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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
P0A9N4 | PFLA_ECOLI | MSVIGRIHSFESCGTVDGPGIRFITFFQGCLMRCLYCHNRDTWDTHGGKEVTVEDLMKEVVTYRHFMNASGGGVTASGGEAILQAEFVRDWFRACKKEGIHTCLDTNGFVRRYDPVIDELLEVTDLVMLDLKQMNDEIHQNLVGVSNHRTLEFAKYLANKNVKVWIRYVVVPGWSDDDDSAHRLGEFTRDMGNVEKIELLPYHELGKHKWVAMGEEYKLDGVKPPKKETMERVKGILEQYGHKVMF | 1.97.1.4 | COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000269|PubMed:18852451}; Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. {ECO:0000269|PubMed:18852451}; | DNA damage response [GO:0006974]; glucose metabolic process [GO:0006006]; protein maturation [GO:0051604] | cytosol [GO:0005829] | 4 iron, 4 sulfur cluster binding [GO:0051539]; [formate-C-acetyltransferase]-activating enzyme activity [GO:0043365]; oxidoreductase activity [GO:0016491]; potassium ion binding [GO:0030955] | PF13353;PF04055; | 3.20.20.70; | Organic radical-activating enzymes family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=glycyl-[formate C-acetyltransferase] + reduced [flavodoxin] + S-adenosyl-L-methionine = 5'-deoxyadenosine + glycin-2-yl radical-[formate C-acetyltransferase] + H(+) + L-methionine + semiquinone [flavodoxin]; Xref=Rhea:RHEA:19225, Rhea:RHEA-COMP:10622, Rhea:RHEA-COMP:12190, Rhea:RHEA-COMP:12... | null | null | null | null | FUNCTION: Activation of pyruvate formate-lyase 1 under anaerobic conditions by generation of an organic free radical, using S-adenosylmethionine and reduced flavodoxin as cosubstrates to produce 5'-deoxy-adenosine. | Escherichia coli (strain K12) |
P0A9N8 | NRDG_ECOLI | MNYHQYYPVDIVNGPGTRCTLFVSGCVHECPGCYNKSTWRVNSGQPFTKAMEDQIINDLNDTRIKRQGISLSGGDPLHPQNVPDILKLVQRIRAECPGKDIWVWTGYKLDELNAAQMQVVDLINVLVDGKFVQDLKDPSLIWRGSSNQVVHHLR | 1.97.1.- | COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000269|PubMed:10821845, ECO:0000269|PubMed:7852304, ECO:0000269|PubMed:8621608, ECO:0000269|PubMed:9305874}; Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. {ECO:0000250|UniPro... | 2'-deoxyribonucleotide biosynthetic process [GO:0009265]; nucleobase-containing small molecule interconversion [GO:0015949] | anaerobic ribonucleoside-triphosphate reductase complex [GO:0031250] | 4 iron, 4 sulfur cluster binding [GO:0051539]; [formate-C-acetyltransferase]-activating enzyme activity [GO:0043365]; iron-sulfur cluster binding [GO:0051536]; metal ion binding [GO:0046872]; ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor [GO:0004748] | PF13353; | 3.20.20.70; | Organic radical-activating enzymes family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=glycyl-[protein] + reduced [flavodoxin] + S-adenosyl-L-methionine = 5'-deoxyadenosine + glycin-2-yl radical-[protein] + H(+) + L-methionine + semiquinone [flavodoxin]; Xref=Rhea:RHEA:61976, Rhea:RHEA-COMP:10622, Rhea:RHEA-COMP:14480, Rhea:RHEA-COMP:15993, Rhea:RHEA-COMP:15994, ChEBI:CHEBI:1... | null | null | null | null | FUNCTION: Activation of anaerobic ribonucleoside-triphosphate reductase under anaerobic conditions by generation of an organic free radical, using S-adenosylmethionine and reduced flavodoxin as cosubstrates to produce 5'-deoxy-adenosine. {ECO:0000269|PubMed:1460049, ECO:0000269|PubMed:7852304, ECO:0000269|PubMed:930587... | Escherichia coli (strain K12) |
P0A9P0 | DLDH_ECOLI | MSTEIKTQVVVLGAGPAGYSAAFRCADLGLETVIVERYNTLGGVCLNVGCIPSKALLHVAKVIEEAKALAEHGIVFGEPKTDIDKIRTWKEKVINQLTGGLAGMAKGRKVKVVNGLGKFTGANTLEVEGENGKTVINFDNAIIAAGSRPIQLPFIPHEDPRIWDSTDALELKEVPERLLVMGGGIIGLEMGTVYHALGSQIDVVEMFDQVIPAADKDIVKVFTKRISKKFNLMLETKVTAVEAKEDGIYVTMEGKKAPAEPQRYDAVLVAIGRVPNGKNLDAGKAGVEVDDRGFIRVDKQLRTNVPHIFAIGDIVGQPML... | 1.8.1.4 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250}; Note=Binds 1 FAD per subunit. {ECO:0000250}; | 2-oxoglutarate metabolic process [GO:0006103]; glycine decarboxylation via glycine cleavage system [GO:0019464]; one-carbon metabolic process [GO:0006730]; pyruvate catabolic process [GO:0042867]; pyruvate metabolic process [GO:0006090]; response to oxidative stress [GO:0006979]; tricarboxylic acid cycle [GO:0006099] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic oxoglutarate dehydrogenase complex [GO:0045248]; cytosolic pyruvate dehydrogenase complex [GO:0045250]; glycine cleavage complex [GO:0005960]; membrane [GO:0016020]; oxoglutarate dehydrogenase complex [GO:0045252]; plasma membrane [GO:0005886]; pyruvate dehydrogen... | dihydrolipoyl dehydrogenase activity [GO:0004148]; disulfide oxidoreductase activity [GO:0015036]; flavin adenine dinucleotide binding [GO:0050660]; identical protein binding [GO:0042802]; zinc ion binding [GO:0008270] | PF07992;PF02852; | 3.30.390.30;3.50.50.60; | Class-I pyridine nucleotide-disulfide oxidoreductase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16079137}. Cell inner membrane {ECO:0000269|PubMed:16079137}; Peripheral membrane protein {ECO:0000269|PubMed:16079137}. | CATALYTIC ACTIVITY: Reaction=N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] + NAD(+) = H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[protein] + NADH; Xref=Rhea:RHEA:15045, Rhea:RHEA-COMP:10474, Rhea:RHEA-COMP:10475, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:83099, ChEBI:CHEBI:83100; EC=1.8.1.4; | null | null | null | null | FUNCTION: Lipoamide dehydrogenase is a component of the glycine cleavage system as well as of the alpha-ketoacid dehydrogenase complexes. | Escherichia coli (strain K12) |
P0A9P4 | TRXB_ECOLI | MGTTKHSKLLILGSGPAGYTAAVYAARANLQPVLITGMEKGGQLTTTTEVENWPGDPNDLTGPLLMERMHEHATKFETEIIFDHINKVDLQNRPFRLNGDNGEYTCDALIIATGASARYLGLPSEEAFKGRGVSACATCDGFFYRNQKVAVIGGGNTAVEEALYLSNIASEVHLIHRRDGFRAEKILIKRLMDKVENGNIILHTNRTLEEVTGDQMGVTGVRLRDTQNSDNIESLDVAGLFVAIGHSPNTAIFEGQLELENGYIKVQSGIHGNATQTSIPGVFAAGDVMDHIYRQAITSAGTGCMAALDAERYLDGLADA... | 1.8.1.9 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:8114095}; Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:8114095}; | cell redox homeostasis [GO:0045454]; removal of superoxide radicals [GO:0019430] | cytosol [GO:0005829]; thioredoxin-disulfide reductase complex [GO:1902515] | flavin adenine dinucleotide binding [GO:0050660]; thioredoxin-disulfide reductase (NADP) activity [GO:0004791] | PF07992; | 3.50.50.60; | Class-II pyridine nucleotide-disulfide oxidoreductase family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=[thioredoxin]-dithiol + NADP(+) = [thioredoxin]-disulfide + H(+) + NADPH; Xref=Rhea:RHEA:20345, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.9; | null | null | null | null | null | Escherichia coli (strain K12) |
P0A9P6 | DEAD_ECOLI | MAEFETTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLQNLDPELKAPQILVLAPTRELAVQVAEAMTDFSKHMRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMRKNEALVRFLEAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNY... | 3.6.4.13 | null | cellular response to cold [GO:0070417]; mRNA stabilization [GO:0048255]; positive regulation of translation [GO:0045727]; response to cold [GO:0009409]; response to radiation [GO:0009314]; RNA catabolic process [GO:0006401] | cytosol [GO:0005829]; ribosome [GO:0005840] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; protein homodimerization activity [GO:0042803]; RNA helicase activity [GO:0003724]; RNA strand annealing activity [GO:0033592] | PF03880;PF00270;PF12343;PF00271; | 3.30.70.330;3.40.50.300; | DEAD box helicase family, DeaD/CsdA subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00964, ECO:0000269|PubMed:8552679}. | 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=3.6.4.13; Evidence={ECO:0000255|HAMAP-Rule:MF_00964, ECO:0000269|PubMed:15196029, ECO:0000269|PubMed:17259309}; | null | null | null | null | FUNCTION: DEAD-box RNA helicase involved in various cellular processes at low temperature, including ribosome biogenesis, mRNA degradation and translation initiation. Exhibits RNA-stimulated ATP hydrolysis and RNA unwinding activity at low temperature. Involved in 50S ribosomal subunit assembly, acting after SrmB, and ... | Escherichia coli (strain K12) |
P0A9Q1 | ARCA_ECOLI | MQTPHILIVEDELVTRNTLKSIFEAEGYDVFEATDGAEMHQILSEYDINLVIMDINLPGKNGLLLARELREQANVALMFLTGRDNEVDKILGLEIGADDYITKPFNPRELTIRARNLLSRTMNLGTVSEERRSVESYKFNGWELDINSRSLIGPDGEQYKLPRSEFRAMLHFCENPGKIQSRAELLKKMTGRELKPHDRTVDVTIRRIRKHFESTPDTPEIIATIHGEGYRFCGDLED | null | null | negative regulation of DNA-templated transcription [GO:0045892]; phosphorelay signal transduction system [GO:0000160]; positive regulation of DNA-templated transcription [GO:0045893]; regulation of DNA-templated transcription [GO:0006355] | cytosol [GO:0005829]; protein-DNA complex [GO:0032993] | DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription repressor activity [GO:0001217]; identical protein binding [GO:0042802]; phosphorelay response regulator activity [GO:0000156]; transcription cis-regulatory region binding [GO:0000976] | PF00072;PF00486; | 3.40.50.2300;6.10.250.690;1.10.10.10; | null | PTM: Phosphorylated by ArcB. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | null | null | null | null | null | FUNCTION: Member of the two-component regulatory system ArcB/ArcA. Represses a wide variety of aerobic enzymes under anaerobic conditions. Controls the resistance of E.coli to dyes; required for expression of the alkaline phosphatase and sex factor F genes; it may also be involved in the osmoregulation of envelope prot... | Escherichia coli (strain K12) |
P0A9Q5 | ACCD_ECOLI | MSWIERIKSNITPTRKASIPEGVWTKCDSCGQVLYRAELERNLEVCPKCDHHMRMTARNRLHSLLDEGSLVELGSELEPKDVLKFRDSKKYKDRLASAQKETGEKDALVVMKGTLYGMPVVAAAFEFAFMGGSMGSVVGARFVRAVEQALEDNCPLICFSASGGARMQEALMSLMQMAKTSAALAKMQERGLPYISVLTDPTMGGVSASFAMLGDLNIAEPKALIGFAGPRVIEQTVREKLPPGFQRSEFLIEKGAIDMIVRRPEMRLKLASILAKLMNLPAPNPEAPREGVVVPPVPDQEPEA | 2.1.3.15 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_01395, ECO:0000269|PubMed:19965770}; Note=Binds 1 zinc ion per subunit. The zinc is involved in both translation regulation via mRNA-binding and catalysis. {ECO:0000255|HAMAP-Rule:MF_01395, ECO:0000269|PubMed:19965770}; | fatty acid biosynthetic process [GO:0006633]; long-chain fatty acid biosynthetic process [GO:0042759]; malonyl-CoA biosynthetic process [GO:2001295]; negative regulation of translation [GO:0017148] | acetate CoA-transferase complex [GO:0009329]; acetyl-CoA carboxylase complex [GO:0009317]; cytosol [GO:0005829] | acetyl-CoA carboxylase activity [GO:0003989]; ATP binding [GO:0005524]; carboxyl- or carbamoyltransferase activity [GO:0016743]; DNA binding [GO:0003677]; mRNA binding [GO:0003729]; zinc ion binding [GO:0008270] | PF01039;PF17848; | null | AccD/PCCB family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein]; Xref=Rhea:RHEA:54728, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145; EC=2.1.3.15; Evidence={ECO:0000255|HAMAP-Rule:MF... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=40 uM for malonyl-CoA {ECO:0000269|PubMed:15066985, ECO:0000269|PubMed:19965770}; KM=11.4 mM for biocytin {ECO:0000269|PubMed:15066985, ECO:0000269|PubMed:19965770}; | PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01395}. | null | null | FUNCTION: Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA.; FUNCTION: Controls translation of mRNA for both itself a... | Escherichia coli (strain K12) |
P0A9Q7 | ADHE_ECOLI | MAVTNVAELNALVERVKKAQREYASFTQEQVDKIFRAAALAAADARIPLAKMAVAESGMGIVEDKVIKNHFASEYIYNAYKDEKTCGVLSEDDTFGTITIAEPIGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKDATNKAADIVLQAAIAAGAPKDLIGWIDQPSVELSNALMHHPDINLILATGGPGMVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVASVLMSKTFDNGVICASEQSVVVVDSVYDAVRERFATHGGYLLQGKELKAVQDVILKNGALNAAIVGQPAYKIAELAGFSVPENTKILI... | 1.1.1.1; 1.2.1.10 | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000269|PubMed:1325457, ECO:0000269|PubMed:2015910, ECO:0000269|PubMed:32188856}; | carbon utilization [GO:0015976]; ethanol biosynthetic process [GO:0006115]; mixed acid fermentation [GO:0019664]; protein homooligomerization [GO:0051260]; response to oxidative stress [GO:0006979] | cytosol [GO:0005829]; membrane [GO:0016020] | acetaldehyde dehydrogenase (acetylating) activity [GO:0008774]; alcohol dehydrogenase (NAD+) activity [GO:0004022]; alcohol dehydrogenase activity, iron-dependent [GO:0004025]; ferrous iron binding [GO:0008198]; identical protein binding [GO:0042802] | PF00171;PF00465; | 3.40.50.1970;1.20.1090.10; | Aldehyde dehydrogenase family; Iron-containing alcohol dehydrogenase family | null | null | CATALYTIC ACTIVITY: Reaction=acetaldehyde + CoA + NAD(+) = acetyl-CoA + H(+) + NADH; Xref=Rhea:RHEA:23288, ChEBI:CHEBI:15343, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.2.1.10; Evidence={ECO:0000269|PubMed:10612730, ECO:0000269|PubMed:10922373, ECO:0000269|PubMed... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5.4 mM for acetaldehyde (for acetaldehyde dehydrogenase activity) {ECO:0000269|PubMed:10922373}; KM=240 mM for ethanol (for ethanol dehydrogenase activity) {ECO:0000269|PubMed:10922373}; | null | null | null | FUNCTION: Under fermentative conditions, catalyzes the sequential NADH-dependent reduction of acetyl-CoA to acetaldehyde and then to ethanol (PubMed:10612730, PubMed:10922373, PubMed:17280641, PubMed:2015910, PubMed:6752127). Under aerobic conditions, despite the reversibility of the two NADH-coupled reactions, wild-ty... | Escherichia coli (strain K12) |
P0A9Q8 | ADHE_ECO57 | MAVTNVAELNALVERVKKAQREYASFTQEQVDKIFRAAALAAADARIPLAKMAVAESGMGIVEDKVIKNHFASEYIYNAYKDEKTCGVLSEDDTFGTITIAEPIGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKDATNKAADIVLQAAIAAGAPKDLIGWIDQPSVELSNALMHHPDINLILATGGPGMVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVASVLMSKTFDNGVICASEQSVVVVDSVYDAVRERFATHGGYLLQGKELKAVQDVILKNGALNAAIVGQPAYKIAELAGFSVPENTKILI... | 1.1.1.1; 1.2.1.10 | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000269|PubMed:32880589}; | alcohol metabolic process [GO:0006066]; carbon utilization [GO:0015976] | null | acetaldehyde dehydrogenase (acetylating) activity [GO:0008774]; alcohol dehydrogenase (NAD+) activity [GO:0004022]; metal ion binding [GO:0046872] | PF00171;PF00465; | 3.40.50.1970;1.20.1090.10; | Aldehyde dehydrogenase family; Iron-containing alcohol dehydrogenase family | null | null | CATALYTIC ACTIVITY: Reaction=acetaldehyde + CoA + NAD(+) = acetyl-CoA + H(+) + NADH; Xref=Rhea:RHEA:23288, ChEBI:CHEBI:15343, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.2.1.10; Evidence={ECO:0000250|UniProtKB:P0A9Q7}; PhysiologicalDirection=right-to-left; Xref=Rh... | null | null | null | null | FUNCTION: Under fermentative conditions, catalyzes the sequential NADH-dependent reduction of acetyl-CoA to acetaldehyde and then to ethanol (By similarity). Plays an important role in virulence and is critical for proper regulation of virulence gene expression (PubMed:24846743). {ECO:0000250|UniProtKB:P0A9Q7, ECO:0000... | Escherichia coli O157:H7 |
P0A9Q9 | DHAS_ECOLI | MKNVGFIGWRGMVGSVLMQRMVEERDFDAIRPVFFSTSQLGQAAPSFGGTTGTLQDAFDLEALKALDIIVTCQGGDYTNEIYPKLRESGWQGYWIDAASSLRMKDDAIIILDPVNQDVITDGLNNGIRTFVGGNCTVSLMLMSLGGLFANDLVDWVSVATYQAASGGGARHMRELLTQMGHLYGHVADELATPSSAILDIERKVTTLTRSGELPVDNFGVPLAGSLIPWIDKQLDNGQSREEWKGQAETNKILNTSSVIPVDGLCVRVGALRCHSQAFTIKLKKDVSIPTVEELLAAHNPWAKVVPNDREITMRELTPAA... | 1.2.1.11 | null | 'de novo' L-methionine biosynthetic process [GO:0071266]; diaminopimelate biosynthetic process [GO:0019877]; DNA damage response [GO:0006974]; homoserine biosynthetic process [GO:0009090]; isoleucine biosynthetic process [GO:0009097]; lysine biosynthetic process via diaminopimelate [GO:0009089]; threonine biosynthetic ... | cytosol [GO:0005829] | aspartate-semialdehyde dehydrogenase activity [GO:0004073]; NAD binding [GO:0051287]; NADP binding [GO:0050661]; protein dimerization activity [GO:0046983] | PF01118;PF02774; | 3.40.50.720; | Aspartate-semialdehyde dehydrogenase family | null | null | CATALYTIC ACTIVITY: Reaction=L-aspartate 4-semialdehyde + NADP(+) + phosphate = 4-phospho-L-aspartate + H(+) + NADPH; Xref=Rhea:RHEA:24284, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57535, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:537519; EC=1.2.1.11; Evidence={ECO:0000269|PubMed:11368768, ECO:0000269|P... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=22 uM for L-4-aspartyl phosphate {ECO:0000269|PubMed:11368768}; KM=29 uM for NADPH {ECO:0000269|PubMed:11368768}; KM=110 uM for L-aspartate 4-semialdehyde {ECO:0000269|PubMed:11368768}; KM=144 uM for NADP(+) {ECO:0000269|PubMed:11368768}; KM=10.2 mM for phosphate {... | PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4. {ECO:0000255|HAMAP-Rule:MF_02121}.; PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 2/3. {ECO:0000255|HAMAP-Rule:MF_02121}.... | null | null | FUNCTION: Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate. {ECO:0000269|PubMed:11368768, ECO:0000269|PubMed:6102909}. | Escherichia coli (strain K12) |
