTE_ECOLI | MRYLATLLLSLAVLITAGCGWHLRDTTQVPSTMKVMILDSGDPNGPLSRAVRNQLRLNGVELLDKETTRKDVPSLRLGKVSIAKDTASVFRNGQTAEYQMIMTVNATVLIPGRDIYPISAKVFRSFFDNPQMALAKDNEQDMIVKEMYDRAAEQLIRKLPSIRAADIRSDEEQTSTTTDTPATPARVSTTLGN | null | null | Gram-negative-bacterium-type cell outer membrane assembly [GO:0043165]; lipopolysaccharide transport [GO:0015920] | cell outer membrane [GO:0009279]; transporter complex [GO:1990351] | lipopolysaccharide binding [GO:0001530] | PF04390; | 3.30.160.150; | LptE lipoprotein family | null | SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-Rule:MF_01186, ECO:0000269|PubMed:20446753, ECO:0000269|PubMed:21257904, ECO:0000269|PubMed:3316191}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_01186, ECO:0000269|PubMed:20446753, ECO:0000269|PubMed:21257904, ECO:0000269|PubMed:3316191}. Note=A substantial port... | null | null | null | null | null | FUNCTION: Together with LptD, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane. Required for the proper assembly of LptD. Binds LPS and may serve as the LPS recognition site at the outer membrane. {ECO:0000255|HAMAP-Rule:MF_01186, ECO:0000269|PubMed:16861298, ECO:0000269|PubM... | Escherichia coli (strain K12) |
P0ADE4 | TAMA_ECOLI | MRYIRQLCCVSLLCLSGSAVAANVRLQVEGLSGQLEKNVRAQLSTIESDEVTPDRRFRARVDDAIREGLKALGYYQPTIEFDLRPPPKKGRQVLIAKVTPGVPVLIGGTDVVLRGGARTDKDYLKLLDTRPAIGTVLNQGDYENFKKSLTSIALRKGYFDSEFTKAQLGIALGLHKAFWDIDYNSGERYRFGHVTFEGSQIRDEYLQNLVPFKEGDEYESKDLAELNRRLSATGWFNSVVVAPQFDKARETKVLPLTGVVSPRTENTIETGVGYSTDVGPRVKATWKKPWMNSYGHSLTTSTSISAPEQTLDFSYKMPLL... | null | null | protein localization to outer membrane [GO:0089705]; protein secretion [GO:0009306] | cell outer membrane [GO:0009279]; plasma membrane [GO:0005886]; TAM protein secretion complex [GO:0097347] | null | PF01103;PF07244;PF17243; | 3.10.20.310;2.40.160.50; | TamA family | null | SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000269|PubMed:16522795, ECO:0000269|PubMed:17214547, ECO:0000269|PubMed:22466966, ECO:0000269|PubMed:25341963}. | null | null | null | null | null | FUNCTION: Part of the translocation and assembly module (TAM) autotransporter assembly complex, which functions in translocation of autotransporters across the outer membrane (PubMed:22466966, PubMed:25341963). Allows substrate (Ag43, AC P39180) to initiate penetration into the outer membrane; TamB is not necessary but... | Escherichia coli (strain K12) |
P0ADG4 | SUHB_ECOLI | MHPMLNIAVRAARKAGNLIAKNYETPDAVEASQKGSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEESGELEGTDQDVQWVIDPLDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTILATGFPFKAKQYATTYINIVGKLFNECADFRRTGSAALDLAYVAAGRVDGFFEIGLRPWDFAAGELLVREAGGIVSDFTGGHNYMLTGNIVAGNPRVVKAMLANMRDELSDALKR | 3.1.3.25 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:10747806, ECO:0000269|PubMed:31020314, ECO:0000269|PubMed:32871103, ECO:0000269|PubMed:8002619}; Note=Partial activity is seen with Co(2+), Ni(2+), Mn(2+), Zn(2+) and Fe(2+); in the presence of Mg(2+) these cations inhibit. {ECO:0000269|PubMed:... | inositol metabolic process [GO:0006020]; phosphatidylinositol phosphate biosynthetic process [GO:0046854]; ribosome biogenesis [GO:0042254]; signal transduction [GO:0007165]; transcription antitermination [GO:0031564] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | glycerol-2-phosphatase activity [GO:0047954]; inositol monophosphate 1-phosphatase activity [GO:0008934]; inositol monophosphate 3-phosphatase activity [GO:0052832]; inositol monophosphate 4-phosphatase activity [GO:0052833]; lithium ion binding [GO:0031403]; magnesium ion binding [GO:0000287]; rRNA primary transcript ... | PF00459; | 3.40.190.80;3.30.540.10; | Inositol monophosphatase superfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:10747806}. | CATALYTIC ACTIVITY: Reaction=a myo-inositol phosphate + H2O = myo-inositol + phosphate; Xref=Rhea:RHEA:24056, ChEBI:CHEBI:15377, ChEBI:CHEBI:17268, ChEBI:CHEBI:43474, ChEBI:CHEBI:84139; EC=3.1.3.25; Evidence={ECO:0000269|PubMed:10747806, ECO:0000269|PubMed:8002619}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1-phosph... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=71 uM for myo-inositol phosphate {ECO:0000269|PubMed:8002619}; KM=64 uM for 1D-myo-inositol 1-phosphate {ECO:0000269|PubMed:10747806}; KM=79 uM for 1D-myo-inositol 3-phosphate {ECO:0000269|PubMed:10747806}; KM=69 uM for myo-inositol phosphate {ECO:0000269|PubMed:10... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.8. {ECO:0000269|PubMed:8002619}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 80 degrees Celsius, 90% of activity remains after heating at 70 degrees Celsius for 5 minutes. {ECO:0000269|PubMed:10747806}; | 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) |