P0A9R4 | FER_ECOLI | MPKIVILPHQDLCPDGAVLEANSGETILDAALRNGIEIEHACEKSCACTTCHCIVREGFDSLPESSEQEDDMLDKAWGLEPESRLSCQARVTDEDLVVEIPRYTINHAREH | null | COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Note=Binds 1 [2Fe-2S] cluster.; | electron transport chain [GO:0022900]; iron-sulfur cluster assembly [GO:0016226]; P450-containing electron transport chain [GO:0140647] | cytosol [GO:0005829] | 2 iron, 2 sulfur cluster binding [GO:0051537]; electron transfer activity [GO:0009055]; metal ion binding [GO:0046872] | PF00111; | 3.10.20.30; | Adrenodoxin/putidaredoxin family | null | null | null | null | null | null | null | FUNCTION: Ferredoxin are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. Although the function of this ferredoxin is unknown it is probable that it has a role as a cellular electron transfer protein. Involved in the in vivo assembly of the Fe-S clusters in a wide variety of iron-s... | Escherichia coli (strain K12) |
P0A9R7 | FTSE_ECOLI | MIRFEHVSKAYLGGRQALQGVTFHMQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDINLISRRSYRMLTLSDGHLHGGVGHE | 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]; response to antibiotic [GO:0046677]; transmembrane transport [GO:0055085] | ATPase complex [GO:1904949]; cell division site [GO:0032153]; cytoplasm [GO:0005737]; division septum [GO:0000935]; divisome complex [GO:1990586]; extrinsic component of membrane [GO:0019898]; plasma membrane [GO:0005886]; plasma membrane protein complex [GO:0098797] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; transmembrane transporter activity [GO:0022857] | PF00005; | 3.40.50.300; | ABC transporter superfamily | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:10048040, ECO:0000269|PubMed:3323846}; Peripheral membrane protein {ECO:0000269|PubMed:10048040}; Cytoplasmic side {ECO:0000305}. Note=Associated with the membrane through an interaction with FtsX (PubMed:10048040). Localizes to the septal ring at the later ... | 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. {ECO:0000269|PubMed:14729705}. | Escherichia coli (strain K12) |
P0A9S1 | FUCO_ECOLI | MANRMILNETAWFGRGAVGALTDEVKRRGYQKALIVTDKTLVQCGVVAKVTDKMDAAGLAWAIYDGVVPNPTITVVKEGLGVFQNSGADYLIAIGGGSPQDTCKAIGIISNNPEFADVRSLEGLSPTNKPSVPILAIPTTAGTAAEVTINYVITDEEKRRKFVCVDPHDIPQVAFIDADMMDGMPPALKAATGVDALTHAIEGYITRGAWALTDALHIKAIEIIAGALRGSVAGDKDAGEEMALGQYVAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMRYNADFTGEKYRDIARVMGVKVEGMSLEEARN... | 1.1.1.77 | COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000269|PubMed:15995211}; | glycol catabolic process [GO:0042846]; L-fucose catabolic process [GO:0042355]; propanediol metabolic process [GO:0051143]; rhamnose catabolic process [GO:0019301] | cytosol [GO:0005829] | alcohol dehydrogenase (NAD+) activity [GO:0004022]; ferrous iron binding [GO:0008198]; lactaldehyde reductase activity [GO:0008912]; nucleotide binding [GO:0000166]; protein homodimerization activity [GO:0042803]; R-lactaldehyde reductase activity [GO:0052660]; S-lactaldehyde reductase activity [GO:0052661] | PF00465; | 3.40.50.1970;1.20.1090.10; | Iron-containing alcohol dehydrogenase family | null | null | CATALYTIC ACTIVITY: Reaction=(R)-propane-1,2-diol + NAD(+) = (R)-lactaldehyde + H(+) + NADH; Xref=Rhea:RHEA:23872, ChEBI:CHEBI:15378, ChEBI:CHEBI:17167, ChEBI:CHEBI:28972, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.77; CATALYTIC ACTIVITY: Reaction=(S)-propane-1,2-diol + NAD(+) = (S)-lactaldehyde + H(+) + NADH; Xref... | null | PATHWAY: Carbohydrate degradation; L-fucose degradation. | null | null | null | Escherichia coli (strain K12) |
P0A9S5 | GLDA_ECOLI | MDRIIQSPGKYIQGADVINRLGEYLKPLAERWLVVGDKFVLGFAQSTVEKSFKDAGLVVEIAPFGGECSQNEIDRLRGIAETAQCGAILGIGGGKTLDTAKALAHFMGVPVAIAPTIASTDAPCSALSVIYTDEGEFDRYLLLPNNPNMVIVDTKIVAGAPARLLAAGIGDALATWFEARACSRSGATTMAGGKCTQAALALAELCYNTLLEEGEKAMLAAEQHVVTPALERVIEANTYLSGVGFESGGLAAAHAVHNGLTAIPDAHHYYHGEKVAFGTLTQLVLENAPVEEIETVAALSHAVGLPITLAQLDIKEDVPA... | 1.1.1.6; 1.1.1.75 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305|PubMed:30839292}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:30839292}; | anaerobic glycerol catabolic process [GO:0019588]; methylglyoxal catabolic process [GO:0051596]; protein homotetramerization [GO:0051289] | cytosol [GO:0005829]; protein-containing complex [GO:0032991] | (R)-aminopropanol dehydrogenase activity [GO:0019147]; glycerol dehydrogenase [NAD+] activity [GO:0008888]; identical protein binding [GO:0042802]; zinc ion binding [GO:0008270] | PF00465; | 3.40.50.1970;1.20.1090.10; | Iron-containing alcohol dehydrogenase family | null | null | CATALYTIC ACTIVITY: Reaction=glycerol + NAD(+) = dihydroxyacetone + H(+) + NADH; Xref=Rhea:RHEA:13769, ChEBI:CHEBI:15378, ChEBI:CHEBI:16016, ChEBI:CHEBI:17754, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.6; Evidence={ECO:0000269|PubMed:18179582, ECO:0000269|PubMed:3920199, ECO:0000269|PubMed:40950, ECO:0000269|PubMe... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.8 mM for DL-1,2-propanediol {ECO:0000269|PubMed:6365902}; KM=8 mM for DL-1,2-butanediol {ECO:0000269|PubMed:6365902}; KM=14.5 mM for D-1-amino-2-propanol {ECO:0000269|PubMed:6365902}; KM=56 mM for glycerol (at 25 degrees Celsius and pH 7) {ECO:0000269|PubMed:1817... | PATHWAY: Polyol metabolism; glycerol fermentation; glycerone phosphate from glycerol (oxidative route): step 1/2. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.5-6.0 for dihydroxyacetone reduction and 9.5-10.0 for glycerol oxidation (PubMed:40950). Optimum pH is 10.0-10.2 for 1-amino-2-propanol oxidation (for homooctameric form) (PubMed:6365902). {ECO:0000269|PubMed:40950, ECO:0000269|PubMed:6365902}; | null | FUNCTION: Catalyzes the NAD-dependent oxidation of glycerol to dihydroxyacetone (glycerone) (PubMed:18179582, PubMed:3920199, PubMed:40950, PubMed:6365902, PubMed:8132480). Allows microorganisms to utilize glycerol as a source of carbon under anaerobic conditions (PubMed:18632294). In E.coli, an important role of GldA ... | Escherichia coli (strain K12) |
P0A9S7 | LIVG_ECOLI | MSQPLLSVNGLMMRFGGLLAVNNVNLELYPQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRDQHLEGLPGQQIARMGVVRTFQHVRLFREMTVIENLLVAQHQQLKTGLFSGLLKTPSFRRAQSEALDRAATWLERIGLLEHANRQASNLAYGDQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNHHNTTILLIEHDMKLVMGISDRIYVVNQGTPLANGTPEQIRNNPDVIRAYLGEA | null | null | branched-chain amino acid transport [GO:0015803]; D-alanine transmembrane transport [GO:0042941]; isoleucine transmembrane transport [GO:1903714]; L-alanine transport [GO:0015808]; L-isoleucine import across plasma membrane [GO:1903806]; L-valine import across plasma membrane [GO:1903805]; L-valine transmembrane transp... | ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing [GO:0055052]; membrane [GO:0016020]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; branched-chain amino acid transmembrane transporter activity [GO:0015658]; L-isoleucine transmembrane transporter activity [GO:0015188]; L-phenylalanine transmembrane transporter activity [GO:0015192]; L-valine transmembrane transporter activity [GO:000530... | PF00005;PF12399; | 3.40.50.300; | ABC transporter superfamily | null | null | null | null | null | null | null | FUNCTION: Component of the leucine-specific transport system. | Escherichia coli (strain K12) |
P0A9T0 | SERA_ECOLI | MAKVSLEKDKIKFLLVEGVHQKALESLRAAGYTNIEFHKGALDDEQLKESIRDAHFIGLRSRTHLTEDVINAAEKLVAIGCFCIGTNQVDLDAAAKRGIPVFNAPFSNTRSVAELVIGELLLLLRGVPEANAKAHRGVWNKLAAGSFEARGKKLGIIGYGHIGTQLGILAESLGMYVYFYDIENKLPLGNATQVQHLSDLLNMSDVVSLHVPENPSTKNMMGAKEISLMKPGSLLINASRGTVVDIPALCDALASKHLAGAAIDVFPTEPATNSDPFTSPLCEFDNVLLTPHIGGSTQEAQENIGLEVAGKLIKYSDNGS... | 1.1.1.399; 1.1.1.95 | null | L-serine biosynthetic process [GO:0006564] | cytosol [GO:0005829] | 2-hydroxyglutarate dehydrogenase activity [GO:0047545]; identical protein binding [GO:0042802]; NAD+ binding [GO:0070403]; NADH binding [GO:0070404]; phosphoglycerate dehydrogenase activity [GO:0004617]; serine binding [GO:0070905] | PF00389;PF02826;PF01842; | 3.30.70.260;3.40.50.720; | D-isomer specific 2-hydroxyacid dehydrogenase family | null | null | CATALYTIC ACTIVITY: Reaction=(2R)-3-phosphoglycerate + NAD(+) = 3-phosphooxypyruvate + H(+) + NADH; Xref=Rhea:RHEA:12641, ChEBI:CHEBI:15378, ChEBI:CHEBI:18110, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58272; EC=1.1.1.95; Evidence={ECO:0000269|PubMed:8550422}; CATALYTIC ACTIVITY: Reaction=(R)-2-hydroxyglutarate... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.2 mM for 3-phospho-D-glycerate {ECO:0000269|PubMed:8550422}; KM=3.2 uM for 3-phosphonooxypyruvate {ECO:0000269|PubMed:8550422}; KM=88 uM for 2-oxoglutarate {ECO:0000269|PubMed:8550422}; KM=0.37 mM for (R)-2-hydroxyglutarate {ECO:0000269|PubMed:8550422}; KM=2.9 mM... | PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 1/3. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5 for the reductase activities and 9.0 for the dehydrogenase activities. {ECO:0000269|PubMed:8550422}; | null | FUNCTION: Catalyzes the reversible oxidation of 3-phospho-D-glycerate to 3-phosphonooxypyruvate, the first step of the phosphorylated L-serine biosynthesis pathway. Also catalyzes the reversible oxidation of 2-hydroxyglutarate to 2-oxoglutarate. {ECO:0000269|PubMed:8550422}. | Escherichia coli (strain K12) |
P0A9V1 | LPTB_ECOLI | MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDDDISLLPLHARARRGIGYLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVYLGEDFRL | 7.5.2.- | null | Gram-negative-bacterium-type cell outer membrane assembly [GO:0043165]; lipopolysaccharide transport [GO:0015920]; transmembrane transport [GO:0055085] | ATP-binding cassette (ABC) transporter complex [GO:0043190]; cytoplasm [GO:0005737]; membrane [GO:0016020]; plasma membrane [GO:0005886]; transporter complex [GO:1990351] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887] | PF00005;PF12399; | 3.40.50.300; | ABC transporter superfamily, Outer membrane lipopolysaccharide export (TC 1.B.42) family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16079137}. Cell inner membrane {ECO:0000269|PubMed:16079137}; Peripheral membrane protein {ECO:0000269|PubMed:16079137}; Cytoplasmic side {ECO:0000269|PubMed:16079137}. | null | null | null | null | null | FUNCTION: Part of the ABC transporter complex LptBFG involved in the translocation of lipopolysaccharide (LPS) from the inner membrane to the outer membrane. Probably responsible for energy coupling to the transport system. {ECO:0000269|PubMed:16765569, ECO:0000269|PubMed:17056748, ECO:0000269|PubMed:18424520}. | Escherichia coli (strain K12) |
P0A9V8 | SQUU_ECOLI | MAAIAFIGLGQMGSPMASNLLQQGHQLRVFDVNAEAVRHLVDKGATPAANPAQAAKDAEFIITMLPNGDLVRNVLFGENGVCEGLSTDALVIDMSTIHPLQTDKLIADMQAKGFSMMDVPVGRTSANAITGTLLLLAGGTAEQVERATPILMAMGSELINAGGPGMGIRVKLINNYMSIALNALSAEAAVLCEALNLPFDVAVKVMSGTAAGKGHFTTSWPNKVLSGDLSPAFMIDLAHKDLGIALDVANQLHVPMPLGAASREVYSQARAAGRGRQDWSAILEQVRVSAGMTAKVKM | 1.1.1.373; 1.1.1.61 | null | 6-sulfoquinovose(1-) catabolic process [GO:1902777]; 6-sulfoquinovose(1-) catabolic process to glycerone phosphate and 3-sulfolactaldehyde [GO:0061720]; protein homotetramerization [GO:0051289]; toxin catabolic process [GO:0009407]; valine catabolic process [GO:0006574] | protein-containing complex [GO:0032991] | 3-hydroxyisobutyrate dehydrogenase activity [GO:0008442]; 3-sulfolactaldehyde reductase activity [GO:0061596]; 4-hydroxybutyrate dehydrogenase activity [GO:0047577]; identical protein binding [GO:0042802]; NAD binding [GO:0051287]; NADP binding [GO:0050661]; oxidoreductase activity, acting on the CH-OH group of donors,... | PF14833;PF03446; | 3.40.50.720; | HIBADH-related family, 3-sulfolactaldehyde reductase subfamily | null | null | CATALYTIC ACTIVITY: Reaction=(2S)-3-sulfopropanediol + NAD(+) = (2S)-3-sulfolactaldehyde + H(+) + NADH; Xref=Rhea:RHEA:40511, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:90109, ChEBI:CHEBI:176527; EC=1.1.1.373; Evidence={ECO:0000255|HAMAP-Rule:MF_01913, ECO:0000269|PubMed:24463506, ECO:0000269|... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.3 mM for 3-sulfolactaldehyde {ECO:0000269|Ref.6}; KM=0.082 mM for NADH {ECO:0000269|Ref.6}; KM=4.3 mM for succinic semialdehyde {ECO:0000269|PubMed:19372223}; KM=9 mM for methylglyoxal {ECO:0000269|PubMed:19372223}; KM=102 mM for 4-hydroxybutyrate {ECO:0000269|Pu... | null | null | null | FUNCTION: Reduces 3-sulfolactaldehyde (SLA) to 2,3-dihydroxypropane 1-sulfonate (DHPS) (PubMed:24463506, Ref.6). Metabolite profiling studies showed that the enzyme also catalyzes in vitro the NADH-dependent reduction of succinic semialdehyde (SSA) to 4-hydroxybutyrate (GHB), and that it could be involved in the metabo... | Escherichia coli (strain K12) |
P0A9W3 | ETTA_ECOLI | MAQFVYTMHRVGKVVPPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEARPQPDIKIGYLPQEPQLNPEHTVRESIEEAVSEVVNALKRLDEVYALYADPDADFDKLAAEQGRLEEIIQAHDGHNLNVQLERAADALRLPDWDAKIANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFEGTVVAITHDRYFLDNVAGWILELDRGEGIPWEGNYSSWLEQKDQRLAQEASQEAARRKSIEKELEWVRQGTKGRQSKGKARLARFEELNSTEYQKRNETNELFIPPGPRLG... | 3.6.1.- | null | negative regulation of translational elongation [GO:0045900]; translation [GO:0006412] | cytoplasm [GO:0005737] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ribosome binding [GO:0043022]; rRNA binding [GO:0019843]; tRNA binding [GO:0000049] | PF00005;PF12848; | 3.40.50.300; | ABC transporter superfamily, ABCF family, Translational throttle EttA subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00847, ECO:0000269|PubMed:24389466}. Note=Associates with ribosomes and polysomes. {ECO:0000255|HAMAP-Rule:MF_00847}. | 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; Evidence={ECO:0000255|HAMAP-Rule:MF_00847, ECO:0000269|PubMed:24389465}; | null | null | null | null | FUNCTION: A translation factor that gates the progression of the 70S ribosomal initiation complex (IC, containing tRNA(fMet) in the P-site) into the translation elongation cycle by using a mechanism sensitive to the ATP/ADP ratio. Binds to the 70S ribosome E-site where it modulates the state of the translating ribosome... | Escherichia coli (strain K12) |
P0A9X4 | MREB_ECOLI | MLKKFRGMFSNDLSIDLGTANTLIYVKGQGIVLNEPSVVAIRQDRAGSPKSVAAVGHDAKQMLGRTPGNIAAIRPMKDGVIADFFVTEKMLQHFIKQVHSNSFMRPSPRVLVCVPVGATQVERRAIRESAQGAGAREVFLIEEPMAAAIGAGLPVSEATGSMVVDIGGGTTEVAVISLNGVVYSSSVRIGGDRFDEAIINYVRRNYGSLIGEATAERIKHEIGSAYPGDEVREIEVRGRNLAEGVPRGFTLNSNEILEALQEPLTGIVSAVMVALEQCPPELASDISERGMVLTGGGALLRNLDRLLMEETGIPVVVAED... | null | null | cell morphogenesis [GO:0000902]; FtsZ-dependent cytokinesis [GO:0043093]; negative regulation of cell division [GO:0051782]; peptidoglycan biosynthetic process [GO:0009252]; regulation of cell shape [GO:0008360]; regulation of chromosome segregation [GO:0051983] | cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; plasma membrane [GO:0005886]; polymeric cytoskeletal fiber [GO:0099513] | ATP binding [GO:0005524]; identical protein binding [GO:0042802] | PF06723; | 3.30.420.40; | FtsA/MreB family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15612918}. Note=Membrane-associated (PubMed:15612918). Preferentially localizes to regions of negative curvature (PubMed:24550515). May associate with the membrane via MreC (PubMed:15612918). Localization depends on MreC, MreD and RodA (PubMed:15612918). {ECO:0000269|... | null | null | null | null | null | FUNCTION: Forms membrane-associated dynamic filaments that are essential for cell shape determination (PubMed:15612918, PubMed:21903929). Acts by regulating cell wall synthesis and cell elongation, and thus cell shape (PubMed:21903929). A feedback loop between cell geometry and MreB localization maintains elongated cel... | Escherichia coli (strain K12) |
P0A9X9 | CSPA_ECOLI | MSGKMTGIVKWFNADKGFGFITPDDGSKDVFVHFSAIQNDGYKSLDEGQKVSFTIESGAKGPAAGNVTSL | null | null | negative regulation of termination of DNA-templated transcription [GO:0060567]; positive regulation of DNA-templated transcription [GO:0045893]; regulation of gene expression [GO:0010468]; response to cold [GO:0009409] | cytosol [GO:0005829] | DNA binding [GO:0003677]; nucleic acid binding [GO:0003676]; RNA binding [GO:0003723]; single-stranded DNA binding [GO:0003697]; single-stranded RNA binding [GO:0003727]; transcription antitermination factor activity, RNA binding [GO:0001072] | PF00313; | 2.40.50.140; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:2404279}. | null | null | null | null | null | FUNCTION: Binds to and stimulates the transcription of the CCAAT-containing, cold-shock-inducible promoters of the H-NS and GyrA proteins. Binds also to the inverted repeat 5'-ATTGG-3'. {ECO:0000269|PubMed:1961761}. | Escherichia coli (strain K12) |
P0A9Y6 | CSPC_ECOLI | MAKIKGQVKWFNESKGFGFITPADGSKDVFVHFSAIQGNGFKTLAEGQNVEFEIQDGQKGPAAVNVTAI | null | null | cellular response to heat [GO:0034605]; negative regulation of termination of DNA-templated transcription [GO:0060567]; regulation of gene expression [GO:0010468] | cytosol [GO:0005829]; membrane [GO:0016020] | nucleic acid binding [GO:0003676]; protein homodimerization activity [GO:0042803]; protein-folding chaperone binding [GO:0051087]; RNA binding [GO:0003723]; single-stranded DNA binding [GO:0003697]; transcription antitermination factor activity, RNA binding [GO:0001072] | PF00313; | 2.40.50.140; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | null | null | null | null | null | null | Escherichia coli (strain K12) |
P0A9Z1 | GLNB_ECOLI | MKKIDAIIKPFKLDDVREALAEVGITGMTVTEVKGFGRQKGHTELYRGAEYMVDFLPKVKIEIVVPDDIVDTCVDTIIRTAQTGKIGDGKIFVFDVARVIRIRTGEEDDAAI | null | null | regulation of fatty acid biosynthetic process [GO:0042304]; regulation of nitrogen utilization [GO:0006808] | cytosol [GO:0005829] | ATP binding [GO:0005524]; enzyme activator activity [GO:0008047]; enzyme regulator activity [GO:0030234]; identical protein binding [GO:0042802]; small molecule binding [GO:0036094] | PF00543; | 3.30.70.120; | P(II) protein family | PTM: Uridylylated/deuridylylated by GlnD. | null | null | null | null | null | null | FUNCTION: P-II indirectly controls the transcription of the glutamine synthetase gene (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of GlnA. When P-II is uridylylated to P-II-UMP, these events are reversed. When the ratio of Gln to 2-ketoglutarate decreases, P... | Escherichia coli (strain K12) |
P0AA04 | PTHP_ECOLI | MFQQEVTITAPNGLHTRPAAQFVKEAKGFTSEITVTSNGKSASAKSLFKLQTLGLTQGTVVTISAEGEDEQKAVEHLVKLMAELE | null | null | phosphoenolpyruvate-dependent sugar phosphotransferase system [GO:0009401]; positive regulation of glycogen catabolic process [GO:0045819]; regulation of carbon utilization [GO:0043609] | cytosol [GO:0005829] | antisigma factor binding [GO:0045152]; enzyme activator activity [GO:0008047]; enzyme inhibitor activity [GO:0004857]; enzyme regulator activity [GO:0030234]; phosphotransferase activity, nitrogenous group as acceptor [GO:0016775] | PF00381; | 3.30.1340.10; | HPr family | null | SUBCELLULAR LOCATION: Cytoplasm. | null | null | null | null | null | FUNCTION: General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The phosphoryl gr... | Escherichia coli (strain K12) |
P0AA10 | RL13_ECOLI | MKTFTAKPETVKRDWYVVDATGKTLGRLATELARRLRGKHKAEYTPHVDTGDYIIVLNADKVAVTGNKRTDKVYYHHTGHIGGIKQATFEEMIARRPERVIEIAVKGMLPKGPLGRAMFRKLKVYAGNEHNHAAQQPQVLDI | null | null | cytoplasmic translation [GO:0002181]; negative regulation of translation [GO:0017148] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625]; ribosome [GO:0005840] | large ribosomal subunit rRNA binding [GO:0070180]; mRNA 5'-UTR binding [GO:0048027]; mRNA binding [GO:0003729]; structural constituent of ribosome [GO:0003735]; zinc ion binding [GO:0008270] | PF00572; | 3.90.1180.10; | Universal ribosomal protein uL13 family | null | null | null | null | null | null | null | FUNCTION: This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly. {ECO:0000269|PubMed:3298242}. | Escherichia coli (strain K12) |
P0AA16 | OMPR_ECOLI | MQENYKILVVDDDMRLRALLERYLTEQGFQVRSVANAEQMDRLLTRESFHLMVLDLMLPGEDGLSICRRLRSQSNPMPIIMVTAKGEEVDRIVGLEIGADDYIPKPFNPRELLARIRAVLRRQANELPGAPSQEEAVIAFGKFKLNLGTREMFREDEPMPLTSGEFAVLKALVSHPREPLSRDKLMNLARGREYSAMERSIDVQISRLRRMVEEDPAHPRYIQTVWGLGYVFVPDGSKA | null | null | phosphorelay signal transduction system [GO:0000160]; positive regulation of DNA-templated transcription [GO:0045893]; regulation of DNA-templated transcription [GO:0006355] | cytosol [GO:0005829]; protein-DNA complex [GO:0032993] | phosphorelay response regulator activity [GO:0000156]; transcription cis-regulatory region binding [GO:0000976] | PF00072;PF00486; | 3.40.50.2300;6.10.250.690;1.10.10.10; | null | PTM: Phosphorylated by EnvZ (PubMed:2277041, PubMed:2656684, PubMed:2668281, PubMed:2674113, PubMed:7934854). Asp-55 is the primary phosphate acceptor site, but Asp-11 may also serve as a phosphorylation site, particularly in the absence of Asp-55 (Probable) (PubMed:7934854). Phosphorylation stimulates the DNA-binding ... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:3533941}. | null | null | null | null | null | FUNCTION: Member of the two-component regulatory system EnvZ/OmpR involved in osmoregulation (particularly of genes ompF and ompC) as well as other genes (PubMed:3010044, PubMed:3536870). Plays a central role in both acid and osmotic stress responses (PubMed:28526842, PubMed:30524381). Binds AT-rich DNA (PubMed:1063311... | Escherichia coli (strain K12) |
P0AA25 | THIO_ECOLI | MSDKIIHLTDDSFDTDVLKADGAILVDFWAEWCGPCKMIAPILDEIADEYQGKLTVAKLNIDQNPGTAPKYGIRGIPTLLLFKNGEVAATKVGALSKGQLKEFLDANLA | null | null | cell redox homeostasis [GO:0045454] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | DNA polymerase processivity factor activity [GO:0030337]; protein-disulfide reductase activity [GO:0015035] | PF00085; | 3.40.30.10; | Thioredoxin family | null | null | null | null | null | null | null | FUNCTION: Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. | Escherichia coli (strain K12) |
P0AA37 | RLUA_ECOLI | MGMENYNPPQEPWLVILYQDDHIMVVNKPSGLLSVPGRLEEHKDSVMTRIQRDYPQAESVHRLDMATSGVIVVALTKAAERELKRQFREREPKKQYVARVWGHPSPAEGLVDLPLICDWPNRPKQKVCYETGKPAQTEYEVVEYAADNTARVVLKPITGRSHQLRVHMLALGHPILGDRFYASPEARAMAPRLLLHAEMLTITHPAYGNSMTFKAPADF | 5.4.99.28; 5.4.99.29 | null | enzyme-directed rRNA pseudouridine synthesis [GO:0000455]; pseudouridine synthesis [GO:0001522]; RNA modification [GO:0009451]; rRNA processing [GO:0006364]; rRNA pseudouridine synthesis [GO:0031118]; tRNA processing [GO:0008033]; tRNA pseudouridine synthesis [GO:0031119] | null | 23S rRNA pseudouridine(746) synthase activity [GO:0160142]; pseudouridine synthase activity [GO:0009982]; RNA binding [GO:0003723]; rRNA pseudouridine synthase activity [GO:0120159]; tRNA pseudouridine synthase activity [GO:0106029] | PF00849; | 3.30.2350.10; | Pseudouridine synthase RluA family | null | null | CATALYTIC ACTIVITY: Reaction=uridine(32) in tRNA = pseudouridine(32) in tRNA; Xref=Rhea:RHEA:42544, Rhea:RHEA-COMP:10107, Rhea:RHEA-COMP:10108, ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; EC=5.4.99.28; Evidence={ECO:0000269|PubMed:7493321}; CATALYTIC ACTIVITY: Reaction=uridine(746) in 23S rRNA = pseudouridine(746) in 23S rRN... | null | null | null | null | FUNCTION: Dual specificity enzyme that catalyzes the synthesis of pseudouridine from uracil-746 in 23S ribosomal RNA and from uracil-32 in the anticodon stem and loop of transfer RNAs. {ECO:0000269|PubMed:10383384, ECO:0000269|PubMed:7493321}. | Escherichia coli (strain K12) |
P0AA41 | TRUC_ECOLI | MLEILYQDEWLVAVNKPSGWLVHRSWLDRDEKVVVMQTVRDQIGQHVFTAHRLDRPTSGVLLMGLSSEAGRLLAQQFEQHQIQKRYHAIVRGWLMEEAVLDYPLVEELDKIADKFAREDKGPQPAVTHYRGLATVEMPVATGRYPTTRYGLVELEPKTGRKHQLRRHLAHLRHPIIGDSKHGDLRQNRSGAEHFGLQRLMLHASQLSLTHPFTGEPLTIHAGLDDTWMQALSQFGWRGLLPENERVEFSAPSGQDGEISS | 5.4.99.26 | null | enzyme-directed rRNA pseudouridine synthesis [GO:0000455]; RNA modification [GO:0009451]; tRNA metabolic process [GO:0006399]; tRNA processing [GO:0008033]; tRNA pseudouridine synthesis [GO:0031119] | cytosol [GO:0005829] | pseudouridine synthase activity [GO:0009982]; RNA binding [GO:0003723]; tRNA pseudouridine synthase activity [GO:0106029] | PF00849; | 3.30.2350.10; | Pseudouridine synthase RluA family | null | null | CATALYTIC ACTIVITY: Reaction=uridine(65) in tRNA = pseudouridine(65) in tRNA; Xref=Rhea:RHEA:42536, Rhea:RHEA-COMP:10103, Rhea:RHEA-COMP:10104, ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; EC=5.4.99.26; Evidence={ECO:0000269|PubMed:11720289}; | null | null | null | null | FUNCTION: Responsible for synthesis of pseudouridine from uracil-65 in transfer RNAs. {ECO:0000269|PubMed:11720289}. | Escherichia coli (strain K12) |
P0AA43 | RSUA_ECOLI | MRLDKFIAQQLGVSRAIAGREIRGNRVTVDGEIVRNAAFKLLPEHDVAYDGNPLAQQHGPRYFMLNKPQGYVCSTDDPDHPTVLYFLDEPVAWKLHAAGRLDIDTTGLVLMTDDGQWSHRITSPRHHCEKTYLVTLESPVADDTAEQFAKGVQLHNEKDLTKPAVLEVITPTQVRLTISEGRYHQVKRMFAAVGNHVVELHRERIGGITLDADLAPGEYRPLTEEEIASVV | 5.4.99.19 | null | enzyme-directed rRNA pseudouridine synthesis [GO:0000455] | cytosol [GO:0005829] | 16S rRNA pseudouridine(516) synthase activity [GO:0160136]; pseudouridine synthase activity [GO:0009982]; RNA binding [GO:0003723]; rRNA pseudouridine synthase activity [GO:0120159] | PF00849;PF01479; | 3.30.70.1560;3.30.70.580;3.10.290.10; | Pseudouridine synthase RsuA family | null | null | CATALYTIC ACTIVITY: Reaction=uridine(516) in 16S rRNA = pseudouridine(516) in 16S rRNA; Xref=Rhea:RHEA:38867, Rhea:RHEA-COMP:10089, Rhea:RHEA-COMP:10090, ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; EC=5.4.99.19; Evidence={ECO:0000269|PubMed:10376875, ECO:0000269|PubMed:7612632}; | null | null | null | null | FUNCTION: Responsible for synthesis of pseudouridine from uracil-516 in 16S ribosomal RNA. {ECO:0000269|PubMed:10376875, ECO:0000269|PubMed:7612632}. | Escherichia coli (strain K12) |
P0AA47 | PLAP_ECOLI | MSHNVTPNTSRVELRKTLTLVPVVMMGLAYMQPMTLFDTFGIVSGLTDGHVPTAYAFALIAILFTALSYGKLVRRYPSAGSAYTYAQKSISPTVGFMVGWSSLLDYLFAPMINILLAKIYFEALVPSIPSWMFVVALVAFMTAFNLRSLKSVANFNTVIVVLQVVLIAVILGMVVYGVFEGEGAGTLASTRPFWSGDAHVIPMITGATILCFSFTGFDGISNLSEETKDAERVIPRAIFLTALIGGMIFIFATYFLQLYFPDISRFKDPDASQPEIMLYVAGKAFQVGALIFSTITVLASGMAAHAGVARLMYVMGRDGV... | null | null | amino acid transport [GO:0006865]; cell motility [GO:0048870]; putrescine transport [GO:0015847] | plasma membrane [GO:0005886] | putrescine transmembrane transporter activity [GO:0015489]; solute:proton symporter activity [GO:0015295] | PF13520; | 1.20.1740.10; | Amino acid-polyamine-organocation (APC) superfamily | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=H(+)(in) + putrescine(in) = H(+)(out) + putrescine(out); Xref=Rhea:RHEA:28891, ChEBI:CHEBI:15378, ChEBI:CHEBI:326268; Evidence={ECO:0000305|PubMed:21266585}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28893; Evidence={ECO:0000305|PubMed:21266585}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=155 uM for putrescine {ECO:0000269|PubMed:21266585}; Vmax=9.3 nmol/min/mg enzyme {ECO:0000269|PubMed:21266585}; | null | null | null | FUNCTION: Putrescine importer. Required for induction of type 1 pili-driven surface motility. {ECO:0000269|PubMed:21266585}. | Escherichia coli (strain K12) |
P0AA76 | DGOT_ECOLI | MDIPVNAAKPGRRRYLTLVMIFITVVICYVDRANLAVASAHIQEEFGITKAEMGYVFSAFAWLYTLCQIPGGWFLDRVGSRVTYFIAIFGWSVATLFQGFATGLMSLIGLRAITGIFEAPAFPTNNRMVTSWFPEHERASAVGFYTSGQFVGLAFLTPLLIWIQEMLSWHWVFIVTGGIGIIWSLIWFKVYQPPRLTKGISKAELDYIRDGGGLVDGDAPVKKEARQPLTAKDWKLVFHRKLIGVYLGQFAVASTLWFFLTWFPNYLTQEKGITALKAGFMTTVPFLAAFVGVLLSGWVADLLVRKGFSLGFARKTPIIC... | null | null | D-galactonate catabolic process [GO:0034194]; D-galactonate transmembrane transport [GO:0042875] | plasma membrane [GO:0005886] | D-galactonate transmembrane transporter activity [GO:0042881]; solute:proton symporter activity [GO:0015295] | PF07690; | 1.20.1250.20; | Major facilitator superfamily, Phthalate permease family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:31083648}; Multi-pass membrane protein {ECO:0000269|PubMed:31083648}. | CATALYTIC ACTIVITY: Reaction=D-galactonate(in) + H(+)(in) = D-galactonate(out) + H(+)(out); Xref=Rhea:RHEA:29835, ChEBI:CHEBI:12931, ChEBI:CHEBI:15378; Evidence={ECO:0000269|PubMed:31083648}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29837; Evidence={ECO:0000269|PubMed:31083648}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=18 uM for D-galactonate {ECO:0000269|PubMed:31083648}; Vmax=1.94 nmol/min/ug enzyme {ECO:0000269|PubMed:31083648}; | null | null | null | FUNCTION: Involved in D-galactonate metabolism (PubMed:211976, PubMed:30455279). Catalyzes the proton-dependent uptake of galactonate into the cell (PubMed:31083648). {ECO:0000269|PubMed:211976, ECO:0000269|PubMed:30455279, ECO:0000269|PubMed:31083648}. | Escherichia coli (strain K12) |
P0AA78 | EXUT_ECOLI | MRKIKGLRWYMIALVTLGTVLGYLTRNTVAAAAPTLMEELNISTQQYSYIIAAYSAAYTVMQPVAGYVLDVLGTKIGYAMFAVLWAVFCGATALAGSWGGLAVARGAVGAAEAAMIPAGLKASSEWFPAKERSIAVGYFNVGSSIGAMIAPPLVVWAIVMHSWQMAFIISGALSFIWAMAWLIFYKHPRDQKHLTDEERDYIINGQEAQHQVSTAKKMSVGQILRNRQFWGIALPRFLAEPAWGTFNAWIPLFMFKVYGFNLKEIAMFAWMPMLFADLGCILGGYLPPLFQRWFGVNLIVSRKMVVTLGAVLMIGPGMIG... | null | null | hexuronate transmembrane transport [GO:0015736] | plasma membrane [GO:0005886] | hexuronate transmembrane transporter activity [GO:0015134] | PF07690; | 1.20.1250.20; | Major facilitator superfamily, Phthalate permease family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=aldehydo-D-glucuronate(in) + H(+)(in) = aldehydo-D-glucuronate(out) + H(+)(out); Xref=Rhea:RHEA:28955, ChEBI:CHEBI:15378, ChEBI:CHEBI:142686; Evidence={ECO:0000305|PubMed:783117}; CATALYTIC ACTIVITY: Reaction=aldehydo-D-galacturonate(out) + H(+)(out) = aldehydo-D-galacturonate(in) + H(+)(in... | null | null | null | null | FUNCTION: Transport of aldohexuronates such as D-glucuronate and D-galacturonate (PubMed:6343797, PubMed:783117). Under anaerobic conditions, can play a critical role as a D-glucose transporter in the absence of sugar-PTS system (PubMed:32038601). {ECO:0000269|PubMed:32038601, ECO:0000269|PubMed:6343797, ECO:0000269|Pu... | Escherichia coli (strain K12) |
P0AA84 | CLSB_ECOLI | MKCSWREGNKIQLLENGEQYYPAVFKAIGEAQERIILETFIWFEDDVGKQLHAALLAAAQRGVKAEVLLDGYGSPDLSDEFVNELTAAGVVFRYYDPRPRLFGMRTNVFRRMHRKIVVIDARIAFIGGLNYSAEHMSSYGPEAKQDYAVRLEGPIVEDILQFELENLPGQSAARRWWRRHHKAEENRQPGEAQVLLVWRDNEEHRDDIERHYLKMLTQARREVIIANAYFFPGYRFLHALRKAARRGVRIKLIIQGEPDMPIVRVGARLLYNYLVKGGVQVFEYRRRPLHGKVALMDDHWATVGSSNLDPLSLSLNLEAN... | 2.7.8.- | null | cardiolipin biosynthetic process [GO:0032049] | membrane [GO:0016020]; plasma membrane [GO:0005886] | cardiolipin synthase activity [GO:0008808]; phospholipase D activity [GO:0004630] | PF13091; | 3.30.870.10; | Phospholipase D family, Cardiolipin synthase subfamily, ClsB sub-subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:10634942}; Peripheral membrane protein {ECO:0000305|PubMed:10634942}. | CATALYTIC ACTIVITY: Reaction=2 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) = a cardiolipin + glycerol; Xref=Rhea:RHEA:31451, ChEBI:CHEBI:17754, ChEBI:CHEBI:62237, ChEBI:CHEBI:64716; Evidence={ECO:0000255|HAMAP-Rule:MF_01917, ECO:0000269|PubMed:10634942}; | null | null | null | null | FUNCTION: Catalyzes the phosphatidyl group transfer from one phosphatidylglycerol molecule to another to form cardiolipin (CL) (diphosphatidylglycerol) and glycerol. Can also catalyze phosphatidyl group transfer to water to form phosphatidate. {ECO:0000255|HAMAP-Rule:MF_01917, ECO:0000269|PubMed:10634942, ECO:0000269|P... | Escherichia coli (strain K12) |