P0ADG7 | IMDH_ECOLI | MLRIAKEALTFDDVLLVPAHSTVLPNTADLSTQLTKTIRLNIPMLSAAMDTVTEARLAIALAQEGGIGFIHKNMSIERQAEEVRRVKKHESGVVTDPQTVLPTTTLREVKELTERNGFAGYPVVTEENELVGIITGRDVRFVTDLNQPVSVYMTPKERLVTVREGEAREVVLAKMHEKRVEKALVVDDEFHLIGMITVKDFQKAERKPNACKDEQGRLRVGAAVGAGAGNEERVDALVAAGVDVLLIDSSHGHSEGVLQRIRETRAKYPDLQIIGGNVATAAGARALAEAGCSAVKVGIGPGSICTTRIVTGVGVPQITA... | 1.1.1.205 | COFACTOR: Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000255|HAMAP-Rule:MF_01964}; | GMP biosynthetic process [GO:0006177]; GTP biosynthetic process [GO:0006183]; protein homotetramerization [GO:0051289]; response to UV [GO:0009411] | cytosol [GO:0005829]; protein-containing complex [GO:0032991] | ATP binding [GO:0005524]; C-rich single-stranded DNA binding [GO:1990829]; guanosine tetraphosphate binding [GO:0097216]; identical protein binding [GO:0042802]; IMP dehydrogenase activity [GO:0003938]; metal ion binding [GO:0046872]; single-stranded DNA binding [GO:0003697] | PF00571;PF00478; | 3.20.20.70; | IMPDH/GMPR family | null | null | CATALYTIC ACTIVITY: Reaction=H2O + IMP + NAD(+) = H(+) + NADH + XMP; Xref=Rhea:RHEA:11708, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57464, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58053; EC=1.1.1.205; Evidence={ECO:0000255|HAMAP-Rule:MF_01964}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=61 uM for Inosine 5'-phosphate {ECO:0000269|PubMed:9341229}; KM=2000 uM for NAD(+) {ECO:0000269|PubMed:9341229}; KM=2.8 mM for K(+) {ECO:0000269|PubMed:9341229}; | PATHWAY: Purine metabolism; XMP biosynthesis via de novo pathway; XMP from IMP: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01964}. | null | null | FUNCTION: Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. {ECO:0000255|HAMAP-Rule:MF_01964, ECO:0000269|PubMed:9341... | Escherichia coli (strain K12) |
P0ADI4 | ENTB_ECOLI | MAIPKLQAYALPESHDIPQNKVDWAFEPQRAALLIHDMQDYFVSFWGENCPMMEQVIANIAALRDYCKQHNIPVYYTAQPKEQSDEDRALLNDMWGPGLTRSPEQQKVVDRLTPDADDTVLVKWRYSAFHRSPLEQMLKESGRNQLIITGVYAHIGCMTTATDAFMRDIKPFMVADALADFSRDEHLMSLKYVAGRSGRVVMTEELLPAPIPASKAALREVILPLLDESDEPFDDDNLIDYGLDSVRMMALAARWRKVHGDIDFVMLAKNPTIDAWWKLLSREVK | 3.3.2.1; 6.3.2.14 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:16632253}; | enterobactin biosynthetic process [GO:0009239] | cytosol [GO:0005829]; plasma membrane [GO:0005886] | 2,3-dihydroxybenzoate-serine ligase activity [GO:0047527]; identical protein binding [GO:0042802]; isochorismatase activity [GO:0008908]; magnesium ion binding [GO:0000287]; phosphopantetheine binding [GO:0031177]; transferase activity, transferring alkyl or aryl (other than methyl) groups [GO:0016765] | PF00857;PF00550; | 1.10.1200.10;3.40.50.850; | Isochorismatase family | PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine of apo-EntB by EntD. Holo-EntB so formed is then acylated with 2,3-dihydroxybenzoate in a reaction catalyzed by EntE. {ECO:0000269|PubMed:22365602}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10692387}. | CATALYTIC ACTIVITY: Reaction=3 2,3-dihydroxybenzoate + 6 ATP + 3 L-serine = 6 AMP + 6 diphosphate + enterobactin + 4 H(+); Xref=Rhea:RHEA:30571, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:33384, ChEBI:CHEBI:36654, ChEBI:CHEBI:77805, ChEBI:CHEBI:456215; EC=6.3.2.14; Evidence={ECO:0000269|PubMed... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=14.7 uM for isochorismate (at pH 7 and 37 degrees Celsius) {ECO:0000269|PubMed:2139796}; KM=23 uM for 4,5-dihydroisochorismate (at pH 7 and 37 degrees Celsius) {ECO:0000269|PubMed:2139796}; KM=86 uM for 3-[(carboxyethenyl)oxy]-1-cyclohexene-1-carboxylic acid (at pH... | PATHWAY: Siderophore biosynthesis; enterobactin biosynthesis. {ECO:0000305|PubMed:9214294}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is between 6.5 and 7.5. At pH 5.5, EntB retains 50% of isochorismatase activity. {ECO:0000269|PubMed:2139796}; | null | FUNCTION: Involved in the biosynthesis of the siderophore enterobactin (enterochelin), which is a macrocyclic trimeric lactone of N-(2,3-dihydroxybenzoyl)-serine. The serine trilactone serves as a scaffolding for the three catechol functionalities that provide hexadentate coordination for the tightly ligated iron(3+) a... | Escherichia coli (strain K12) |