P0AA89 | DOSC_ECOLI | MEMYFKRMKDEWTGLVEQADPPIRAKAAEIAVAHAHYLSIEFYRIVRIDPHAEEFLSNEQVERQLKSAMERWIINVLSAQVDDVERLIQIQHTVAEVHARIGIPVEIVEMGFRVLKKILYPVIFSSDYSAAEKLQVYHFSINSIDIAMEVMTRAFTFSDSSASKEDENYRIFSLLENAEEEKERQIASILSWEIDIIYKILLDSDLGSSLPLSQADFGLWFNHKGRHYFSGIAEVGHISRLIQDFDGIFNQTMRNTRNLNNRSLRVKFLLQIRNTVSQIITLLRELFEEVSRHEVGMDVLTKLLNRRFLPTIFKREIAHA... | 2.7.7.65 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Note=Binds 1 heme group per subunit. The Fe(2+) state binds O(2) and CO while the Fe(3+) state can bind CN(-) and imidazole.; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250}; | cell adhesion involved in single-species biofilm formation [GO:0043709]; negative regulation of bacterial-type flagellum-dependent cell motility [GO:1902201]; response to oxygen levels [GO:0070482] | plasma membrane [GO:0005886] | carbon monoxide binding [GO:0070025]; diguanylate cyclase activity [GO:0052621]; GTP binding [GO:0005525]; heme binding [GO:0020037]; metal ion binding [GO:0046872]; oxygen binding [GO:0019825]; protein homodimerization activity [GO:0042803] | PF21118;PF00990;PF11563; | 3.30.70.270;1.10.490.10; | null | null | null | CATALYTIC ACTIVITY: Reaction=2 GTP = 3',3'-c-di-GMP + 2 diphosphate; Xref=Rhea:RHEA:24898, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:58805; EC=2.7.7.65; Evidence={ECO:0000269|PubMed:19764732, ECO:0000269|PubMed:21067162}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Note=The Fe(III), Fe(II)-O(2), and Fe(II)-CO complexes of DosC display DGC activity with turnover numbers of 0.066, 0.022, and 0.022 min(-1), respectively. The DGC reaction catalyzed by DosC is the rate-determining step for c-di-GMP homeostasis. Binds O(2), CO, cyanid... | PATHWAY: Purine metabolism; 3',5'-cyclic di-GMP biosynthesis. | null | null | FUNCTION: Globin-coupled heme-based oxygen sensor protein displaying diguanylate cyclase (DGC) activity in response to oxygen availability. Thus, catalyzes the synthesis of cyclic diguanylate (c-di-GMP) via the condensation of 2 GTP molecules. Is involved in the modulation of intracellular c-di-GMP levels, in associati... | Escherichia coli (strain K12) |
P0AA93 | YPDA_ECOLI | MHEIFNMLLAVFDRAALMLICLFFLIRIRLFRELLHKSAHSPKELLAVTAIFSLFALFSTWSGVPVEGSLVNVRIIAVMSGGILFGPWVGIITGVIAGIHRYLIDIGGVTAIPCFITSILAGCISGWINLKIPKAQRWRVGILGGMLCETLTMILVIVWAPTTALGIDIVSKIGIPMILGSVCIGFIVLLVQSVEGEKEASAARQAKLALDIANKTLPLFRHVNSESLRKVCEIIRDDIHADAVAITNTDHVLAYVGVGEHNYQNGDDFISPTTRQAMNYGKIIIKNNDEAHRTPEIHSMLVIPLWEKGVVTGTLKIYYC... | 2.7.13.3 | null | cell wall organization [GO:0071555]; cellular response to nutrient [GO:0031670]; signal transduction [GO:0007165] | plasma membrane [GO:0005886] | ATP binding [GO:0005524]; phosphorelay sensor kinase activity [GO:0000155]; protein histidine kinase activity [GO:0004673] | PF07694;PF01590;PF02518;PF06580; | 1.10.1760.20;3.30.450.40;3.30.565.10; | null | PTM: Autophosphorylated. {ECO:0000250}. | 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 YpdA/YpdB, which is part of a nutrient-sensing regulatory network composed of YpdA/YpdB, the high-affinity pyruvate signaling system BtsS/BtsR and their respective target proteins, YhjX and BtsT. YpdA activates YpdB by phosphorylation in response to high concentra... | Escherichia coli (strain K12) |
P0AAB4 | UBID_ECOLI | MDAMKYNDLRDFLTLLEQQGELKRITLPVDPHLEITEIADRTLRAGGPALLFENPKGYSMPVLCNLFGTPKRVAMGMGQEDVSALREVGKLLAFLKEPEPPKGFRDLFDKLPQFKQVLNMPTKRLRGAPCQQKIVSGDDVDLNRIPIMTCWPEDAAPLITWGLTVTRGPHKERQNLGIYRQQLIGKNKLIMRWLSHRGGALDYQEWCAAHPGERFPVSVALGADPATILGAVTPVPDTLSEYAFAGLLRGTKTEVVKCISNDLEVPASAEIVLEGYIEQGETAPEGPYGDHTGYYNEVDSFPVFTVTHITQREDAIYHST... | 4.1.1.98 | COFACTOR: Name=prenyl-FMN; Xref=ChEBI:CHEBI:87746; Evidence={ECO:0000255|HAMAP-Rule:MF_01636, ECO:0000269|PubMed:28057757}; Note=Binds 1 prenylated FMN (prenyl-FMN) per subunit. {ECO:0000255|HAMAP-Rule:MF_01636, ECO:0000269|PubMed:28057757}; COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP-Rul... | cinnamic acid catabolic process [GO:0046281]; ferulate metabolic process [GO:0033494]; protein hexamerization [GO:0034214]; ubiquinone biosynthetic process [GO:0006744]; ubiquinone biosynthetic process from chorismate [GO:0032150] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; plasma membrane [GO:0005886] | 3-octaprenyl-4-hydroxybenzoate carboxy-lyase activity [GO:0008694]; identical protein binding [GO:0042802]; manganese ion binding [GO:0030145]; prenyl-FMNH2 binding [GO:0120233] | PF01977;PF20696;PF20695; | 1.20.5.570;3.40.1670.10; | UbiD family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01636, ECO:0000305|PubMed:782527}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01636, ECO:0000305|PubMed:782527}. | CATALYTIC ACTIVITY: Reaction=a 4-hydroxy-3-all-trans-polyprenylbenzoate + H(+) = a 2-all-trans-polyprenylphenol + CO2; Xref=Rhea:RHEA:41680, Rhea:RHEA-COMP:9514, Rhea:RHEA-COMP:9516, ChEBI:CHEBI:1269, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:78396; EC=4.1.1.98; Evidence={ECO:0000255|HAMAP-Rule:MF_01636, ECO:00... | null | PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01636, ECO:0000269|PubMed:782527}. | null | null | FUNCTION: Catalyzes the decarboxylation of 3-octaprenyl-4-hydroxy benzoate to 2-octaprenylphenol, an intermediate step in ubiquinone biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01636, ECO:0000269|PubMed:782527}. | Escherichia coli (strain K12) |
P0AAC6 | YCCA_ECOLI | MDRIVSSSHDRTSLLSTHKVLRNTYFLLSLTLAFSAITATASTVLMLPSPGLILTLVGMYGLMFLTYKTANKPTGIISAFAFTGFLGYILGPILNTYLSAGMGDVIAMALGGTALVFFCCSAYVLTTRKDMSFLGGMLMAGIVVVLIGMVANIFLQLPALHLAISAVFILISSGAILFETSNIIHGGETNYIRATVSLYVSLYNIFVSLLSILGFASRD | null | null | negative regulation of apoptotic process [GO:0043066]; regulation of proteolysis [GO:0030162] | membrane [GO:0016020]; plasma membrane [GO:0005886] | null | PF01027; | null | BI1 family | PTM: YccA is processively degraded by FtsH; degradation initiates via the approximately 20 residue N-terminal tail in a sequence non-specific manner. The deletion mutant yccA11 is resistant to FtsH-mediated degradation, probably because it is too short to be degraded by FtsH. | SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. Note=There are conflicting results regarding the localization of the C-terminus of this protein: According to a report, the C-terminus localizes in the periplasm (PubMed:10357810). Another report gives the C-terminus in the cytoplasm (PubMed:159199... | null | null | null | null | null | FUNCTION: Negatively modulates the activity of the FtsH protease for membrane substrates. Overexpression or stabilizing YccA counteracts the FtsH-mediated degradation of SecY when the SecYEG preprotein translocator is jammed. {ECO:0000269|PubMed:19661432}. | Escherichia coli (strain K12) |
P0AAC8 | ISCA_ECOLI | MSITLSDSAAARVNTFLANRGKGFGLRLGVRTSGCSGMAYVLEFVDEPTPEDIVFEDKGVKVVVDGKSLQFLDGTQLDFVKEGLNEGFKFTNPNVKDECGCGESFHV | null | COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Note=Binds 2 iron ions per dimer. The dimer may bind additional iron ions.; | iron-sulfur cluster assembly [GO:0016226]; protein maturation by iron-sulfur cluster transfer [GO:0097428] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; iron-sulfur cluster transfer complex [GO:1990230] | 2 iron, 2 sulfur cluster binding [GO:0051537]; ferrous iron binding [GO:0008198]; iron chaperone activity [GO:0034986] | PF01521; | 2.60.300.12; | HesB/IscA family | null | null | null | null | null | null | null | FUNCTION: Is able to transfer iron-sulfur clusters to apo-ferredoxin. Multiple cycles of [2Fe2S] cluster formation and transfer are observed, suggesting that IscA acts catalytically. Recruits intracellular free iron so as to provide iron for the assembly of transient iron-sulfur cluster in IscU in the presence of IscS,... | Escherichia coli (strain K12) |
P0AAD6 | SDAC_ECOLI | METTQTSTIASKDSRSAWRKTDTMWMLGLYGTAIGAGVLFLPINAGVGGMIPLIIMAILAFPMTFFAHRGLTRFVLSGKNPGEDITEVVEEHFGIGAGKLITLLYFFAIYPILLVYSVAITNTVESFMSHQLGMTPPPRAILSLILIVGMMTIVRFGEQMIVKAMSILVFPFVGVLMLLALYLIPQWNGAALETLSLDTASATGNGLWMTLWLAIPVMVFSFNHSPIISSFAVAKREEYGDMAEQKCSKILAFAHIMMVLTVMFFVFSCVLSLTPADLAAAKEQNISILSYLANHFNAPVIAWMAPIIAIIAITKSFLGH... | null | null | L-serine transport [GO:0015825] | plasma membrane [GO:0005886] | L-serine transmembrane transporter activity [GO:0015194]; symporter activity [GO:0015293] | null | null | Amino acid/polyamine transporter 2 family, SdaC/TdcC subfamily | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=H(+)(in) + L-serine(in) = H(+)(out) + L-serine(out); Xref=Rhea:RHEA:28887, ChEBI:CHEBI:15378, ChEBI:CHEBI:33384; Evidence={ECO:0000269|PubMed:3129404}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28889; Evidence={ECO:0000269|PubMed:3129404}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=50 uM for L-serine {ECO:0000269|PubMed:3129404}; Vmax=23 nmol/min/mg enzyme {ECO:0000269|PubMed:3129404}; | null | null | null | FUNCTION: Mediates the import of L-serine into the cell (PubMed:3129404, PubMed:8026499). Is energized by proton cotransport (PubMed:3129404). Promotes amino acid homeostasis during adaptation to glucose limitation (PubMed:31680488). May also be involved in ampicillin sensitivity (Probable). {ECO:0000269|PubMed:3129404... | Escherichia coli (strain K12) |
P0AAD8 | TDCC_ECOLI | MSTSDSIVSSQTKQSSWRKSDTTWTLGLFGTAIGAGVLFFPIRAGFGGLIPILLMLVLAYPIAFYCHRALARLCLSGSNPSGNITETVEEHFGKTGGVVITFLYFFAICPLLWIYGVTITNTFMTFWENQLGFAPLNRGFVALFLLLLMAFVIWFGKDLMVKVMSYLVWPFIASLVLISLSLIPYWNSAVIDQVDLGSLSLTGHDGILITVWLGISIMVFSFNFSPIVSSFVVSKREEYEKDFGRDFTERKCSQIISRASMLMVAVVMFFAFSCLFTLSPANMAEAKAQNIPVLSYLANHFASMTGTKTTFAITLEYAAS... | null | null | amino acid transport [GO:0006865]; L-serine transport [GO:0015825]; threonine transport [GO:0015826] | plasma membrane [GO:0005886] | L-serine transmembrane transporter activity [GO:0015194]; L-threonine transmembrane transporter activity [GO:0015195]; solute:proton symporter activity [GO:0015295]; threonine efflux transmembrane transporter activity [GO:0015565] | PF03222; | null | Amino acid/polyamine transporter 2 family, SdaC/TdcC subfamily | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_01583, ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:2115866}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01583}. | CATALYTIC ACTIVITY: Reaction=H(+)(in) + L-threonine(in) = H(+)(out) + L-threonine(out); Xref=Rhea:RHEA:28883, ChEBI:CHEBI:15378, ChEBI:CHEBI:57926; Evidence={ECO:0000255|HAMAP-Rule:MF_01583, ECO:0000269|PubMed:2115866}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28885; Evidence={ECO:0000255|HAMAP-Rule:MF_0158... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=6 uM for L-threonine {ECO:0000269|PubMed:2115866}; | null | null | null | FUNCTION: Involved in the import of threonine and serine into the cell, with the concomitant import of a proton (symport system). {ECO:0000255|HAMAP-Rule:MF_01583, ECO:0000269|PubMed:2115866, ECO:0000269|PubMed:9498571}. | Escherichia coli (strain K12) |
P0AAE0 | CYCA_ECOLI | MVDQVKVVADDQAPAEQSLRRNLTNRHIQLIAIGGAIGTGLFMGSGKTISLAGPSIIFVYMIIGFMLFFVMRAMGELLLSNLEYKSFSDFASDLLGPWAGYFTGWTYWFCWVVTGMADVVAITAYAQFWFPDLSDWVASLAVIVLLLTLNLATVKMFGEMEFWFAMIKIVAIVSLIVVGLVMVAMHFQSPTGVEASFAHLWNDGGWFPKGLSGFFAGFQIAVFAFVGIELVGTTAAETKDPEKSLPRAINSIPIRIIMFYVFALIVIMSVTPWSSVVPEKSPFVELFVLVGLPAAASVINFVVLTSAASSANSGVFSTSR... | null | null | beta-alanine transport [GO:0001762]; D-alanine transmembrane transport [GO:0042941]; D-serine transmembrane transport [GO:0042942]; glycine transport [GO:0015816]; L-alanine transport [GO:0015808] | plasma membrane [GO:0005886] | beta-alanine transmembrane transporter activity [GO:0001761]; D-alanine transmembrane transporter activity [GO:0042944]; D-serine transmembrane transporter activity [GO:0042945]; glycine transmembrane transporter activity [GO:0015187]; L-alanine transmembrane transporter activity [GO:0015180]; symporter activity [GO:00... | PF00324; | 1.20.1740.10; | Amino acid-polyamine-organocation (APC) superfamily, Amino acid transporter (AAT) (TC 2.A.3.1) family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=D-alanine(in) + H(+)(in) = D-alanine(out) + H(+)(out); Xref=Rhea:RHEA:28903, ChEBI:CHEBI:15378, ChEBI:CHEBI:57416; Evidence={ECO:0000305|PubMed:23316042, ECO:0000305|PubMed:4574696}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28905; Evidence={ECO:0000305|PubMed:23316042, ECO:00003... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.4 mM for beta-alanine {ECO:0000269|PubMed:15221223}; Vmax=46 nmol/min/mg enzyme {ECO:0000269|PubMed:15221223}; | null | null | null | FUNCTION: Permease that is involved in the transport across the cytoplasmic membrane of D-alanine, D-serine, glycine and beta-alanine (PubMed:15221223, PubMed:23316042, PubMed:4574696, PubMed:4583203, PubMed:4926674). Also contributes to L-alanine uptake (PubMed:4574696, PubMed:4583203). In addition, in minimal media, ... | Escherichia coli (strain K12) |
P0AAE8 | CADB_ECOLI | MSSAKKIGLFACTGVVAGNMMGSGIALLPANLASIGGIAIWGWIISIIGAMSLAYVYARLATKNPQQGGPIAYAGEISPAFGFQTGVLYYHANWIGNLAIGITAVSYLSTFFPVLNDPVPAGIACIAIVWVFTFVNMLGGTWVSRLTTIGLVLVLIPVVMTAIVGWHWFDAATYAANWNTADTTDGHAIIKSILLCLWAFVGVESAAVSTGMVKNPKRTVPLATMLGTGLAGIVYIAATQVLSGMYPSSVMAASGAPFAISASTILGNWAAPLVSAFTAFACLTSLGSWMMLVGQAGVRAANDGNFPKVYGEVDSNGIPK... | null | null | cadaverine transport [GO:0015839]; cellular stress response to acidic pH [GO:1990451]; L-lysine transmembrane transport [GO:1903401] | membrane [GO:0016020]; plasma membrane [GO:0005886] | antiporter activity [GO:0015297]; lysine:cadaverine antiporter activity [GO:0043872]; solute:proton symporter activity [GO:0015295] | PF13520; | 1.20.1740.10; | Amino acid-polyamine-organocation (APC) superfamily, Basic amino acid/polyamine antiporter (APA) (TC 2.A.3.2) family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:16877381}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=cadaverine(in) + L-lysine(out) = cadaverine(out) + L-lysine(in); Xref=Rhea:RHEA:28895, ChEBI:CHEBI:32551, ChEBI:CHEBI:58384; Evidence={ECO:0000269|PubMed:14982633, ECO:0000305|PubMed:1556085}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28896; Evidence={ECO:0000269|PubMed:14982633,... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=303 uM for cadaverine (for export activity, at low pH) {ECO:0000269|PubMed:14982633}; KM=390 uM for cadaverine (for export activity) {ECO:0000269|PubMed:16877381}; KM=20.8 uM for cadaverine (for uptake activity, at neutral pH) {ECO:0000269|PubMed:14982633, ECO:0000... | null | null | null | FUNCTION: Under acidic conditions, in the presence of lysine, functions as a cadaverine:lysine antiporter that facilitates the excretion of cadaverine and the uptake of lysine (PubMed:14982633, PubMed:1556085). At neutral pH, also catalyzes the uptake of cadaverine via a proton symport mechanism, however the physiologi... | Escherichia coli (strain K12) |
P0AAF1 | POTE_ECOLI | MSQAKSNKMGVVQLTILTMVNMMGSGIIMLPTKLAEVGTISIISWLVTAVGSMALAWAFAKCGMFSRKSGGMGGYAEYAFGKSGNFMANYTYGVSLLIANVAIAISAVGYGTELLGASLSPVQIGLATIGVLWICTVANFGGARITGQISSITVWGVIIPVVGLCIIGWFWFSPTLYVDSWNPHHAPFFSAVGSSIAMTLWAFLGLESACANTDVVENPERNVPIAVLGGTLGAAVIYIVSTNVIAGIVPNMELANSTAPFGLAFAQMFTPEVGKVIMALMVMSCCGSLLGWQFTIAQVFKSSSDEGYFPKIFSRVTKVD... | null | null | putrescine transport [GO:0015847] | plasma membrane [GO:0005886] | putrescine:ornithine antiporter activity [GO:0015496]; symporter activity [GO:0015293] | PF13520; | 1.20.1740.10; | Amino acid-polyamine-organocation (APC) superfamily, Basic amino acid/polyamine antiporter (APA) (TC 2.A.3.2) family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_02073, ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:9045651, ECO:0000305|PubMed:1939141}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_02073}. | CATALYTIC ACTIVITY: Reaction=H(+)(in) + putrescine(in) = H(+)(out) + putrescine(out); Xref=Rhea:RHEA:28891, ChEBI:CHEBI:15378, ChEBI:CHEBI:326268; Evidence={ECO:0000255|HAMAP-Rule:MF_02073, ECO:0000269|PubMed:9045651}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28893; Evidence={ECO:0000255|HAMAP-Rule:MF_02073... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.8 uM for putrescine (for uptake activity) {ECO:0000269|PubMed:9045651}; KM=73 uM for putrescine (for antiporter activity) {ECO:0000269|PubMed:1584788, ECO:0000269|PubMed:9045651}; KM=108 uM for ornithine (for antiporter activity) {ECO:0000269|PubMed:9045651}; Vma... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5 for uptake activity. Optimum pH is 9.2 for antiporter activity. {ECO:0000269|PubMed:9045651}; | null | FUNCTION: Catalyzes both the uptake and excretion of putrescine. The uptake of putrescine is dependent on the membrane potential and the excretion involves putrescine-ornithine antiporter activity. {ECO:0000255|HAMAP-Rule:MF_02073, ECO:0000269|PubMed:1584788, ECO:0000269|PubMed:1939141, ECO:0000269|PubMed:9045651}. | Escherichia coli (strain K12) |