P0ADL1 | NEPI_ECOLI | MSEFIAENRGADAITRPNWSAVFSVAFCVACLIIVEFLPVSLLTPMAQDLGISEGVAGQSVTVTAFVAMFASLFITQTIQATDRRYVVILFAVLLTLSCLLVSFANSFSLLLIGRACLGLALGGFWAMSASLTMRLVPPRTVPKALSVIFGAVSIALVIAAPLGSFLGELIGWRNVFNAAAVMGVLCIFWIIKSLPSLPGEPSHQKQNTFRLLQRPGVMAGMIAIFMSFAGQFAFFTYIRPVYMNLAGFGVDGLTLVLLSFGIASFIGTSLSSFILKRSVKLALAGAPLILAVSALVLTLWGSDKIVATGVAIIWGLTFA... | null | null | purine nucleoside transmembrane transport [GO:0015860]; transmembrane transport [GO:0055085] | plasma membrane [GO:0005886] | antiporter activity [GO:0015297]; purine nucleoside transmembrane transporter activity [GO:0015211]; transmembrane transporter activity [GO:0022857] | PF07690; | 1.20.1250.20; | Major facilitator superfamily, DHA1 family, NepI (TC 2.A.1.2.26) subfamily | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_01189, ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=H(+)(out) + inosine(in) = H(+)(in) + inosine(out); Xref=Rhea:RHEA:29211, ChEBI:CHEBI:15378, ChEBI:CHEBI:17596; Evidence={ECO:0000255|HAMAP-Rule:MF_01189, ECO:0000269|PubMed:16040204}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29212; Evidence={ECO:0000255|HAMAP-Rule:MF_01189, ECO:... | null | null | null | null | FUNCTION: Involved in the efflux of purine ribonucleosides, such as inosine and guanosine (PubMed:16040204). Adenosine may also be a substrate (PubMed:16040204). Confers resistance to the hypoxanthine analog 6-mercaptopurine, however the level of resistance is rather low (PubMed:16040204). {ECO:0000269|PubMed:16040204}... | Escherichia coli (strain K12) |
P0ADP0 | YIGB_ECOLI | MRFYRPLGRISALTFDLDDTLYDNRPVILRTEREALTFVQNYHPALRSFQNEDLQRLRQAVREAEPEIYHDVTRWRFRSIEQAMLDAGLSAEEASAGAHAAMINFAKWRSRIDVPQQTHDTLKQLAKKWPLVAITNGNAQPELFGLGDYFEFVLRAGPHGRSKPFSDMYFLAAEKLNVPIGEILHVGDDLTTDVGGAIRSGMQACWIRPENGDLMQTWDSRLLPHLEISRLASLTSLI | 3.1.3.104 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:16990279}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:16990279}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000269|PubMed:16990279}; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:16990279}; No... | dephosphorylation [GO:0016311]; dormancy process [GO:0022611]; N-acetylneuraminate biosynthetic process [GO:0046380]; riboflavin biosynthetic process [GO:0009231] | null | 5-amino-6-(5-phosphoribitylamino)uracil phosphatase activity [GO:0043726]; magnesium ion binding [GO:0000287]; N-acylneuraminate-9-phosphatase activity [GO:0050124]; phosphatase activity [GO:0016791] | PF00702; | 1.20.120.1600;3.40.50.1000; | HAD-like hydrolase superfamily | null | null | CATALYTIC ACTIVITY: Reaction=5-amino-6-(5-phospho-D-ribitylamino)uracil + H2O = 5-amino-6-(D-ribitylamino)uracil + phosphate; Xref=Rhea:RHEA:25197, ChEBI:CHEBI:15377, ChEBI:CHEBI:15934, ChEBI:CHEBI:43474, ChEBI:CHEBI:58421; EC=3.1.3.104; Evidence={ECO:0000269|PubMed:24123841}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=20 uM for 5-amino-6-(5-phospho-D-ribitylamino)uracil {ECO:0000269|PubMed:24123841}; KM=1 mM for FMN (with magnesium ions as cofactor and at pH 9) {ECO:0000269|PubMed:16990279}; Vmax=4 umol/min/mg enzyme with 5-amino-6-(5-phospho-D-ribitylamino)uracil as substrate {... | PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 4/4. {ECO:0000305|PubMed:24123841}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6-7.5. {ECO:0000269|PubMed:16990279}; | null | FUNCTION: Catalyzes the dephosphorylation of 5-amino-6-(5-phospho-D-ribitylamino)uracil, and thus could be involved in the riboflavin biosynthesis pathway (PubMed:24123841). Is also able to dephosphorylate flavin mononucleotide (FMN) and other phosphoric acid esters (PubMed:16990279, PubMed:24123841). YigB is important... | Escherichia coli (strain K12) |
P0ADP2 | YIGI_ECOLI | MSAVLTAEQALKLVGEMFVYHMPFNRALGMELERYEKEFAQLAFKNQPMMVGNWAQSILHGGVIASALDVAAGLVCVGSTLTRHETISEDELRQRLSRMGTIDLRVDYLRPGRGERFTATSSLLRAGNKVAVARVELHNEEQLYIASATATYMVG | 3.1.2.20 | null | lipid metabolic process [GO:0006629]; monocarboxylic acid metabolic process [GO:0032787]; organic substance catabolic process [GO:1901575] | cytosol [GO:0005829] | acyl-CoA hydrolase activity [GO:0016289] | PF03061; | 3.10.129.10; | YigI thioesterase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:35876515}. | CATALYTIC ACTIVITY: Reaction=a fatty acyl-CoA + H2O = a fatty acid + CoA + H(+); Xref=Rhea:RHEA:16781, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57287, ChEBI:CHEBI:77636; EC=3.1.2.20; Evidence={ECO:0000269|PubMed:35876515}; CATALYTIC ACTIVITY: Reaction=a medium-chain fatty acyl-CoA + H2O = a ... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=19.78 mM for decanoyl-CoA {ECO:0000269|PubMed:35876515}; KM=1.04 mM for hexadecanoyl-CoA {ECO:0000269|PubMed:35876515}; Note=kcat is 1.461 sec(-1) with decanoyl-CoA as substrate. kcat is 3.204 sec(-1) with hexadecanoyl-CoA as substrate. {ECO:0000269|PubMed:35876515... | null | null | null | FUNCTION: Displays thioesterase activity against medium- to long-chain acyl-CoA substrates (PubMed:35876515). Is involved in the thioesterase-dependent beta-oxidation pathway of (9Z,11E)-octadecadienoate (conjugated linoleic acid or CLA), along with TesB and FadM (PubMed:35876515). In vitro, is active against decanoyl-... | Escherichia coli (strain K12) |
P0ADR8 | PPNN_ECOLI | MITHISPLGSMDMLSQLEVDMLKRTASSDLYQLFRNCSLAVLNSGSLTDNSKELLSRFENFDINVLRRERGVKLELINPPEEAFVDGRIIRALQANLFAVLRDILFVYGQIHNTVRFPNLNLDNSVHITNLVFSILRNARALHVGEAPNMVVCWGGHSINENEYLYARRVGNQLGLRELNICTGCGPGAMEAPMKGAAVGHAQQRYKDSRFIGMTEPSIIAAEPPNPLVNELIIMPDIEKRLEAFVRIAHGIIIFPGGVGTAEELLYLLGILMNPANKDQVLPLILTGPKESADYFRVLDEFVVHTLGENARRHYRIIID... | 3.2.2.-; 3.2.2.10; 3.2.2.4 | null | protein homotetramerization [GO:0051289] | cytosol [GO:0005829]; protein-containing complex [GO:0032991] | AMP nucleosidase activity [GO:0008714]; guanosine tetraphosphate binding [GO:0097216]; identical protein binding [GO:0042802]; inosinate nucleosidase activity [GO:0047723]; pyrimidine-5'-nucleotide nucleosidase activity [GO:0047405] | PF14793;PF03641;PF11892; | 3.40.50.450;3.30.1850.10; | LOG family | null | null | CATALYTIC ACTIVITY: Reaction=a pyrimidine ribonucleoside 5'-phosphate + H2O = a pyrimidine nucleobase + D-ribose 5-phosphate; Xref=Rhea:RHEA:13425, ChEBI:CHEBI:15377, ChEBI:CHEBI:26432, ChEBI:CHEBI:78346, ChEBI:CHEBI:138238; EC=3.2.2.10; Evidence={ECO:0000269|PubMed:27941785}; CATALYTIC ACTIVITY: Reaction=AMP + H2O = a... | null | null | null | null | FUNCTION: Catalyzes the hydrolysis of the N-glycosidic bond of diverse pyrimidine and purine nucleotide 5'-monophosphates, to form ribose 5-phosphate and the corresponding free base. Can use AMP, GMP, IMP, CMP, dTMP and UMP as substrates. Cannot catalyze the reverse reactions. Is required for optimal growth in glucose ... | Escherichia coli (strain K12) |
P0ADS2 | ZAPA_ECOLI | MSAQPVDIQIFGRSLRVNCPPDQRDALNQAADDLNQRLQDLKERTRVTNTEQLVFIAALNISYELAQEKAKTRDYAASMEQRIRMLQQTIEQALLEQGRITEKTNQNFE | null | null | cell division [GO:0051301]; division septum assembly [GO:0000917]; FtsZ-dependent cytokinesis [GO:0043093]; septin ring assembly [GO:0000921] | cell division site [GO:0032153]; cell septum [GO:0030428]; cytosol [GO:0005829]; plasma membrane [GO:0005886] | identical protein binding [GO:0042802] | PF05164; | 1.20.5.50;3.30.160.880; | ZapA family, Type 1 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12368265}. Note=Localizes at mid-cell. | null | null | null | null | null | FUNCTION: Activator of cell division through the inhibition of FtsZ GTPase activity, therefore promoting FtsZ assembly into bundles of protofilaments necessary for the formation of the division Z ring. It is recruited early at mid-cell but it is not essential for cell division. {ECO:0000269|PubMed:15060045}. | Escherichia coli (strain K12) |
P0ADV1 | LPTA_ECOLI | MKFKTNKLSLNLVLASSLLAASIPAFAVTGDTDQPIHIESDQQSLDMQGNVVTFTGNVIVTQGTIKINADKVVVTRPGGEQGKEVIDGYGKPATFYQMQDNGKPVEGHASQMHYELAKDFVVLTGNAYLQQVDSNIKGDKITYLVKEQKMQAFSDKGKRVTTVLVPSQLQDKNNKGQTPAQKKGN | null | null | Gram-negative-bacterium-type cell outer membrane assembly [GO:0043165]; lipopolysaccharide transport [GO:0015920] | cell outer membrane [GO:0009279]; outer membrane-bounded periplasmic space [GO:0030288]; periplasmic space [GO:0042597]; transporter complex [GO:1990351] | glycolipid transfer activity [GO:0017089]; identical protein binding [GO:0042802]; lipopolysaccharide binding [GO:0001530] | PF03968; | 2.60.450.10; | LptA family | null | SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_01914, ECO:0000269|PubMed:17056748, ECO:0000269|PubMed:18480051, ECO:0000269|PubMed:20446753}. Note=Associates with both the inner membrane and the outer membrane. | null | null | null | null | null | FUNCTION: Involved in the assembly of lipopolysaccharide (LPS). Required for the translocation of LPS from the inner membrane to the outer membrane. May form a bridge between the inner membrane and the outer membrane, via interactions with LptC and LptD, thereby facilitating LPS transfer across the periplasm. {ECO:0000... | Escherichia coli (strain K12) |
P0ADV9 | LPTC_ECOLI | MSKARRWVIIVLSLAVLVMIGINMAEKDDTAQVVVNNNDPTYKSEHTDTLVYNPEGALSYRLIAQHVEYYSDQAVSWFTQPVLTTFDKDKIPTWSVKADKAKLTNDRMLYLYGHVEVNALVPDSQLRRITTDNAQINLVTQDVTSEDLVTLYGTTFNSSGLKMRGNLRSKNAELIEKVRTSYEIQNKQTQP | null | null | Gram-negative-bacterium-type cell outer membrane assembly [GO:0043165]; lipopolysaccharide transport [GO:0015920] | membrane [GO:0016020]; outer membrane-bounded periplasmic space [GO:0030288]; plasma membrane [GO:0005886]; transporter complex [GO:1990351] | glycolipid transfer activity [GO:0017089]; identical protein binding [GO:0042802]; lipopolysaccharide transmembrane transporter activity [GO:0015221] | PF06835; | 2.60.450.10; | LptC family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_01915, ECO:0000269|PubMed:18424520, ECO:0000269|PubMed:20720015}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01915, ECO:0000269|PubMed:18424520, ECO:0000269|PubMed:20720015}. | null | null | null | null | null | FUNCTION: Involved in the assembly of lipopolysaccharide (LPS). Required for the translocation of LPS from the inner membrane to the outer membrane. Facilitates the transfer of LPS from the inner membrane to the periplasmic protein LptA. Could be a docking site for LptA. {ECO:0000255|HAMAP-Rule:MF_01915, ECO:0000269|Pu... | Escherichia coli (strain K12) |