P0AAG0 | DPPD_ECOLI | MALLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVMAEKLEFNGQDLQRISEKERRNLVGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKSTRRQRAIDLLNQVGIPDPASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGDAHAIFHAPRHPYTQALLRALPEFAQDKERLASLPGVVPGKYDRPNGCLLNPRCPYATDRCRAEEPALNMLADGRQSKCHYPLD... | 7.4.2.9 | null | dipeptide transport [GO:0042938]; heme transmembrane transport [GO:0035351]; protein transport [GO:0015031] | ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing [GO:0055052]; membrane [GO:0016020]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; heme transmembrane transporter activity [GO:0015232] | PF00005;PF08352; | 3.40.50.300; | ABC transporter superfamily | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=a dipeptide(out) + ATP + H2O = a dipeptide(in) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:23120, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:90799, ChEBI:CHEBI:456216; EC=7.4.2.9; Evidence={ECO:0000305|PubMed:7536291}; | null | null | null | null | FUNCTION: Part of the ABC transporter DppABCDF involved in dipeptide transport (PubMed:7536291). Responsible for energy coupling to the transport system (Probable). {ECO:0000269|PubMed:7536291, ECO:0000305}.; FUNCTION: When a foreign outer membrane heme receptor is expressed in E.coli, DppABCDF can also transport heme ... | Escherichia coli (strain K12) |
P0AAH0 | PSTB_ECOLI | MSMVETAPSKIQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFELYPEQRAEGEILLDGDNILTNSQDIALLRAKVGMVFQKPTPFPMSIYDNIAFGVRLFEKLSRADMDERVQWALTKAALWNETKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTKPAKKQTEDYITGRYG | 7.3.2.1 | null | phosphate ion transmembrane transport [GO:0035435]; phosphate ion transport [GO:0006817] | ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing [GO:0055052]; membrane [GO:0016020]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled phosphate ion transmembrane transporter activity [GO:0015415]; inorganic phosphate transmembrane transporter activity [GO:0005315] | PF00005; | 3.40.50.300; | ABC transporter superfamily, Phosphate importer (TC 3.A.1.7) family | null | SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. | CATALYTIC ACTIVITY: Reaction=ATP + H2O + phosphate(out) = ADP + H(+) + 2 phosphate(in); Xref=Rhea:RHEA:24440, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.3.2.1; Evidence={ECO:0000255|HAMAP-Rule:MF_01702}; | null | null | null | null | FUNCTION: Part of the ABC transporter complex PstSACB involved in phosphate import. Responsible for energy coupling to the transport system. | Escherichia coli (strain K12) |
P0AAH4 | SAPD_ECOLI | MPLLDIRNLTIEFKTGDEWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVNKDNWRVTADRMRFDDIDLLRLSARERRKLVGHNVSMIFQEPQSCLDPSERVGRQLMQNIPAWTYKGRWWQRFGWRKRRAIELLHRVGIKDHKDAMRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNSMEPTTQAQIFRLLTRLNQNSNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTMPHHPYTQALIRAIPDFGSAMPHKSRLNTLPGAIPLLEQLPIGCRLGPRCPYAQRECIVTPRLTGAKNHLYA... | null | null | peptide transport [GO:0015833]; potassium ion transmembrane transport [GO:0071805]; putrescine transport [GO:0015847] | ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing [GO:0055052]; membrane [GO:0016020] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; putrescine transmembrane transporter activity [GO:0015489] | PF00005;PF08352; | 3.40.50.300; | ABC transporter superfamily | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: Part of a putrescine export transport system, does not play a role in resistance to antimicrobial peptides (PubMed:27803167). Stimulates K(+)-uptake proteins TrkG and TrkH to import K(+), may act via ATP-binding rather than ATP hydrolysis (PubMed:11700350). {ECO:0000269|PubMed:11700350, ECO:0000269|PubMed:278... | Escherichia coli (strain K12) |
P0AAI3 | FTSH_ECOLI | MAKNLILWLVIAVVLMSVFQSFGPSESNGRKVDYSTFLQEVNNDQVREARINGREINVTKKDSNRYTTYIPVQDPKLLDNLLTKNVKVVGEPPEEPSLLASIFISWFPMLLLIGVWIFFMRQMQGGGGKGAMSFGKSKARMLTEDQIKTTFADVAGCDEAKEEVAELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRPGRFDRQVVVG... | 3.4.24.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 1 zinc ion per subunit.; | protein catabolic process [GO:0030163]; proteolysis [GO:0006508] | membrane protein complex [GO:0098796]; plasma membrane [GO:0005886]; plasma membrane protein complex [GO:0098797] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent peptidase activity [GO:0004176]; metalloendopeptidase activity [GO:0004222]; zinc ion binding [GO:0008270] | PF00004;PF17862;PF06480;PF01434; | 1.10.8.60;3.30.720.210;3.40.50.300;1.20.58.760; | AAA ATPase family; Peptidase M41 family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_01458, ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:8444797, ECO:0000269|PubMed:8947034}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01458, ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:8444797, ECO:0000269|PubMed:8947034}. | null | null | null | null | null | FUNCTION: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins. Degrades a few membrane proteins that have not been assembled into complexes such as SecY, F(0) ATPase subunit a and YccA, and also cytoplasm... | Escherichia coli (strain K12) |
P0AAI5 | FABF_ECOLI | MSKRRVVVTGLGMLSPVGNTVESTWKALLAGQSGISLIDHFDTSAYATKFAGLVKDFNCEDIISRKEQRKMDAFIQYGIVAGVQAMQDSGLEITEENATRIGAAIGSGIGGLGLIEENHTSLMNGGPRKISPFFVPSTIVNMVAGHLTIMYGLRGPSISIATACTSGVHNIGHAARIIAYGDADVMVAGGAEKASTPLGVGGFGAARALSTRNDNPQAASRPWDKERDGFVLGDGAGMLVLEEYEHAKKRGAKIYAELVGFGMSSDAYHMTSPPENGAGAALAMANALRDAGIEASQIGYVNAHGTSTPAGDKAEAQAVK... | 2.3.1.179 | null | fatty acid biosynthetic process [GO:0006633]; fatty acid elongation, saturated fatty acid [GO:0019367]; monounsaturated fatty acid biosynthetic process [GO:1903966]; response to cold [GO:0009409] | cytosol [GO:0005829] | 3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; protein homodimerization activity [GO:0042803] | PF00109;PF02801; | 3.40.47.10; | Thiolase-like superfamily, Beta-ketoacyl-ACP synthases family | null | null | CATALYTIC ACTIVITY: Reaction=a fatty acyl-[ACP] + H(+) + malonyl-[ACP] = a 3-oxoacyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:22836, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:14125, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78776, ChEBI:C... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=8.2 uM for malonyl-[ACP] (in the presence of dodecanoyl-[ACP]) {ECO:0000269|PubMed:22017312}; KM=510 uM for malonyl-CoA (in the presence of dodecanoyl-CoA) {ECO:0000269|PubMed:22017312}; KM=53.7 uM for dodecanoyl-CoA (in the presence of malonyl-CoA) {ECO:0000269|Pu... | PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000269|PubMed:6988423}. | null | null | FUNCTION: Involved in the type II fatty acid elongation cycle (PubMed:6988423, PubMed:9013860). Catalyzes the elongation of a wide range of acyl-ACP by the addition of two carbons from malonyl-ACP to an acyl acceptor (PubMed:22017312, PubMed:9013860). Can efficiently catalyze the conversion of palmitoleoyl-ACP (cis-hex... | Escherichia coli (strain K12) |
P0AAJ3 | FDNH_ECOLI | MAMETQDIIKRSATNSITPPSQVRDYKAEVAKLIDVSTCIGCKACQVACSEWNDIRDEVGHCVGVYDNPADLSAKSWTVMRFSETEQNGKLEWLIRKDGCMHCEDPGCLKACPSAGAIIQYANGIVDFQSENCIGCGYCIAGCPFNIPRLNKEDNRVYKCTLCVDRVSVGQEPACVKTCPTGAIHFGTKKEMLELAEQRVAKLKARGYEHAGVYNPEGVGGTHVMYVLHHADQPELYHGLPKDPKIDTSVSLWKGALKPLAAAGFIATFAGLIFHYIGIGPNKEVDDDEEDHHE | null | COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000269|PubMed:11884747}; Note=Binds 4 [4Fe-4S] clusters per subunit. {ECO:0000269|PubMed:11884747}; | anaerobic electron transport chain [GO:0019645]; anaerobic respiration [GO:0009061]; formate oxidation [GO:0015944]; heme oxidation [GO:0006788] | formate dehydrogenase complex [GO:0009326]; membrane [GO:0016020]; plasma membrane [GO:0005886] | 4 iron, 4 sulfur cluster binding [GO:0051539]; electron transfer activity [GO:0009055]; formate dehydrogenase (quinone) activity [GO:0036397]; metal ion binding [GO:0046872] | PF13247;PF12800;PF09163; | 3.30.70.20;1.20.5.480; | null | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:11884747}; Single-pass membrane protein {ECO:0000269|PubMed:11884747}. | null | null | null | null | null | FUNCTION: Formate dehydrogenase allows E.coli to use formate as major electron donor during anaerobic respiration, when nitrate is used as electron acceptor. The beta subunit FdnH is an electron transfer unit containing 4 iron-sulfur clusters; it serves as a conduit for electrons that are transferred from the formate o... | Escherichia coli (strain K12) |
P0AAM1 | CYBH_ECOLI | MQQKSDNVVSHYVFEAPVRIWHWLTVLCMAVLMVTGYFIGKPLPSVSGEATYLFYMGYIRLIHFSAGMVFTVVLLMRIYWAFVGNRYSRELFIVPVWRKSWWQGVWYEIRWYLFLAKRPSADIGHNPIAQAAMFGYFLMSVFMIITGFALYSEHSQYAIFAPFRYVVEFFYWTGGNSMDIHSWHRLGMWLIGAFVIGHVYMALREDIMSDDTVISTMVNGYRSHKFGKISNKERS | null | null | 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]; periplasmic side of plasma membrane [GO:0098567]; plasma membrane [GO:0005886] | electron transfer activity [GO:0009055]; heme binding [GO:0020037]; hydrogenase (acceptor) activity [GO:0033748]; iron ion binding [GO:0005506] | PF01292; | 1.20.950.20; | HupC/HyaC/HydC family | null | SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. | null | null | null | null | null | FUNCTION: Probable b-type cytochrome. | Escherichia coli (strain K12) |
P0AAM3 | HYPC_ECOLI | MCIGVPGQIRTIDGNQAKVDVCGIQRDVDLTLVGSCDENGQPRVGQWVLVHVGFAMSVINEAEARDTLDALQNMFDVEPDVGALLYGEEK | null | null | protein maturation [GO:0051604]; protein-containing complex assembly [GO:0065003] | null | carbon dioxide binding [GO:1902670]; identical protein binding [GO:0042802]; iron ion binding [GO:0005506] | PF01455; | 2.30.30.140;6.10.250.910; | HupF/HypC family | null | null | null | null | PATHWAY: Protein modification; [NiFe] hydrogenase maturation. {ECO:0000305}. | null | null | FUNCTION: Involved in the maturation of [NiFe] hydrogenases. Involved in the biosynthesis of the Fe(CN)(2)CO cofactor (PubMed:15504408, PubMed:23022438). HypC delivers iron-bound CO(2) to HypD where reduction to CO probably occurs (PubMed:23851071). In complex with HypD, accepts the cyanide ligand generated by HypF and... | Escherichia coli (strain K12) |
P0AAM7 | HYBG_ECOLI | MCIGVPGQVLAVGEDIHQLAQVEVCGIKRDVNIALICEGNPADLLGQWVLVHVGFAMSIIDEDEAKATLDALRQMDYDITSA | null | null | protein maturation [GO:0051604]; protein-containing complex assembly [GO:0065003] | null | carbon dioxide binding [GO:1902670]; identical protein binding [GO:0042802]; iron ion binding [GO:0005506] | PF01455; | 2.30.30.140; | HupF/HypC family | null | null | null | null | PATHWAY: Protein modification; [NiFe] hydrogenase maturation. {ECO:0000305}. | null | null | FUNCTION: Involved in the maturation of [NiFe] hydrogenases. Involved in the biosynthesis of the Fe(CN)(2)CO cofactor (PubMed:16412426). HybG delivers iron-bound CO(2) to HypD where reduction to CO probably occurs (PubMed:23851071). In complex with HypD, accepts the cyanide ligand generated by HypF and HypE, and also c... | Escherichia coli (strain K12) |
P0AAN3 | HYPB_ECOLI | MCTTCGCGEGNLYIEGDEHNPHSAFRSAPFAPAARPKMKITGIKAPEFTPSQTEEGDLHYGHGEAGTHAPGMSQRRMLEVEIDVLDKNNRLAERNRARFAARKQLVLNLVSSPGSGKTTLLTETLMRLKDSVPCAVIEGDQQTVNDAARIRATGTPAIQVNTGKGCHLDAQMIADAAPRLPLDDNGILFIENVGNLVCPASFDLGEKHKVAVLSVTEGEDKPLKYPHMFAAASLMLLNKVDLLPYLNFDVEKCIACAREVNPEIEIILISATSGEGMDQWLNWLETQRCA | null | null | protein maturation [GO:0051604]; protein maturation by nickel ion transfer [GO:0110147]; protein-containing complex assembly [GO:0065003] | GTPase complex [GO:1905360] | GTP binding [GO:0005525]; GTPase activity [GO:0003924]; guanosine tetraphosphate binding [GO:0097216]; metallochaperone activity [GO:0016530]; nickel cation binding [GO:0016151]; protein homodimerization activity [GO:0042803]; zinc ion binding [GO:0008270] | PF02492; | 3.40.50.300; | SIMIBI class G3E GTPase family, HypB/HupM subfamily | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Note=kcat is 0.18 min(-1) for GTPase activity. kcat is 0.04 min(1) for GTPase activity in the presence of 1 uM Zn(II). kcat is 0.10 min(-1) for GTPase activity in the presence of 10 uM Ni(II). {ECO:0000269|PubMed:21544686}; | null | null | null | FUNCTION: Involved in the maturation of [NiFe] hydrogenases. Required for nickel insertion into the metal center of the hydrogenase (PubMed:7601092, PubMed:8756471). Exhibits a low intrinsic GTPase activity, which is essential for nickel insertion (PubMed:21544686, PubMed:27951644, PubMed:7601092). In the presence of G... | Escherichia coli (strain K12) |
P0AAR3 | YBAK_ECOLI | MTPAVKLLEKNKISFQIHTYEHDPAETNFGDEVVKKLGLNPDQVYKTLLVAVNGDMKHLAVAVTPVAGQLDLKKVAKALGAKKVEMADPMVAQRSTGYLVGGISPLGQKKRLPTIIDAPAQEFATIYVSGGKRGLDIELAAGDLAKILDAKFADIARRD | 4.2.-.- | null | aminoacyl-tRNA metabolism involved in translational fidelity [GO:0106074]; response to X-ray [GO:0010165]; translation [GO:0006412] | cytosol [GO:0005829] | aminoacyl-tRNA editing activity [GO:0002161]; Cys-tRNA(Pro) hydrolase activity [GO:0043907]; lyase activity [GO:0016829] | PF04073; | 3.90.960.10; | Prolyl-tRNA editing family, YbaK/EbsC subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | null | null | null | null | null | FUNCTION: Functions in trans to edit the amino acid from incorrectly charged Cys-tRNA(Pro) via a Cys-tRNA(Pro) deacylase activity. May compensate for the lack of Cys-tRNA(Pro) editing by ProRS. Is also able to deacylate Cys-tRNA(Cys), and displays weak deacylase activity in vitro against Gly-tRNA(Gly), as well as, at h... | Escherichia coli (strain K12) |
P0AAW9 | ACRZ_ECOLI | MLELLKSLVFAVIMVPVVMAIILGLIYGLGEVFNIFSGVGKKDQPGQNH | null | null | cellular response to cell envelope stress [GO:0036460]; response to antibiotic [GO:0046677]; xenobiotic detoxification by transmembrane export across the plasma membrane [GO:1990961] | cell outer membrane [GO:0009279]; plasma membrane [GO:0005886] | xenobiotic transmembrane transporter activity [GO:0042910] | PF10766; | 6.10.250.2480; | AcrZ family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_01484, ECO:0000269|PubMed:19121005, ECO:0000269|PubMed:21778229}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01484, ECO:0000269|PubMed:19121005, ECO:0000269|PubMed:21778229}. Note=In sucrose cushions fractionates with both the inner and o... | null | null | null | null | null | FUNCTION: AcrA-AcrB-AcrZ-TolC is a drug efflux protein complex with a broad substrate specificity. This protein binds to AcrB and is required for efflux of some but not all substrates, suggesting it may influence the specificity of drug export. {ECO:0000255|HAMAP-Rule:MF_01484, ECO:0000269|PubMed:23010927}. | Escherichia coli (strain K12) |