P0ADY1 | PPID_ECOLI | MMDSLRTAANSLVLKIIFGIIIVSFILTGVSGYLIGGGNNYAAKVNDQEISRGQFENAFNSERNRMQQQLGDQYSELAANEGYMKTLRQQVLNRLIDEALLDQYARELKLGISDEQVKQAIFATPAFQVDGKFDNSRYNGILNQMGMTADQYAQALRNQLTTQQLINGVAGTDFMLKGETDELAALVAQQRVVREATIDVNALAAKQPVTEQEIASYYEQNKNNFMTPEQFRVSYIKLDAATMQQPVSDADIQSYYDQHQDQFTQPQRTRYSIIQTKTEDEAKAVLDELNKGGDFAALAKEKSADIISARNGGDMGWLED... | null | null | chaperone-mediated protein folding [GO:0061077] | plasma membrane [GO:0005886] | identical protein binding [GO:0042802]; peptidyl-prolyl cis-trans isomerase activity [GO:0003755] | PF13145;PF13624; | 3.10.50.40;1.10.4030.10; | PpiD chaperone family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:16079137, ECO:0000269|PubMed:21210718, ECO:0000269|PubMed:9670013}; Single-pass type II membrane protein {ECO:0000269|PubMed:21210718, ECO:0000269|PubMed:9670013}; Periplasmic side {ECO:0000269|PubMed:21210718, ECO:0000269|PubMed:9670013}. Note=Located at th... | null | null | null | null | null | FUNCTION: Chaperone that functions as a gatekeeper on the periplasmic side of the SecYEG translocon (PubMed:18439025, PubMed:20920237, PubMed:29097228). Facilitates the translocation of precursor proteins across SecYEG by interacting with the translocating substrate (PubMed:29097228). Also plays a role in the release o... | Escherichia coli (strain K12) |
P0ADY3 | RL14_ECOLI | MIQEQTMLNVADNSGARRVMCIKVLGGSHRRYAGVGDIIKITIKEAIPRGKVKKGDVLKAVVVRTKKGVRRPDGSVIRFDGNACVLLNNNSEQPIGTRIFGPVTRELRSEKFMKIISLAPEVL | null | null | cytoplasmic translation [GO:0002181] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625] | large ribosomal subunit rRNA binding [GO:0070180]; structural constituent of ribosome [GO:0003735] | PF00238; | 2.40.150.20; | Universal ribosomal protein uL14 family | null | null | null | null | null | null | null | FUNCTION: This protein binds directly to 23S ribosomal RNA. In the E.coli 70S ribosome it has been modeled to make two contacts with the 16S rRNA of the 30S subunit, forming part of bridges B5 and B8, connecting the 2 subunits (PubMed:12809609). Although the protein undergoes significant rotation during the transition ... | Escherichia coli (strain K12) |
P0ADY7 | RL16_ECOLI | MLQPKRTKFRKMHKGRNRGLAQGTDVSFGSFGLKAVGRGRLTARQIEAARRAMTRAVKRQGKIWIRVFPDKPITEKPLAVRMGKGKGNVEYWVALIQPGKVLYEMDGVPEELAREAFKLAAAKLPIKTTFVTKTVM | null | null | cytoplasmic translation [GO:0002181]; ribosomal large subunit assembly [GO:0000027] | cytoplasm [GO:0005737]; cytosolic large ribosomal subunit [GO:0022625] | rRNA binding [GO:0019843]; structural constituent of ribosome [GO:0003735]; tRNA binding [GO:0000049] | PF00252; | 3.90.1170.10; | Universal ribosomal protein uL16 family | PTM: Is hydroxylated on Arg-81 by RoxA. The modification is nearly suppressed when E.coli is grown in anoxia. {ECO:0000269|PubMed:23103944}. | null | null | null | null | null | null | FUNCTION: This protein binds directly to 23S ribosomal RNA and is located at the A site of the peptidyltransferase center. It contacts the A and P site tRNAs (PubMed:8524654). It has an essential role in subunit assembly, which is not well understood (PubMed:3298242). {ECO:0000269|PubMed:3298242, ECO:0000269|PubMed:852... | Escherichia coli (strain K12) |
P0ADZ0 | RL23_ECOLI | MIREERLLKVLRAPHVSEKASTAMEKSNTIVLKVAKDATKAEIKAAVQKLFEVEVEVVNTLVVKGKVKRHGQRIGRRSDWKKAYVTLKEGQNLDFVGGAE | null | null | cytoplasmic translation [GO:0002181]; ribosomal large subunit assembly [GO:0000027] | cytoplasm [GO:0005737]; cytosolic large ribosomal subunit [GO:0022625] | rRNA binding [GO:0019843]; structural constituent of ribosome [GO:0003735] | PF00276; | 3.30.70.330; | Universal ribosomal protein uL23 family | null | null | null | null | null | null | null | FUNCTION: One of the early assembly proteins, it binds 23S rRNA; is essential for growth. One of the proteins that surround the polypeptide exit tunnel on the outside of the subunit. Acts as the docking site for trigger factor (PubMed:12226666) for Ffh binding to the ribosome (SRP54) (PubMed:12756233, PubMed:12702815) ... | Escherichia coli (strain K12) |
P0ADZ4 | RS15_ECOLI | MSLSTEATAKIVSEFGRDANDTGSTEVQVALLTAQINHLQGHFAEHKKDHHSRRGLLRMVSQRRKLLDYLKRKDVARYTQLIERLGLRR | null | null | cytoplasmic translation [GO:0002181]; ribosomal small subunit assembly [GO:0000028]; translation [GO:0006412] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic small ribosomal subunit [GO:0022627] | mRNA base-pairing translational repressor activity [GO:1903231]; rRNA binding [GO:0019843]; small ribosomal subunit rRNA binding [GO:0070181]; structural constituent of ribosome [GO:0003735] | PF00312; | 6.10.250.3130;1.10.287.10; | Universal ribosomal protein uS15 family | null | null | null | null | null | null | null | FUNCTION: One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it helps nucleate assembly of the platform of the 30S subunit by binding and bridging several RNA helices of the 16S rRNA (PubMed:12809609, PubMed:16272117). Binds to its own mRNA, stabilizing it 5-UTR and preventing its translation... | Escherichia coli (strain K12) |