P0AAX8 | YBIS_ECOLI | MNMKLKTLFAAAFAVVGFCSTASAVTYPLPTDGSRLVGQNQVITIPEGNTQPLEYFAAEYQMGLSNMMEANPGVDTFLPKGGTVLNIPQQLILPDTVHEGIVINSAEMRLYYYPKGTNTVIVLPIGIGQLGKDTPINWTTKVERKKAGPTWTPTAKMHAEYRAAGEPLPAVVPAGPDNPMGLYALYIGRLYAIHGTNANFGIGLRVSHGCVRLRNEDIKFLFEKVPVGTRVQFIDEPVKATTEPDGSRYIEVHNPLSTTEAQFEGQEIVPITLTKSVQTVTGQPDVDQVVLDEAIKNRSGMPVRLN | 2.-.-.- | null | cell wall organization [GO:0071555]; peptidoglycan-protein cross-linking [GO:0018104]; regulation of cell shape [GO:0008360] | extracellular region [GO:0005576]; outer membrane-bounded periplasmic space [GO:0030288] | glycosyltransferase activity [GO:0016757]; peptidoglycan L,D-transpeptidase activity [GO:0071972] | PF17969;PF03734; | 2.40.440.10; | YkuD family | PTM: In vivo a sulfenic acid can be formed on Cys-210, which probably inactivates the protein. This disulfide is subsequently reduced by DsbG and DsbC. | SUBCELLULAR LOCATION: Periplasm. | null | null | PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. | null | null | FUNCTION: Responsible, at least in part, for anchoring of the major outer membrane lipoprotein (Lpp, also known as the Braun lipoprotein) to the peptidoglycan via a meso-diaminopimelyl-L-Lys- bond on the terminal residue of Lpp. Can be oxidized in vivo, its reduction depends preferentially on DsbG, although DsbC is abl... | Escherichia coli (strain K12) |
P0AAZ4 | RARA_ECOLI | MSNLSLDFSDNTFQPLAARMRPENLAQYIGQQHLLAAGKPLPRAIEAGHLHSMILWGPPGTGKTTLAEVIARYANADVERISAVTSGVKEIREAIERARQNRNAGRRTILFVDEVHRFNKSQQDAFLPHIEDGTITFIGATTENPSFELNSALLSRARVYLLKSLSTEDIEQVLTQAMEDKTRGYGGQDIVLPDETRRAIAELVNGDARRALNTLEMMADMAEVDDSGKRVLKPELLTEIAGERSARFDNKGDRFYDLISALHKSVRGSAPDAALYWYARIITAGGDPLYVARRCLAIASEDVGNADPRAMQVAIAAWDC... | null | null | DNA recombination [GO:0006310]; DNA synthesis involved in DNA repair [GO:0000731]; DNA-templated DNA replication [GO:0006261]; protein homotetramerization [GO:0051289] | replisome [GO:0030894] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent activity, acting on DNA [GO:0008094]; DNA binding [GO:0003677]; enzyme activator activity [GO:0008047]; identical protein binding [GO:0042802]; single-stranded DNA helicase activity [GO:0017116] | PF00004;PF16193;PF12002; | 1.10.8.60;1.20.272.10;1.10.3710.10;3.40.50.300; | AAA ATPase family, RarA/MGS1/WRNIP1 subfamily | null | null | null | null | null | null | null | FUNCTION: DNA-dependent ATPase that plays important roles in cellular responses to stalled DNA replication processes. {ECO:0000269|PubMed:11459952, ECO:0000269|PubMed:15743409, ECO:0000269|PubMed:21297161}. | Escherichia coli (strain K12) |
P0AB38 | LPOB_ECOLI | MTKMSRYALITALAMFLAGCVGQREPAPVEEVKPAPEQPAEPQQPVPTVPSVPTIPQQPGPIEHEDQTAPPAPHIRHYDWNGAMQPMVSKMLGADGVTAGSVLLVDSVNNRTNGSLNAAEATETLRNALANNGKFTLVSAQQLSMAKQQLGLSPQDSLGTRSKAIGIARNVGAHYVLYSSASGNVNAPTLQMQLMLVQTGEIIWSGKGAVSQQ | null | null | peptidoglycan biosynthetic process [GO:0009252]; regulation of cell shape [GO:0008360] | cell outer membrane [GO:0009279]; periplasmic side of cell outer membrane [GO:0031241] | enzyme activator activity [GO:0008047]; enzyme binding [GO:0019899]; enzyme regulator activity [GO:0030234] | PF13036; | 3.40.50.10610; | LpoB family | null | SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000269|PubMed:21183073, ECO:0000269|PubMed:21183074}; Lipid-anchor {ECO:0000269|PubMed:21183073, ECO:0000269|PubMed:21183074}; Periplasmic side {ECO:0000269|PubMed:21183073, ECO:0000269|PubMed:21183074}. Note=Localizes to the divisome and to the lateral wall. | null | null | null | null | null | FUNCTION: Regulator of peptidoglycan synthesis that is essential for the function of penicillin-binding protein 1B (PBP1b). Stimulates transpeptidase and transglycosylase activities of PBP1b in vitro. May also contribute to outer membrane constriction during cell division, in complex with PBP1b. {ECO:0000269|PubMed:211... | Escherichia coli (strain K12) |
P0AB58 | LAPB_ECOLI | MLELLFLLLPVAAAYGWYMGRRSAQQNKQDEANRLSRDYVAGVNFLLSNQQDKAVDLFLDMLKEDTGTVEAHLTLGNLFRSRGEVDRAIRIHQTLMESASLTYEQRLLAIQQLGRDYMAAGLYDRAEDMFNQLTDETDFRIGALQQLLQIYQATSEWQKAIDVAERLVKLGKDKQRVEIAHFYCELALQHMASDDLDRAMTLLKKGAAADKNSARVSIMMGRVFMAKGEYAKAVESLQRVISQDRELVSETLEMLQTCYQQLGKTAEWAEFLQRAVEENTGADAELMLADIIEARDGSEAAQVYITRQLQRHPTMRVFHK... | null | null | lipopolysaccharide metabolic process [GO:0008653]; regulation of lipid biosynthetic process [GO:0046890] | cytoplasmic side of plasma membrane [GO:0009898]; cytosol [GO:0005829]; plasma membrane [GO:0005886] | iron ion binding [GO:0005506]; metal ion binding [GO:0046872] | PF18073;PF14559;PF13176; | 1.25.40.10; | LapB family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_00994, ECO:0000269|PubMed:24187084, ECO:0000269|PubMed:24722986}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00994, ECO:0000269|PubMed:24187084}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_00994, ECO:0000269|PubMed:24187084}. | null | null | null | null | null | FUNCTION: Modulates cellular lipopolysaccharide (LPS) levels by regulating LpxC, which is involved in lipid A biosynthesis. May act by modulating the proteolytic activity of FtsH towards LpxC. May also coordinate assembly of proteins involved in LPS synthesis at the plasma membrane. {ECO:0000255|HAMAP-Rule:MF_00994, EC... | Escherichia coli (strain K12) |
P0AB71 | ALF_ECOLI | MSKIFDFVKPGVITGDDVQKVFQVAKENNFALPAVNCVGTDSINAVLETAAKVKAPVIVQFSNGGASFIAGKGVKSDVPQGAAILGAISGAHHVHQMAEHYGVPVILHTDHCAKKLLPWIDGLLDAGEKHFAATGKPLFSSHMIDLSEESLQENIEICSKYLERMSKIGMTLEIELGCTGGEEDGVDNSHMDASALYTQPEDVDYAYTELSKISPRFTIAASFGNVHGVYKPGNVVLTPTILRDSQEYVSKKHNLPHNSLNFVFHGGSGSTAQEIKDSVSYGVVKMNIDTDTQWATWEGVLNYYKANEAYLQGQLGNPKG... | 4.1.2.13 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:10080900, ECO:0000269|PubMed:8836102, ECO:0000269|PubMed:8939754}; Note=Binds 2 Zn(2+) ions per subunit. One is catalytic and the other provides a structural contribution. {ECO:0000269|PubMed:10080900, ECO:0000269|PubMed:8836102, ECO:0000269|Pu... | gluconeogenesis [GO:0006094]; glycolytic process [GO:0006096] | cytosol [GO:0005829] | fructose-bisphosphate aldolase activity [GO:0004332]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]; zinc ion binding [GO:0008270] | PF01116; | 3.20.20.70; | Class II fructose-bisphosphate aldolase family | null | null | CATALYTIC ACTIVITY: Reaction=beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate; Xref=Rhea:RHEA:14729, ChEBI:CHEBI:32966, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=4.1.2.13; Evidence={ECO:0000269|PubMed:10712619}; CATALYTIC ACTIVITY: Reaction=D-erythrose 4-phosphate + dihydroxya... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.17 mM for fructose-1,6-bisphosphate {ECO:0000269|PubMed:10712619}; KM=0.35 mM for tagatose-1,6-bisphosphate {ECO:0000269|PubMed:10712619}; Note=The catalytic efficiency measured with fructose-1,6-bisphosphate as substrate is 1440-fold higher than that with tagato... | PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4. | null | null | FUNCTION: Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis (PubMed:10712619). In addition, is involved in the utilization of D-sedoheptulose... | Escherichia coli (strain K12) |
P0AB74 | KBAY_ECOLI | MSIISTKYLLQDAQANGYAVPAFNIHNAETIQAILEVCSEMRSPVILAGTPGTFKHIALEEIYALCSAYSTTYNMPLALHLDHHESLDDIRRKVHAGVRSAMIDGSHFPFAENVKLVKSVVDFCHSQDCSVEAELGRLGGVEDDMSVDAESAFLTDPQEAKRFVELTGVDSLAVAIGTAHGLYSKTPKIDFQRLAEIREVVDVPLVLHGASDVPDEFVRRTIELGVTKVNVATELKIAFAGAVKAWFAENPQGNDPRYYMRVGMDAMKEVVRNKINVCGSANRISA | 4.1.2.40 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 1 zinc ion per subunit.; | carbohydrate metabolic process [GO:0005975]; D-tagatose 6-phosphate catabolic process [GO:2001059]; protein homotetramerization [GO:0051289] | catalytic complex [GO:1902494]; cytosol [GO:0005829]; protein-containing complex [GO:0032991] | identical protein binding [GO:0042802]; tagatose-bisphosphate aldolase activity [GO:0009025]; zinc ion binding [GO:0008270] | PF01116; | 3.20.20.70; | Class II fructose-bisphosphate aldolase family, TagBP aldolase KbaY subfamily | null | null | CATALYTIC ACTIVITY: Reaction=D-tagatofuranose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate; Xref=Rhea:RHEA:22948, ChEBI:CHEBI:57642, ChEBI:CHEBI:58694, ChEBI:CHEBI:59776; EC=4.1.2.40; Evidence={ECO:0000269|PubMed:10712619}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.26 mM for tagatose-1,6-bisphosphate {ECO:0000269|PubMed:10712619}; KM=1.3 mM for fructose-1,6-bisphosphate {ECO:0000269|PubMed:10712619}; Note=The catalytic efficiency measured with tagatose-1,6-bisphosphate as substrate is 340-fold higher than that with fructose... | PATHWAY: Carbohydrate metabolism; D-tagatose 6-phosphate degradation; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-tagatose 6-phosphate: step 2/2. | null | null | FUNCTION: Catalytic subunit of the tagatose-1,6-bisphosphate aldolase KbaYZ, which catalyzes the reversible aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to produce tagatose 1,6-bisphosphate (TBP). Requires KbaZ subunit for full activity and stabili... | Escherichia coli (strain K12) |
P0AB77 | KBL_ECOLI | MRGEFYQQLTNDLETARAEGLFKEERIITSAQQADITVADGSHVINFCANNYLGLANHPDLIAAAKAGMDSHGFGMASVRFICGTQDSHKELEQKLAAFLGMEDAILYSSCFDANGGLFETLLGAEDAIISDALNHASIIDGVRLCKAKRYRYANNDMQELEARLKEAREAGARHVLIATDGVFSMDGVIANLKGVCDLADKYDALVMVDDSHAVGFVGENGRGSHEYCDVMGRVDIITGTLGKALGGASGGYTAARKEVVEWLRQRSRPYLFSNSLAPAIVAASIKVLEMVEAGSELRDRLWANARQFREQMSAAGFTL... | 2.3.1.29 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000255|HAMAP-Rule:MF_00985, ECO:0000269|PubMed:2104756}; Note=Binds 1 pyridoxal phosphate per subunit. {ECO:0000255|HAMAP-Rule:MF_00985, ECO:0000269|PubMed:2104756}; | biosynthetic process [GO:0009058]; L-threonine catabolic process to glycine [GO:0019518] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | glycine C-acetyltransferase activity [GO:0008890]; ligase activity [GO:0016874]; metal ion binding [GO:0046872]; pyridoxal phosphate binding [GO:0030170] | PF00155; | 3.90.1150.10;3.40.640.10; | Class-II pyridoxal-phosphate-dependent aminotransferase family | null | null | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + glycine = (2S)-2-amino-3-oxobutanoate + CoA; Xref=Rhea:RHEA:20736, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57305, ChEBI:CHEBI:78948; EC=2.3.1.29; Evidence={ECO:0000255|HAMAP-Rule:MF_00985, ECO:0000269|PubMed:2104756}; | null | PATHWAY: Amino-acid degradation; L-threonine degradation via oxydo-reductase pathway; glycine from L-threonine: step 2/2. {ECO:0000255|HAMAP-Rule:MF_00985}. | null | null | FUNCTION: Catalyzes the cleavage of 2-amino-3-ketobutyrate to glycine and acetyl-CoA. {ECO:0000255|HAMAP-Rule:MF_00985, ECO:0000269|PubMed:2104756}. | Escherichia coli (strain K12) |
P0AB80 | ILVE_ECOLI | MTTKKADYIWFNGEMVRWEDAKVHVMSHALHYGTSVFEGIRCYDSHKGPVVFRHREHMQRLHDSAKIYRFPVSQSIDELMEACRDVIRKNNLTSAYIRPLIFVGDVGMGVNPPAGYSTDVIIAAFPWGAYLGAEALEQGIDAMVSSWNRAAPNTIPTAAKAGGNYLSSLLVGSEARRHGYQEGIALDVNGYISEGAGENLFEVKDGVLFTPPFTSSALPGITRDAIIKLAKELGIEVREQVLSRESLYLADEVFMSGTAAEITPVRSVDGIQVGEGRCGPVTKRIQQAFFGLFTGETEDKWGWLDQVNQ | 2.6.1.42 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; | aspartate biosynthetic process [GO:0006532]; isoleucine biosynthetic process [GO:0009097]; leucine biosynthetic process [GO:0009098]; valine biosynthetic process [GO:0009099] | cytosol [GO:0005829] | branched-chain-amino-acid transaminase activity [GO:0004084]; identical protein binding [GO:0042802]; L-isoleucine transaminase activity [GO:0052656]; L-leucine transaminase activity [GO:0052654]; L-leucine:2-oxoglutarate aminotransferase activity [GO:0050048]; L-valine transaminase activity [GO:0052655] | PF01063; | 3.30.470.10;3.20.10.10; | Class-IV pyridoxal-phosphate-dependent aminotransferase family | null | null | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:18321, ChEBI:CHEBI:16810, ChEBI:CHEBI:17865, ChEBI:CHEBI:29985, ChEBI:CHEBI:57427; EC=2.6.1.42; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate + L-glutamate; Xref=R... | null | PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 4/4.; PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 4/4.; PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 4/4. | null | null | FUNCTION: Acts on leucine, isoleucine and valine. | Escherichia coli (strain K12) |
P0AB83 | END3_ECOLI | MNKAKRLEILTRLRENNPHPTTELNFSSPFELLIAVLLSAQATDVSVNKATAKLYPVANTPAAMLELGVEGVKTYIKTIGLYNSKAENIIKTCRILLEQHNGEVPEDRAALEALPGVGRKTANVVLNTAFGWPTIAVDTHIFRVCNRTQFAPGKNVEQVEEKLLKVVPAEFKVDCHHWLILHGRYTCIARKPRCGSCIIEDLCEYKEKVDI | 4.2.99.18 | COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000255|HAMAP-Rule:MF_00942, ECO:0000269|PubMed:7664751, ECO:0000269|PubMed:8092678}; Note=Binds 1 [4Fe-4S] cluster. The cluster does not appear to play a role in catalysis, but is probably involved in DNA-binding and proper positioning of the enzym... | base-excision repair, AP site formation [GO:0006285]; base-excision repair, AP site formation via deaminated base removal [GO:0097510]; cellular response to UV [GO:0034644] | null | 4 iron, 4 sulfur cluster binding [GO:0051539]; class I DNA-(apurinic or apyrimidinic site) endonuclease activity [GO:0140078]; DNA binding [GO:0003677]; DNA N-glycosylase activity [GO:0019104]; DNA-(apurinic or apyrimidinic site) endonuclease activity [GO:0003906]; metal ion binding [GO:0046872]; oxidized pyrimidine nu... | PF10576;PF00633;PF00730; | 1.10.1670.10; | Nth/MutY family | null | null | CATALYTIC ACTIVITY: Reaction=2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-phospho-2'-deoxyribonucleoside-DNA + H(+); Xref=Rhea:RHEA:66592, Rhea:RHEA-COMP:13180, Rhea:RHEA-COMP:16897, Rhea:RH... | null | null | null | null | FUNCTION: DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site ... | Escherichia coli (strain K12) |
P0AB87 | FUCA_ECOLI | MERNKLARQIIDTCLEMTRLGLNQGTAGNVSVRYQDGMLITPTGIPYEKLTESHIVFIDGNGKHEEGKLPSSEWRFHMAAYQSRPDANAVVHNHAVHCTAVSILNRSIPAIHYMIAAAGGNSIPCAPYATFGTRELSEHVALALKNRKATLLQHHGLIACEVNLEKALWLAHEVEVLAQLYLTTLAITDPVPVLSDEEIAVVLEKFKTYGLRIEE | 4.1.2.17 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_00987, ECO:0000269|PubMed:10821675, ECO:0000269|PubMed:11054289, ECO:0000269|PubMed:13898172, ECO:0000269|PubMed:15299567, ECO:0000269|PubMed:8515438, ECO:0000269|PubMed:8676381}; Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rul... | D-arabinose catabolic process [GO:0019571]; L-fucose catabolic process [GO:0042355]; pentose catabolic process [GO:0019323] | cytosol [GO:0005829] | aldehyde-lyase activity [GO:0016832]; L-fuculose-phosphate aldolase activity [GO:0008738]; zinc ion binding [GO:0008270] | PF00596; | 3.40.225.10; | Aldolase class II family, AraD/FucA subfamily | null | null | CATALYTIC ACTIVITY: Reaction=L-fuculose 1-phosphate = (S)-lactaldehyde + dihydroxyacetone phosphate; Xref=Rhea:RHEA:12933, ChEBI:CHEBI:18041, ChEBI:CHEBI:57642, ChEBI:CHEBI:57846; EC=4.1.2.17; Evidence={ECO:0000255|HAMAP-Rule:MF_00987, ECO:0000269|PubMed:10821675, ECO:0000269|PubMed:11054289, ECO:0000269|PubMed:1389817... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.7 mM for L-fuculose 1-phosphate (Fuc1P) {ECO:0000269|PubMed:13898172}; KM=1.5 mM for L-fuculose 1-phosphate (Fuc1P) {ECO:0000269|Ref.9}; KM=2.2 mM for L-fuculose 1-phosphate (Fuc1P) {ECO:0000269|PubMed:10821675}; Note=kcat is 19.3 sec(-1) for L-fuculose 1-phospha... | PATHWAY: Carbohydrate degradation; L-fucose degradation; L-lactaldehyde and glycerone phosphate from L-fucose: step 3/3. {ECO:0000255|HAMAP-Rule:MF_00987, ECO:0000269|PubMed:13898172}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.2. {ECO:0000269|PubMed:13898172}; | null | FUNCTION: Involved in the degradation of L-fucose and D-arabinose (PubMed:13898172). Catalyzes the reversible cleavage of L-fuculose 1-phosphate (Fuc1P) to yield dihydroxyacetone phosphate (DHAP) and L-lactaldehyde (PubMed:10821675, PubMed:11054289, PubMed:13898172, Ref.8, Ref.9). Also able to catalyze the reversible c... | Escherichia coli (strain K12) |