P0AE01 | TRMJ_ECOLI | MLQNIRIVLVETSHTGNMGSVARAMKTMGLTNLWLVNPLVKPDSQAIALAAGASDVIGNAHIVDTLDEALAGCSLVVGTSARSRTLPWPMLDPRECGLKSVAEAANTPVALVFGRERVGLTNEELQKCHYHVAIAANPEYSSLNLAMAVQVIAYEVRMAWLATQENGEQVEHEETPYPLVDDLERFYGHLEQTLLATGFIRENHPGQVMNKLRRLFTRARPESQELNILRGILASIEQQNKGNKAE | 2.1.1.200 | null | tRNA nucleoside ribose methylation [GO:0002128] | cytosol [GO:0005829] | protein homodimerization activity [GO:0042803]; RNA binding [GO:0003723]; tRNA (uracil-2'-O-)-methyltransferase activity [GO:0052665] | PF00588; | 1.10.8.590;3.40.1280.10; | Class IV-like SAM-binding methyltransferase superfamily, RNA methyltransferase TrmH family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=cytidine(32) in tRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(32) in tRNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:42932, Rhea:RHEA-COMP:10288, Rhea:RHEA-COMP:10289, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74495, ChEBI:CHEBI:82748; EC=2.1.1.200;... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.67 uM for tRNA(fMet1) {ECO:0000269|PubMed:26202969}; KM=0.81 uM for tRNA(fMet2) {ECO:0000269|PubMed:26202969}; KM=0.94 uM for tRNA(Trp1) {ECO:0000269|PubMed:26202969}; KM=9.88 uM for tRNA(Gln1) {ECO:0000269|PubMed:26202969}; KM=5.79 uM for tRNA(Gln2) {ECO:0000269... | null | null | null | FUNCTION: Catalyzes the formation of 2'O-methylated cytidine (Cm32) or 2'O-methylated uridine (Um32) at position 32 in tRNA (PubMed:16848900, PubMed:24951554, PubMed:26202969). Can also methylate adenosine or guanosine, even though these nucleosides are rare or absent at position 32 in the anticodon loop of tRNA (PubMe... | Escherichia coli (strain K12) |
P0AE05 | AADB1_KLEPN | MDTTQVTLIHKILAAADERNLPLWIGGGWAIDARLGRVTRKHDDIDLTFPGERRGELEAIVEMLGGRVMEELDYGFLAEIGDELLDCEPAWWADEAYEIAEAPQGSCPEAAEGVIAGRPVRCNSWEAIIWDYFYYADEVPPVDWPTKHIESYRLACTSLGAEKVEVLRAAFRSRYAA | 2.7.7.46 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:25564464, ECO:0007744|PDB:4WQK, ECO:0007744|PDB:4WQL}; Note=Binds 2 Mg(2+). {ECO:0000269|PubMed:25564464}; | response to antibiotic [GO:0046677] | null | aminoglycoside 2''-nucleotidyltransferase activity [GO:0008871]; metal ion binding [GO:0046872] | PF10706; | 3.30.460.40; | null | null | null | CATALYTIC ACTIVITY: Reaction=nucleoside triphosphate + gentamicin = diphosphate + 2''-nucleotidylgentamicin.; EC=2.7.7.46; Evidence={ECO:0000269|PubMed:2850441, ECO:0000305|PubMed:25564464}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=23.9 uM for kanamycin B {ECO:0000269|PubMed:25564464}; KM=35 uM for ATP {ECO:0000269|PubMed:25564464}; Note=kcat is 15.3 sec(-1) for ATP and 5.2 sec(-1) for kanamycin B. {ECO:0000269|PubMed:25564464}; | null | null | null | FUNCTION: Mediates bacterial resistance to kanamycin, gentamicin, dibekacin, sisomicin and tobramycin by adenylating the 2''-hydroxyl group of these antibiotics. {ECO:0000269|PubMed:25564464, ECO:0000269|PubMed:2850441, ECO:0000269|Ref.2}. | Klebsiella pneumoniae |
P0AE06 | ACRA_ECOLI | MNKNRGFTPLAVVLMLSGSLALTGCDDKQAQQGGQQMPAVGVVTVKTEPLQITTELPGRTSAYRIAEVRPQVSGIILKRNFKEGSDIEAGVSLYQIDPATYQATYDSAKGDLAKAQAAANIAQLTVNRYQKLLGTQYISKQEYDQALADAQQANAAVTAAKAAVETARINLAYTKVTSPISGRIGKSNVTEGALVQNGQATALATVQQLDPIYVDVTQSSNDFLRLKQELANGTLKQENGKAKVSLITSDGIKFPQDGTLEFSDVTVDQTTGSITLRAIFPNPDHTLLPGMFVRARLEEGLNPNAILVPQQGVTRTPRGD... | null | null | bile acid and bile salt transport [GO:0015721]; response to antibiotic [GO:0046677]; xenobiotic detoxification by transmembrane export across the cell outer membrane [GO:0140330]; xenobiotic transport [GO:0042908] | efflux pump complex [GO:1990281]; outer membrane-bounded periplasmic space [GO:0030288]; periplasmic side of plasma membrane [GO:0098567] | identical protein binding [GO:0042802]; transmembrane transporter activity [GO:0022857] | PF00529;PF16576; | 2.40.30.170;2.40.420.20;2.40.50.100;1.10.287.470; | Membrane fusion protein (MFP) (TC 8.A.1) family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15228545, ECO:0000269|PubMed:16079137}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303, ECO:0000269|PubMed:15228545, ECO:0000269|PubMed:16079137}. Note=An unlipidated version of this protein (directed to the periplasm by the OmpA signal sequence) functio... | null | null | null | null | null | FUNCTION: AcrA-AcrB-AcrZ-TolC is a drug efflux protein complex with broad substrate specificity that uses the proton motive force to export substrates. This subunit may act as an adapter protein that links AcrB and TolC stably together. It is elongated in shape, being long enough to span the periplasm. {ECO:0000269|Pub... | Escherichia coli (strain K12) |
P0AE08 | AHPC_ECOLI | MSLINTKIKPFKNQAFKNGEFIEITEKDTEGRWSVFFFYPADFTFVCPTELGDVADHYEELQKLGVDVYAVSTDTHFTHKAWHSSSETIAKIKYAMIGDPTGALTRNFDNMREDEGLADRATFVVDPQGIIQAIEVTAEGIGRDASDLLRKIKAAQYVASHPGEVCPAKWKEGEATLAPSLDLVGKI | 1.11.1.26 | null | cell redox homeostasis [GO:0045454]; cellular response to sulfate starvation [GO:0009970]; hydrogen peroxide catabolic process [GO:0042744]; response to alkyl hydroperoxide [GO:0033195]; response to hydroperoxide [GO:0033194]; response to oxidative stress [GO:0006979]; siderophore biosynthetic process [GO:0019290] | alkyl hydroperoxide reductase complex [GO:0009321]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020] | hydroperoxide reductase activity [GO:0032843]; identical protein binding [GO:0042802]; NADH-dependent peroxiredoxin activity [GO:0102039]; oxidoreductase activity, acting on peroxide as acceptor [GO:0016684]; peroxidase activity [GO:0004601]; thioredoxin peroxidase activity [GO:0008379] | PF10417;PF00578; | 3.40.30.10; | Peroxiredoxin family, AhpC/Prx1 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7499381}. | CATALYTIC ACTIVITY: Reaction=a hydroperoxide + H(+) + NADH = an alcohol + H2O + NAD(+); Xref=Rhea:RHEA:62628, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.11.1.26; Evidence={ECO:0000269|PubMed:11717276}; | null | null | null | null | FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. Is the primary scavenger for endogenously generated hydrogen peroxides. {ECO:0000269|Pu... | Escherichia coli (strain K12) |
P0AE12 | AMN_ECOLI | MNNKGSGLTPAQALDKLDALYEQSVVALRNAIGNYITSGELPDENARKQGLFVYPSLTVTWDGSTTNPPKTRAFGRFTHAGSYTTTITRPTLFRSYLNEQLTLLYQDYGAHISVQPSQHEIPYPYVIDGSELTLDRSMSAGLTRYFPTTELAQIGDETADGIYHPTEFSPLSHFDARRVDFSLARLRHYTGTPVEHFQPFVLFTNYTRYVDEFVRWGCSQILDPDSPYIALSCAGGNWITAETEAPEEAISDLAWKKHQMPAWHLITADGQGITLVNIGVGPSNAKTICDHLAVLRPDVWLMIGHCGGLRESQAIGDYVL... | 3.2.2.4 | null | AMP salvage [GO:0044209]; nucleoside metabolic process [GO:0009116] | cytosol [GO:0005829] | AMP nucleosidase activity [GO:0008714] | PF10423;PF01048; | 3.30.1730.10;3.40.50.1580; | AMP nucleosidase family | null | null | CATALYTIC ACTIVITY: Reaction=AMP + H2O = adenine + D-ribose 5-phosphate; Xref=Rhea:RHEA:20129, ChEBI:CHEBI:15377, ChEBI:CHEBI:16708, ChEBI:CHEBI:78346, ChEBI:CHEBI:456215; EC=3.2.2.4; Evidence={ECO:0000255|HAMAP-Rule:MF_01932, ECO:0000269|PubMed:7000783}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=15 mM for AMP (in the absence of Mg-ATP) {ECO:0000269|PubMed:7000783}; KM=0.09 mM for AMP (in the presence of saturating Mg-ATP) {ECO:0000269|PubMed:7000783}; | null | null | null | FUNCTION: Catalyzes the hydrolysis of the N-glycosidic bond of AMP to form adenine and ribose 5-phosphate. Involved in regulation of AMP concentrations. {ECO:0000255|HAMAP-Rule:MF_01932, ECO:0000269|PubMed:7000783}. | Escherichia coli (strain K12) |
P0AE18 | MAP1_ECOLI | MAISIKTPEDIEKMRVAGRLAAEVLEMIEPYVKPGVSTGELDRICNDYIVNEQHAVSACLGYHGYPKSVCISINEVVCHGIPDDAKLLKDGDIVNIDVTVIKDGFHGDTSKMFIVGKPTIMGERLCRITQESLYLALRMVKPGINLREIGAAIQKFVEAEGFSVVREYCGHGIGRGFHEEPQVLHYDSRETNVVLKPGMTFTIEPMVNAGKKEIRTMKDGWTVKTKDRSLSAQYEHTIVVTDNGCEILTLRKDDTIPAIISHDE | 3.4.11.18 | COFACTOR: Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000255|HAMAP-Rule:MF_01974, ECO:0000269|PubMed:10387007, ECO:0000269|PubMed:10460163, ECO:0000269|PubMed:10555963, ECO:0000269|PubMed:10736182, ECO:0000269|PubMed:17120228, ECO:0000269|PubMed:20017927}; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000... | proteolysis [GO:0006508] | cytosol [GO:0005829] | ferrous iron binding [GO:0008198]; initiator methionyl aminopeptidase activity [GO:0004239]; metalloaminopeptidase activity [GO:0070006] | PF00557; | 3.90.230.10; | Peptidase M24A family, Methionine aminopeptidase type 1 subfamily | null | null | CATALYTIC ACTIVITY: Reaction=Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.; EC=3.4.11.18; Evidence={ECO:0000255|HAMAP-Rule:MF_01974, ECO:0000269|PubMed:17120228, ECO:0000269|PubMed:20521764, ECO:0000269|PubMed:3027045}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2 mM for a Met-Gly-Met-Met peptide (for the Fe(2+)-complexed enzyme) {ECO:0000269|PubMed:10460163, ECO:0000269|PubMed:12755633, ECO:0000269|PubMed:18855426, ECO:0000269|PubMed:19019076}; KM=1.3 mM for a Met-Gly-Met-Met peptide (for the Mn(2+)-complexed enzyme) {ECO... | null | null | null | FUNCTION: Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrol... | Escherichia coli (strain K12) |