P0AB89 | PUR8_ECOLI | MELSSLTAVSPVDGRYGDKVSALRGIFSEYGLLKFRVQVEVRWLQKLAAHAAIKEVPAFAADAIGYLDAIVASFSEEDAARIKTIERTTNHDVKAVEYFLKEKVAEIPELHAVSEFIHFACTSEDINNLSHALMLKTARDEVILPYWRQLIDGIKDLAVQYRDIPLLSRTHGQPATPSTIGKEMANVAYRMERQYRQLNQVEILGKINGAVGNYNAHIAAYPEVDWHQFSEEFVTSLGIQWNPYTTQIEPHDYIAELFDCVARFNTILIDFDRDVWGYIALNHFKQKTIAGEIGSSTMPHKVNPIDFENSEGNLGLSNAV... | 4.3.2.2 | null | 'de novo' AMP biosynthetic process [GO:0044208]; 'de novo' IMP biosynthetic process [GO:0006189]; DNA damage response [GO:0006974] | cytosol [GO:0005829] | (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido) succinate lyase (fumarate-forming) activity [GO:0070626]; guanosine tetraphosphate binding [GO:0097216]; N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity [GO:0004018] | PF08328;PF00206; | 1.10.40.30;1.20.200.10;1.10.275.10; | Lyase 1 family, Adenylosuccinate lyase subfamily | null | null | CATALYTIC ACTIVITY: Reaction=N(6)-(1,2-dicarboxyethyl)-AMP = AMP + fumarate; Xref=Rhea:RHEA:16853, ChEBI:CHEBI:29806, ChEBI:CHEBI:57567, ChEBI:CHEBI:456215; EC=4.3.2.2; Evidence={ECO:0000269|PubMed:17531264}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16854; Evidence={ECO:0000305|PubMed:17531264}; CATALYTIC A... | null | PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 2/2. {ECO:0000305|PubMed:17531264}.; PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 2/2. {ECO:0... | null | null | FUNCTION: Catalyzes two reactions in de novo purine nucleotide biosynthesis. Catalyzes the breakdown of 5-aminoimidazole- (N-succinylocarboxamide) ribotide (SAICAR or 2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamido]succinate) to 5-aminoimidazole-4-carboxamide ribotide (AICAR or 5-amino-1-(5-phospho-beta-... | Escherichia coli (strain K12) |
P0AB91 | AROG_ECOLI | MNYQNDDLRIKEIKELLPPVALLEKFPATENAANTVAHARKAIHKILKGNDDRLLVVIGPCSIHDPVAAKEYATRLLALREELKDELEIVMRVYFEKPRTTVGWKGLINDPHMDNSFQINDGLRIARKLLLDINDSGLPAAGEFLDMITPQYLADLMSWGAIGARTTESQVHRELASGLSCPVGFKNGTDGTIKVAIDAINAAGAPHCFLSVTKWGHSAIVNTSGNGDCHIILRGGKEPNYSAKHVAEVKEGLNKAGLPAQVMIDFSHANSSKQFKKQMDVCADVCQQIAGGEKAIIGVMVESHLVEGNQSLESGEPLAY... | 2.5.1.54 | null | amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | 3-deoxy-7-phosphoheptulonate synthase activity [GO:0003849]; identical protein binding [GO:0042802] | PF00793; | 3.20.20.70; | Class-I DAHP synthase family | null | null | CATALYTIC ACTIVITY: Reaction=D-erythrose 4-phosphate + H2O + phosphoenolpyruvate = 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate + phosphate; Xref=Rhea:RHEA:14717, ChEBI:CHEBI:15377, ChEBI:CHEBI:16897, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394, ChEBI:CHEBI:58702; EC=2.5.1.54; | null | PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 1/7. | null | null | FUNCTION: Stereospecific condensation of phosphoenolpyruvate (PEP) and D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP). | Escherichia coli (strain K12) |
P0AB98 | ATP6_ECOLI | MASENMTPQDYIGHHLNNLQLDLRTFSLVDPQNPPATFWTINIDSMFFSVVLGLLFLVLFRSVAKKATSGVPGKFQTAIELVIGFVNGSVKDMYHGKSKLIAPLALTIFVWVFLMNLMDLLPIDLLPYIAEHVLGLPALRVVPSADVNVTLSMALGVFILILFYSIKMKGIGGFTKELTLQPFNHWAFIPVNLILEGVSLLSKPVSLGLRLFGNMYAGELIFILIAGLLPWWSQWILNVPWAIFHILIITLQAFIFMVLTIVYLSMASEEH | null | null | proton motive force-driven plasma membrane ATP synthesis [GO:0042777] | plasma membrane [GO:0005886]; proton-transporting ATP synthase complex [GO:0045259]; proton-transporting ATP synthase complex, coupling factor F(o) [GO:0045263] | proton-transporting ATP synthase activity, rotational mechanism [GO:0046933] | PF00119; | 1.20.120.220; | ATPase A chain family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_01393, ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01393, ECO:0000269|PubMed:15919996}. | null | null | null | null | null | FUNCTION: Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. | Escherichia coli (strain K12) |
P0ABA4 | ATPD_ECOLI | MSEFITVARPYAKAAFDFAVEHQSVERWQDMLAFAAEVTKNEQMAELLSGALAPETLAESFIAVCGEQLDENGQNLIRVMAENGRLNALPDVLEQFIHLRAVSEATAEVDVISAAALSEQQLAKISAAMEKRLSRKVKLNCKIDKSVMAGVIIRAGDMVIDGSVRGRLERLADVLQS | null | null | photosynthetic electron transport in photosystem I [GO:0009773]; photosynthetic electron transport in photosystem II [GO:0009772]; proton motive force-driven ATP synthesis [GO:0015986]; proton motive force-driven plasma membrane ATP synthesis [GO:0042777] | plasma membrane [GO:0005886]; proton-transporting ATP synthase complex [GO:0045259]; proton-transporting ATP synthase complex, catalytic core F(1) [GO:0045261] | proton-transporting ATP synthase activity, rotational mechanism [GO:0046933]; proton-transporting ATPase activity, rotational mechanism [GO:0046961] | PF00213; | 1.10.520.20; | ATPase delta chain family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_01416, ECO:0000269|PubMed:16079137}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01416, ECO:0000269|PubMed:16079137}. | null | null | null | null | null | FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... | Escherichia coli (strain K12) |
P0ABA6 | ATPG_ECOLI | MAGAKEIRSKIASVQNTQKITKAMEMVAASKMRKSQDRMAASRPYAETMRKVIGHLAHGNLEYKHPYLEDRDVKRVGYLVVSTDRGLCGGLNINLFKKLLAEMKTWTDKGVQCDLAMIGSKGVSFFNSVGGNVVAQVTGMGDNPSLSELIGPVKVMLQAYDEGRLDKLYIVSNKFINTMSQVPTISQLLPLPASDDDDLKHKSWDYLYEPDPKALLDTLLRRYVESQVYQGVVENLASEQAARMVAMKAATDNGGSLIKELQLVYNKARQASITQELTEIVSGAAAV | null | null | proton motive force-driven ATP synthesis [GO:0015986]; proton motive force-driven plasma membrane ATP synthesis [GO:0042777] | membrane [GO:0016020]; plasma membrane [GO:0005886]; proton-transporting ATP synthase complex [GO:0045259]; proton-transporting ATP synthase complex, catalytic core F(1) [GO:0045261] | ATP binding [GO:0005524]; proton-transporting ATP synthase activity, rotational mechanism [GO:0046933]; proton-transporting ATPase activity, rotational mechanism [GO:0046961] | PF00231; | 3.40.1380.10;1.10.287.80; | ATPase gamma chain family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:16079137}; Peripheral membrane protein {ECO:0000269|PubMed:16079137}. | null | null | null | null | null | FUNCTION: Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex. | Escherichia coli (strain K12) |
P0ABB0 | ATPA_ECOLI | MQLNSTEISELIKQRIAQFNVVSEAHNEGTIVSVSDGVIRIHGLADCMQGEMISLPGNRYAIALNLERDSVGAVVMGPYADLAEGMKVKCTGRILEVPVGRGLLGRVVNTLGAPIDGKGPLDHDGFSAVEAIAPGVIERQSVDQPVQTGYKAVDSMIPIGRGQRELIIGDRQTGKTALAIDAIINQRDSGIKCIYVAIGQKASTISNVVRKLEEHGALANTIVVVATASESAALQYLAPYAGCAMGEYFRDRGEDALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAARVNAEYVEAFTKGEVKGK... | 7.1.2.2 | null | proton motive force-driven ATP synthesis [GO:0015986]; proton motive force-driven plasma membrane ATP synthesis [GO:0042777] | membrane [GO:0016020]; plasma membrane [GO:0005886]; proton-transporting ATP synthase complex [GO:0045259]; proton-transporting ATP synthase complex, catalytic core F(1) [GO:0045261] | ADP binding [GO:0043531]; ATP binding [GO:0005524]; proton-transporting ATP synthase activity, rotational mechanism [GO:0046933]; proton-transporting ATPase activity, rotational mechanism [GO:0046961] | PF00006;PF00306;PF02874; | 2.40.30.20;1.20.150.20;3.40.50.300; | ATPase alpha/beta chains family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_01346, ECO:0000269|PubMed:16079137}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01346, ECO:0000269|PubMed:16079137}. | CATALYTIC ACTIVITY: Reaction=ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate; Xref=Rhea:RHEA:57720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.2; Evidence={ECO:0000255|HAMAP-Rule:MF_01346}; | null | null | null | null | FUNCTION: Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. | Escherichia coli (strain K12) |
P0ABB4 | ATPB_ECOLI | MATGKIVQVIGAVVDVEFPQDAVPRVYDALEVQNGNERLVLEVQQQLGGGIVRTIAMGSSDGLRRGLDVKDLEHPIEVPVGKATLGRIMNVLGEPVDMKGEIGEEERWAIHRAAPSYEELSNSQELLETGIKVIDLMCPFAKGGKVGLFGGAGVGKTVNMMELIRNIAIEHSGYSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAVYVPADDLTDPSPATTFAHLDATV... | 7.1.2.2 | null | proton motive force-driven plasma membrane ATP synthesis [GO:0042777] | membrane [GO:0016020]; plasma membrane [GO:0005886]; proton-transporting ATP synthase complex [GO:0045259]; proton-transporting ATP synthase complex, catalytic core F(1) [GO:0045261] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; proton-transporting ATP synthase activity, rotational mechanism [GO:0046933]; proton-transporting ATPase activity, rotational mechanism [GO:0046961] | PF00006;PF02874; | 2.40.10.170;3.40.50.300; | ATPase alpha/beta chains family | null | SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. | CATALYTIC ACTIVITY: Reaction=ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate; Xref=Rhea:RHEA:57720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.2; Evidence={ECO:0000255|HAMAP-Rule:MF_01347}; | null | null | null | null | FUNCTION: Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. | Escherichia coli (strain K12) |
P0ABB8 | ATMA_ECOLI | MFKEIFTRLIRHLPSRLVHRDPLPGAQQTVNTVVPPSLSAHCLKMAVMPEEELWKTFDTHPEGLNQAEVESAREQHGENKLPAQQPSPWWVHLWVCYRNPFNILLTILGAISYATEDLFAAGVIALMVAISTLLNFIQEARSTKAADALKAMVSNTATVLRVINDKGENGWLEIPIDQLVPGDIIKLAAGDMIPADLRILQARDLFVAQASLTGESLPVEKAATTRQPEHSNPLECDTLCFMGTTVVSGTAQAMVIATGANTWFGQLAGRVSEQESEPNAFQQGISRVSMLLIRFMLVMAPVVLLINGYTKGDWWEAALF... | 7.2.2.14 | null | cellular response to magnesium ion [GO:0071286]; magnesium ion transmembrane transport [GO:1903830] | intracellular membrane-bounded organelle [GO:0043231]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled monoatomic cation transmembrane transporter activity [GO:0019829]; metal ion binding [GO:0046872]; P-type ion transporter activity [GO:0015662]; P-type magnesium transporter activity [GO:0015444] | PF00689;PF00690;PF00122;PF00702; | 3.40.1110.10;2.70.150.10;1.20.1110.10;3.40.50.1000; | Cation transport ATPase (P-type) (TC 3.A.3) family, Type IIIB subfamily | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O + Mg(2+)(out) = ADP + H(+) + Mg(2+)(in) + phosphate; Xref=Rhea:RHEA:10260, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:18420, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.14; Evidence={ECO:0000250|UniProtKB:P36640}; | null | null | null | null | FUNCTION: Mediates magnesium influx to the cytosol. {ECO:0000250|UniProtKB:P36640}. | Escherichia coli (strain K12) |
P0ABC7 | HFLK_ECOLI | MAWNQPGNNGQDRDPWGSSKPGGNSEGNGNKGGRDQGPPDLDDIFRKLSKKLGGLGGGKGTGSGGGSSSQGPRPQLGGRVVTIAAAAIVIIWAASGFYTIKEAERGVVTRFGKFSHLVEPGLNWKPTFIDEVKPVNVEAVRELAASGVMLTSDENVVRVEMNVQYRVTNPEKYLYSVTSPDDSLRQATDSALRGVIGKYTMDRILTEGRTVIRSDTQRELEETIRPYDMGITLLDVNFQAARPPEEVKAAFDDAIAARENEQQYIREAEAYTNEVQPRANGQAQRILEEARAYKAQTILEAQGEVARFAKLLPEYKAAPE... | null | null | response to heat [GO:0009408] | cytosol [GO:0005829]; membrane protein complex [GO:0098796]; plasma membrane [GO:0005886]; plasma membrane protein complex [GO:0098797] | null | PF01145;PF12221; | 3.30.479.30; | Band 7/mec-2 family, HflK subfamily | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:8947034}; Single-pass type II membrane protein {ECO:0000269|PubMed:8947034}. | null | null | null | null | null | FUNCTION: HflC and HflK help govern the stability of phage lambda cII protein, and thereby control the lysogenization frequency of phage lambda. HflKC inhibits the SecY-degrading activity of FtsH, possibly helping quality control of integral membrane proteins. {ECO:0000269|PubMed:8947034}. | Escherichia coli (strain K12) |
P0ABD3 | BFR_ECOLI | MKGDTKVINYLNKLLGNELVAINQYFLHARMFKNWGLKRLNDVEYHESIDEMKHADRYIERILFLEGLPNLQDLGKLNIGEDVEEMLRSDLALELDGAKNLREAIGYADSVHDYVSRDMMIEILRDEEGHIDWLETELDLIQKMGLQNYLQAQIREEG | 1.16.3.1 | COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000269|PubMed:19391621}; Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer. {ECO:0000269|PubMed:19391621}; COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000269|PubMed:19391621}; Note=Binds 2 iron ions per subunit. The cataly... | intracellular sequestering of iron ion [GO:0006880]; iron ion transport [GO:0006826] | cytosol [GO:0005829]; membrane [GO:0016020] | ferric iron binding [GO:0008199]; ferroxidase activity [GO:0004322]; heme binding [GO:0020037]; identical protein binding [GO:0042802]; iron ion binding [GO:0005506]; oxidoreductase activity [GO:0016491]; protein homodimerization activity [GO:0042803] | PF00210; | 1.20.1260.10; | Bacterioferritin family | null | null | CATALYTIC ACTIVITY: Reaction=4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O; Xref=Rhea:RHEA:11148, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.16.3.1; Evidence={ECO:0000269|PubMed:10769150, ECO:0000269|PubMed:14636073, ECO:0000269|PubMed:19705876}; | null | null | null | null | FUNCTION: Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex. The mineralized iron core can contain as many as 2700 iron atoms/24-meric molecule. {E... | Escherichia coli (strain K12) |
P0ABD5 | ACCA_ECOLI | MSLNFLDFEQPIAELEAKIDSLTAVSRQDEKLDINIDEEVHRLREKSVELTRKIFADLGAWQIAQLARHPQRPYTLDYVRLAFDEFDELAGDRAYADDKAIVGGIARLDGRPVMIIGHQKGRETKEKIRRNFGMPAPEGYRKALRLMQMAERFKMPIITFIDTPGAYPGVGAEERGQSEAIARNLREMSRLGVPVVCTVIGEGGSGGALAIGVGDKVNMLQYSTYSVISPEGCASILWKSADKAPLAAEAMGIIAPRLKELKLIDSIIPEPLGGAHRNPEAMAASLKAQLLADLADLDVLSTEDLKNRRYQRLMSYGYA | 2.1.3.15 | null | fatty acid biosynthetic process [GO:0006633]; long-chain fatty acid biosynthetic process [GO:0042759]; malonyl-CoA biosynthetic process [GO:2001295] | acetate CoA-transferase complex [GO:0009329]; acetyl-CoA carboxylase complex [GO:0009317]; cytoplasm [GO:0005737]; cytosol [GO:0005829] | acetyl-CoA carboxylase activity [GO:0003989]; ATP binding [GO:0005524]; carboxyl- or carbamoyltransferase activity [GO:0016743]; identical protein binding [GO:0042802] | PF03255; | null | AccA family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein]; Xref=Rhea:RHEA:54728, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145; EC=2.1.3.15; Evidence={ECO:0000255|HAMAP-Rule:MF... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=100 uM for malonyl-CoA {ECO:0000269|PubMed:15066985}; KM=10 mM for biocytin {ECO:0000269|PubMed:15066985}; | PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00823}. | null | null | FUNCTION: Component of the acetyl coenzyme A carboxylase (ACC) complex. First, biotin carboxylase catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the carboxyltransferase to acetyl-CoA to form malonyl-CoA. {ECO:0000255|HAMAP-Rule:MF_00823, ECO:0000269|PubMed... | Escherichia coli (strain K12) |
P0ABD8 | BCCP_ECOLI | MDIRKIKKLIELVEESGISELEISEGEESVRISRAAPAASFPVMQQAYAAPMMQQPAQSNAAAPATVPSMEAPAAAEISGHIVRSPMVGTFYRTPSPDAKAFIEVGQKVNVGDTLCIVEAMKMMNQIEADKSGTVKAILVESGQPVEFDEPLVVIE | null | null | fatty acid biosynthetic process [GO:0006633]; malonyl-CoA biosynthetic process [GO:2001295] | acetyl-CoA carboxylase complex [GO:0009317]; cytoplasm [GO:0005737]; cytosol [GO:0005829] | acetyl-CoA carboxylase activity [GO:0003989]; molecular adaptor activity [GO:0060090] | PF00364; | 2.40.50.100; | null | null | null | null | null | PATHWAY: Lipid metabolism; fatty acid biosynthesis. | null | null | FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000269|PubMed:4934522}. | Escherichia coli (strain K12) |
P0ABE5 | C561_ECOLI | MENKYSRLQISIHWLVFLLVIAAYCAMEFRGFFPRSDRPLINMIHVSCGISILVLMVVRLLLRLKYPTPPIIPKPKPMMTGLAHLGHLVIYLLFIALPVIGLVMMYNRGNPWFAFGLTMPYASEANFERVDSLKSWHETLANLGYFVIGLHAAAALAHHYFWKDNTLLRMMPRKRS | 1.10.3.17 | COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000269|PubMed:29915379, ECO:0000269|PubMed:3510204, ECO:0000269|PubMed:35671795}; Note=Binds 2 heme b (iron-protoporphyrin IX) groups per molecule. {ECO:0000269|PubMed:29915379, ECO:0000269|PubMed:3510204, ECO:0000269|PubMed:35671795}; | removal of superoxide radicals [GO:0019430]; respiratory electron transport chain [GO:0022904] | plasma membrane [GO:0005886] | electron transfer activity [GO:0009055]; heme binding [GO:0020037]; metal ion binding [GO:0046872]; oxidoreductase activity [GO:0016491] | PF01292; | null | Cytochrome b561 family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:29915379, ECO:0000269|PubMed:3510204, ECO:0000269|PubMed:6097799}; Multi-pass membrane protein {ECO:0000269|PubMed:29915379}. | CATALYTIC ACTIVITY: Reaction=a ubiquinol + 2 O2 = a ubiquinone + 2 H(+) + 2 superoxide; Xref=Rhea:RHEA:29171, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976, ChEBI:CHEBI:18421; EC=1.10.3.17; Evidence={ECO:0000269|PubMed:29915379, ECO:0000269|PubMed:3... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.39 uM for ubiquinone {ECO:0000269|PubMed:35671795}; KM=10.29 uM for ubiquinol {ECO:0000269|PubMed:35671795}; | null | null | null | FUNCTION: B-type di-heme cytochrome (PubMed:29915379, PubMed:3510204, PubMed:35671795). Catalyzes the oxidation of superoxide to molecular oxygen and transfers the extracted electrons to ubiquinone through the two hemes (PubMed:29915379, PubMed:35671795). Can also use menaquinone (PubMed:35671795). The enzyme may be re... | Escherichia coli (strain K12) |