P0AE22 | APHA_ECOLI | MRKITQAISAVCLLFALNSSAVALASSPSPLNPGTNVARLAEQAPIHWVSVAQIENSLAGRPPMAVGFDIDDTVLFSSPGFWRGKKTFSPESEDYLKNPVFWEKMNNGWDEFSIPKEVARQLIDMHVRRGDAIFFVTGRSPTKTETVSKTLADNFHIPATNMNPVIFAGDKPGQNTKSQWLQDKNIRIFYGDSDNDITAARDVGARGIRILRASNSTYKPLPQAGAFGEEVIVNSEY | 3.1.3.2 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:14687572, ECO:0000269|PubMed:16330049, ECO:0000269|PubMed:18845157}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:14687572, ECO:0000269|PubMed:16330049, ECO:0000269|PubMed:18845157}; | null | outer membrane-bounded periplasmic space [GO:0030288] | acid phosphatase activity [GO:0003993]; identical protein binding [GO:0042802]; L-phosphoserine phosphatase activity [GO:0036424]; magnesium ion binding [GO:0000287] | PF03767; | 3.40.50.1000; | Class B bacterial acid phosphatase family | null | SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:9011040}. | CATALYTIC ACTIVITY: Reaction=a phosphate monoester + H2O = an alcohol + phosphate; Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.2; Evidence={ECO:0000269|PubMed:12777773, ECO:0000269|PubMed:16297670, ECO:0000269|PubMed:18845157, ECO:0000269|PubMed:9011040}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3 uM for 5'-AMP (at 37 degrees Celsius) {ECO:0000269|PubMed:16297670, ECO:0000269|PubMed:9011040}; KM=15 uM for 5'-GMP (at 37 degrees Celsius) {ECO:0000269|PubMed:16297670, ECO:0000269|PubMed:9011040}; KM=15 uM for 5'-UMP (at 37 degrees Celsius) {ECO:0000269|PubMed... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6-6.5 with 5'-AMP as substrate, and pH 5.5-6 with 3'-AMP or pNPP as substrate. {ECO:0000269|PubMed:16297670, ECO:0000269|PubMed:9011040}; | null | FUNCTION: Dephosphorylates several organic phosphate monoesters including 3'- and 5'-nucleotides, 2'-deoxy-5'-nucleotides, pNPP, phenyl phosphate, glycerol 2-phosphate, ribose 5-phosphate, O-phospho-L-amino acids and phytic acid, showing the highest activity with aryl phosphoesters (pNPP, phenyl phosphate and O-phospho... | Escherichia coli (strain K12) |
P0AE24 | ARAE_ECOLI | MVTINTESALTPRSLRDTRRMNMFVSVAAAVAGLLFGLDIGVIAGALPFITDHFVLTSRLQEWVVSSMMLGAAIGALFNGWLSFRLGRKYSLMAGAILFVLGSIGSAFATSVEMLIAARVVLGIAVGIASYTAPLYLSEMASENVRGKMISMYQLMVTLGIVLAFLSDTAFSYSGNWRAMLGVLALPAVLLIILVVFLPNSPRWLAEKGRHIEAEEVLRMLRDTSEKAREELNEIRESLKLKQGGWALFKINRNVRRAVFLGMLLQAMQQFTGMNIIMYYAPRIFKMAGFTTTEQQMIATLVVGLTFMFATFIAVFTVDK... | null | null | fucose transmembrane transport [GO:0015756]; L-arabinose transmembrane transport [GO:0042882]; transmembrane transport [GO:0055085] | membrane [GO:0016020]; plasma membrane [GO:0005886] | fucose transmembrane transporter activity [GO:0015150]; glucose transmembrane transporter activity [GO:0005355]; L-arabinose transmembrane transporter activity [GO:0015147]; symporter activity [GO:0015293] | PF00083; | 1.20.1250.20; | Major facilitator superfamily, Sugar transporter (TC 2.A.1.1) family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:2836407, ECO:0000269|PubMed:7030324}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=H(+)(in) + L-arabinose(in) = H(+)(out) + L-arabinose(out); Xref=Rhea:RHEA:28951, ChEBI:CHEBI:15378, ChEBI:CHEBI:17535; Evidence={ECO:0000269|PubMed:2836407, ECO:0000269|PubMed:6282256}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28953; Evidence={ECO:0000269|PubMed:2836407, ECO:000... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=316.6 uM for arabinose (in membrane vesicles) {ECO:0000269|PubMed:6282256}; Vmax=24.8 nmol/min/mg enzyme (in membrane vesicles) {ECO:0000269|PubMed:6282256}; | null | null | null | FUNCTION: Uptake of L-arabinose across the cytoplasmic membrane with the concomitant transport of protons into the cell (symport system) (PubMed:2836407, PubMed:6282256, PubMed:7030324). D-fucose, a nonmetabolizable analog of L-arabinose, is also a good substrate (PubMed:6282256). {ECO:0000269|PubMed:2836407, ECO:00002... | Escherichia coli (strain K12) |
P0AE52 | BCP_ECOLI | MNPLKAGDIAPKFSLPDQDGEQVNLTDFQGQRVLVYFYPKAMTPGCTVQACGLRDNMDELKKAGVDVLGISTDKPEKLSRFAEKELLNFTLLSDEDHQVCEQFGVWGEKSFMGKTYDGIHRISFLIDADGKIEHVFDDFKTSNHHDVVLNWLKEHA | 1.11.1.24 | null | cell redox homeostasis [GO:0045454]; cellular response to oxidative stress [GO:0034599]; response to oxidative stress [GO:0006979] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | hydroperoxide reductase activity [GO:0032843]; thioredoxin peroxidase activity [GO:0008379] | PF00578; | 3.40.30.10; | Peroxiredoxin family, BCP/PrxQ subfamily | null | null | CATALYTIC ACTIVITY: Reaction=[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62620, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:50058; EC=1.11.1.24; Evidence={ECO:0000269|PubMed:1... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=76.1 uM for H(2)O(2) (using glutathione Grx1 as electron donor) {ECO:0000269|PubMed:21910476}; KM=99.5 uM for cumene hydroperoxide (using glutathione Grx1 as electron donor) {ECO:0000269|PubMed:21910476}; KM=6800 uM for tert-butyl hydroperoxide (using glutathione G... | null | null | null | FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. {ECO:0000269|PubMed:219104... | Escherichia coli (strain K12) |
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