P0ABF1 | PCNB_ECOLI | MFTRVANFCRKVLSREESEAEQAVARPQVTVIPREQHAISRKDISENALKVMYRLNKAGYEAWLVGGGVRDLLLGKKPKDFDVTTNATPEQVRKLFRNCRLVGRRFRLAHVMFGPEIIEVATFRGHHEGNVSDRTTSQRGQNGMLLRDNIFGSIEEDAQRRDFTINSLYYSVADFTVRDYVGGMKDLKDGVIRLIGNPETRYREDPVRMLRAVRFAAKLGMRISPETAEPIPRLATLLNDIPPARLFEESLKLLQAGYGYETYKLLCEYHLFQPLFPTITRYFTENGDSPMERIIEQVLKNTDTRIHNDMRVNPAFLFAA... | 2.7.7.19 | null | mRNA polyadenylation [GO:0006378]; mRNA processing [GO:0006397]; plasmid maintenance [GO:0006276]; polyadenylation-dependent RNA catabolic process [GO:0043633]; RNA modification [GO:0009451] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; poly(A) RNA polymerase activity [GO:1990817]; RNA binding [GO:0003723] | PF01743;PF12626;PF12627; | 3.30.460.10;1.10.3090.10; | TRNA nucleotidyltransferase/poly(A) polymerase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15737627}. Cell inner membrane {ECO:0000269|PubMed:15737627}. | CATALYTIC ACTIVITY: Reaction=ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide; Xref=Rhea:RHEA:11332, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17347, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:140395, ChEBI:CHEBI:173115; EC=2.7.7.19; Evidence={ECO:0000255|HAMAP-Rule:MF_00957, ECO:0000269|PubMed:1438224}; | null | null | null | null | FUNCTION: Adds poly(A) tail to the 3' end of many RNAs, which usually targets these RNAs for decay. Plays a significant role in the global control of gene expression, through influencing the rate of transcript degradation, and in the general RNA quality control. Rho-independent transcription terminators may serve as po... | Escherichia coli (strain K12) |
P0ABF6 | CDD_ECOLI | MHPRFQTAFAQLADNLQSALEPILADKYFPALLTGEQVSSLKSATGLDEDALAFALLPLAAACARTPLSNFNVGAIARGVSGTWYFGANMEFIGATMQQTVHAEQSAISHAWLSGEKALAAITVNYTPCGHCRQFMNELNSGLDLRIHLPGREAHALRDYLPDAFGPKDLEIKTLLMDEQDHGYALTGDALSQAAIAAANRSHMPYSKSPSGVALECKDGRIFSGSYAENAAFNPTLPPLQGALILLNLKGYDYPDIQRAVLAEKADAPLIQWDATSATLKALGCHSIDRVLLA | 3.5.4.5 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:8289286, ECO:0000269|PubMed:8634261, ECO:0000269|PubMed:9125497}; Note=Binds 1 zinc ion. {ECO:0000269|PubMed:8289286, ECO:0000269|PubMed:8634261, ECO:0000269|PubMed:9125497}; | cytidine deamination [GO:0009972]; deoxycytidine catabolic process [GO:0006217]; nucleobase-containing small molecule interconversion [GO:0015949] | cytosol [GO:0005829] | cytidine deaminase activity [GO:0004126]; deoxycytidine deaminase activity [GO:0047844]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]; pyrimidine nucleoside binding [GO:0001884]; zinc ion binding [GO:0008270] | PF00383;PF08211; | 3.40.140.10; | Cytidine and deoxycytidylate deaminase family | null | null | CATALYTIC ACTIVITY: Reaction=cytidine + H(+) + H2O = NH4(+) + uridine; Xref=Rhea:RHEA:16069, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16704, ChEBI:CHEBI:17562, ChEBI:CHEBI:28938; EC=3.5.4.5; Evidence={ECO:0000255|HAMAP-Rule:MF_01558}; CATALYTIC ACTIVITY: Reaction=2'-deoxycytidine + H(+) + H2O = 2'-deoxyuridine... | null | null | null | null | FUNCTION: This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis. | Escherichia coli (strain K12) |
P0ABG4 | FTSW_ECOLI | MRLSLPRLKMPRLPGFSILVWISTALKGWVMGSREKDTDSLIMYDRTLLWLTFGLAAIGFIMVTSASMPIGQRLTNDPFFFAKRDGVYLILAFILAIITLRLPMEFWQRYSATMLLGSIILLMIVLVVGSSVKGASRWIDLGLLRIQPAELTKLSLFCYIANYLVRKGDEVRNNLRGFLKPMGVILVLAVLLLAQPDLGTVVVLFVTTLAMLFLAGAKLWQFIAIIGMGISAVVLLILAEPYRIRRVTAFWNPWEDPFGSGYQLTQSLMAFGRGELWGQGLGNSVQKLEYLPEAHTDFIFAIIGEELGYVGVVLALLMVF... | 2.4.99.28 | 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]; regulation of cell shape [GO:0008360] | cell division site [GO:0032153]; divisome complex [GO:1990586]; plasma membrane [GO:0005886] | lipid-linked peptidoglycan transporter activity [GO:0015648]; peptidoglycan glycosyltransferase activity [GO:0008955] | PF01098; | null | SEDS family, FtsW subfamily | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_00913, ECO:0000269|PubMed:11807049, ECO:0000269|PubMed:12423747, ECO:0000269|PubMed:9603865}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00913, ECO:0000269|PubMed:11807049, ECO:0000269|PubMed:12423747, ECO:0000269|PubMed:9603865}. Note=Loc... | CATALYTIC ACTIVITY: Reaction=[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n... | null | PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00913}. | null | null | FUNCTION: Peptidoglycan polymerase that is essential for cell division (Probable). Functions probably in conjunction with the penicillin-binding protein 3 (ftsI) (PubMed:11807049, PubMed:9603865). Required for localization of FtsI (PubMed:11807049). {ECO:0000269|PubMed:11807049, ECO:0000269|PubMed:9603865, ECO:0000305|... | Escherichia coli (strain K12) |
P0ABG7 | RODA_ECOLI | MTDNPNKKTFWDKVHLDPTMLLILLALLVYSALVIWSASGQDIGMMERKIGQIAMGLVIMVVMAQIPPRVYEGWAPYLYIICIILLVAVDAFGAISKGAQRWLDLGIVRFQPSEIAKIAVPLMVARFINRDVCPPSLKNTGIALVLIFMPTLLVAAQPDLGTSILVALSGLFVLFLSGLSWRLIGVAVVLVAAFIPILWFFLMHDYQRQRVMMLLDPESDPLGAGYHIIQSKIAIGSGGLRGKGWLHGTQSQLEFLPERHTDFIFAVLAEELGLVGILILLALYILLIMRGLWIAARAQTTFGRVMAGGLMLILFVYVFV... | 2.4.99.28 | null | cell division [GO:0051301]; cell wall organization [GO:0071555]; peptidoglycan biosynthetic process [GO:0009252]; regulation of cell shape [GO:0008360] | cell division site [GO:0032153]; plasma membrane [GO:0005886] | lipid-linked peptidoglycan transporter activity [GO:0015648]; peptidoglycan glycosyltransferase activity [GO:0008955] | PF01098; | null | SEDS family, MrdB/RodA subfamily | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_02079, ECO:0000269|PubMed:6348029}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_02079}. | CATALYTIC ACTIVITY: Reaction=[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n... | null | PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. {ECO:0000255|HAMAP-Rule:MF_02079, ECO:0000269|PubMed:27643381}. | null | null | FUNCTION: Peptidoglycan polymerase that is essential for cell wall elongation (PubMed:27643381). Also required for the maintenance of the rod cell shape (PubMed:2644207). Functions probably in conjunction with the penicillin-binding protein 2 (mrdA) (PubMed:2644207, PubMed:27643381). {ECO:0000269|PubMed:2644207, ECO:00... | Escherichia coli (strain K12) |
P0ABH0 | FTSA_ECOLI | MIKATDRKLVVGLEIGTAKVAALVGEVLPDGMVNIIGVGSCPSRGMDKGGVNDLESVVKCVQRAIDQAELMADCQISSVYLALSGKHISCQNEIGMVPISEEEVTQEDVENVVHTAKSVRVRDEHRVLHVIPQEYAIDYQEGIKNPVGLSGVRMQAKVHLITCHNDMAKNIVKAVERCGLKVDQLIFAGLASSYSVLTEDERELGVCVVDIGGGTMDIAVYTGGALRHTKVIPYAGNVVTSDIAYAFGTPPSDAEAIKVRHGCALGSIVGKDESVEVPSVGGRPPRSLQRQTLAEVIEPRYTELLNLVNEEILQLQEKLR... | null | null | cell division [GO:0051301]; division septum assembly [GO:0000917]; FtsZ-dependent cytokinesis [GO:0043093] | cell division site [GO:0032153]; cytoplasmic side of plasma membrane [GO:0009898]; cytosol [GO:0005829]; divisome complex [GO:1990586]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; identical protein binding [GO:0042802] | PF14450;PF02491; | 3.30.1490.110;3.30.420.40; | FtsA/MreB family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15752196, ECO:0000269|PubMed:2203741}; Peripheral membrane protein {ECO:0000269|PubMed:15752196, ECO:0000269|PubMed:2203741}; Cytoplasmic side {ECO:0000269|PubMed:15752196, ECO:0000269|PubMed:2203741}. Note=Localizes to the Z ring in an FtsZ-dependent manner... | null | null | null | null | null | FUNCTION: Essential cell division protein that assists in the assembly of the Z ring (PubMed:11847116). May serve as the principal membrane anchor for the Z ring (PubMed:15752196). Also required for the recruitment to the septal ring of the downstream cell division proteins FtsK, FtsQ, FtsL, FtsI and FtsN (PubMed:10027... | Escherichia coli (strain K12) |
P0ABH7 | CISY_ECOLI | MADTKAKLTLNGDTAVELDVLKGTLGQDVIDIRTLGSKGVFTFDPGFTSTASCESKITFIDGDEGILLHRGFPIDQLATDSNYLEVCYILLNGEKPTQEQYDEFKTTVTRHTMIHEQITRLFHAFRRDSHPMAVMCGITGALAAFYHDSLDVNNPRHREIAAFRLLSKMPTMAAMCYKYSIGQPFVYPRNDLSYAGNFLNMMFSTPCEPYEVNPILERAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEEISSVKHIPEFVRRAKDKNDSFRLMGFGHRVYKNYDPRATVMR... | 2.3.3.16 | null | protein hexamerization [GO:0034214]; tricarboxylic acid cycle [GO:0006099] | cytosol [GO:0005829] | citrate (Si)-synthase activity [GO:0004108]; identical protein binding [GO:0042802]; NADH binding [GO:0070404] | PF00285; | 2.20.28.60;1.10.580.10;1.10.230.10; | Citrate synthase family | null | null | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + H2O + oxaloacetate = citrate + CoA + H(+); Xref=Rhea:RHEA:16845, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16452, ChEBI:CHEBI:16947, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.3.16; Evidence={ECO:0000255|PROSITE-ProRule:PRU10117}; | null | PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 1/2. | null | null | null | Escherichia coli (strain K12) |
P0ABH9 | CLPA_ECOLI | MLNQELELSLNMAFARAREHRHEFMTVEHLLLALLSNPSAREALEACSVDLVALRQELEAFIEQTTPVLPASEEERDTQPTLSFQRVLQRAVFHVQSSGRNEVTGANVLVAIFSEQESQAAYLLRKHEVSRLDVVNFISHGTRKDEPTQSSDPGSQPNSEEQAGGEERMENFTTNLNQLARVGGIDPLIGREKELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDVPEVMADCTIYSLDIGSLLAGTKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTIIGAGAASGGQVDAANLIKPLLSSGKIRVIG... | null | null | cellular response to heat [GO:0034605]; protein quality control for misfolded or incompletely synthesized proteins [GO:0006515]; protein unfolding [GO:0043335]; response to oxidative stress [GO:0006979] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; endopeptidase Clp complex [GO:0009368] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent peptidase activity [GO:0004176] | PF00004;PF07724;PF17871;PF02861;PF10431; | 1.10.8.60;1.10.1780.10;3.40.50.300; | ClpA/ClpB family | null | null | null | null | null | null | null | FUNCTION: ATP-dependent specificity component of the ClpAP protease. It directs the protease to specific substrates. It has unfoldase activity. The primary function of the ClpA-ClpP complex appears to be the degradation of unfolded or abnormal proteins. | Escherichia coli (strain K12) |
P0ABI4 | CORA_ECOLI | MLSAFQLENNRLTRLEVEESQPLVNAVWIDLVEPDDDERLRVQSELGQSLATRPELEDIEASARFFEDDDGLHIHSFFFFEDAEDHAGNSTVAFTIRDGRLFTLRERELPAFRLYRMRARSQSMVDGNAYELLLDLFETKIEQLADEIENIYSDLEQLSRVIMEGHQGDEYDEALSTLAELEDIGWKVRLCLMDTQRALNFLVRKARLPGGQLEQAREILRDIESLLPHNESLFQKVNFLMQAAMGFINIEQNRIIKIFSVVSVVFLPPTLVASSYGMNFEFMPELKWSFGYPGAIIFMILAGLAPYLYFKRKNWL | null | null | cobalt ion transport [GO:0006824]; magnesium ion transport [GO:0015693]; nickel cation transmembrane transport [GO:0035444] | plasma membrane [GO:0005886] | cobalt ion transmembrane transporter activity [GO:0015087]; magnesium ion transmembrane transporter activity [GO:0015095]; nickel cation transmembrane transporter activity [GO:0015099] | PF01544; | 1.20.58.340; | CorA metal ion transporter (MIT) (TC 1.A.35) family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996, ECO:0000305|PubMed:780341}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9WZ31}. | CATALYTIC ACTIVITY: Reaction=Mg(2+)(in) = Mg(2+)(out); Xref=Rhea:RHEA:29827, ChEBI:CHEBI:18420; Evidence={ECO:0000305|PubMed:780341}; CATALYTIC ACTIVITY: Reaction=Co(2+)(in) = Co(2+)(out); Xref=Rhea:RHEA:28578, ChEBI:CHEBI:48828; Evidence={ECO:0000305|PubMed:780341}; CATALYTIC ACTIVITY: Reaction=Mn(2+)(in) = Mn(2+)(out... | null | null | null | null | FUNCTION: Mediates influx of magnesium ions. Can also mediate cobalt and manganese uptake (PubMed:780341). Alternates between open and closed states. Activated by low cytoplasmic Mg(2+) levels. Inactive when cytoplasmic Mg(2+) levels are high (By similarity). {ECO:0000250|UniProtKB:Q9WZ31, ECO:0000269|PubMed:780341}. | Escherichia coli (strain K12) |
P0ABI8 | CYOB_ECOLI | MFGKLSLDAVPFHEPIVMVTIAGIILGGLALVGLITYFGKWTYLWKEWLTSVDHKRLGIMYIIVAIVMLLRGFADAIMMRSQQALASAGEAGFLPPHHYDQIFTAHGVIMIFFVAMPFVIGLMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFSRKRLFGYTSLVWAT... | 7.1.1.3 | COFACTOR: Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000269|PubMed:11017202, ECO:0000269|PubMed:33408407}; Note=Binds 1 copper B ion per subunit. {ECO:0000269|PubMed:11017202, ECO:0000269|PubMed:33408407}; COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000269|PubMed:11017202, ECO:0000269|PubMed:... | aerobic electron transport chain [GO:0019646]; aerobic respiration [GO:0009060]; electron transport coupled proton transport [GO:0015990]; respiratory electron transport chain [GO:0022904] | cytochrome o ubiquinol oxidase complex [GO:0009319]; plasma membrane [GO:0005886]; respirasome [GO:0070469] | copper ion binding [GO:0005507]; cytochrome bo3 ubiquinol oxidase activity [GO:0009486]; cytochrome-c oxidase activity [GO:0004129]; electron transfer activity [GO:0009055]; heme binding [GO:0020037]; oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor [GO:0016682]; oxidore... | PF00115; | 1.20.210.10; | Heme-copper respiratory oxidase family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:6365921}; Multi-pass membrane protein {ECO:0000269|PubMed:6365921}. | CATALYTIC ACTIVITY: Reaction=2 a ubiquinol + n H(+)(in) + O2 = 2 a ubiquinone + n H(+)(out) + 2 H2O; Xref=Rhea:RHEA:30251, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976; EC=7.1.1.3; Evidence={ECO:0000269|PubMed:11017202, ECO:00002... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=18 uM for ubiquinol-1 {ECO:0000269|PubMed:11017202}; KM=50 uM for ubiquinol-1 {ECO:0000269|PubMed:6365921}; KM=50 uM for ubiquinol-6 {ECO:0000269|PubMed:6365921}; Vmax=15.5 umol/min/nmol enzyme with ubiquinol-1 {ECO:0000269|PubMed:6365921}; Vmax=12.6 umol/min/nmol ... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.4. {ECO:0000269|PubMed:6365921}; | null | FUNCTION: Cytochrome bo(3) ubiquinol oxidase is the terminal enzyme in the aerobic respiratory chain of E.coli that predominates when cells are grown at high aeration. Catalyzes the four-electron reduction of O2 to water, using a ubiquinol as a membrane soluble electron donor for molecular oxygen reduction; ubiquinol-8... | Escherichia coli (strain K12) |
P0ABJ1 | CYOA_ECOLI | MRLRKYNKSLGWLSLFAGTVLLSGCNSALLDPKGQIGLEQRSLILTAFGLMLIVVIPAILMAVGFAWKYRASNKDAKYSPNWSHSNKVEAVVWTVPILIIIFLAVLTWKTTHALEPSKPLAHDEKPITIEVVSMDWKWFFIYPEQGIATVNEIAFPANTPVYFKVTSNSVMNSFFIPRLGSQIYAMAGMQTRLHLIANEPGTYDGISASYSGPGFSGMKFKAIATPDRAAFDQWVAKAKQSPNTMSDMAAFEKLAAPSEYNQVEYFSNVKPDLFADVINKFMAHGKSMDMTQPEGEHSAHEGMEGMDMSHAESAH | null | null | aerobic electron transport chain [GO:0019646]; aerobic respiration [GO:0009060]; ATP synthesis coupled electron transport [GO:0042773]; electron transport coupled proton transport [GO:0015990] | cytochrome o ubiquinol oxidase complex [GO:0009319]; plasma membrane [GO:0005886]; respirasome [GO:0070469] | copper ion binding [GO:0005507]; cytochrome bo3 ubiquinol oxidase activity [GO:0009486]; cytochrome-c oxidase activity [GO:0004129]; electron transfer activity [GO:0009055]; oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor [GO:0016682]; oxidoreduction-driven active trans... | PF00116;PF06481; | 1.10.287.90;2.60.40.420; | Cytochrome c oxidase subunit 2 family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:16079137, ECO:0000269|PubMed:6365921}; Multi-pass membrane protein {ECO:0000269|PubMed:16079137, ECO:0000269|PubMed:6365921}. | null | null | null | null | null | FUNCTION: Cytochrome bo(3) ubiquinol terminal oxidase is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at high aeration. Has proton pump activity across the membrane in addition to electron transfer, pumping 2 protons/electron. {ECO:0000269|PubMed:19542282, ECO:0000269|... | Escherichia coli (strain K12) |
P0ABJ3 | CYOC_ECOLI | MATDTLTHATAHAHEHGHHDAGGTKIFGFWIYLMSDCILFSILFATYAVLVNGTAGGPTGKDIFELPFVLVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTWLFGAGFIGMEIYEFHHLIVNGMGPDRSGFLSAFFALVGTHGLHVTSGLIWMAVLMVQIARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMGAM | null | null | aerobic electron transport chain [GO:0019646]; aerobic respiration [GO:0009060]; electron transport coupled proton transport [GO:0015990] | cytochrome o ubiquinol oxidase complex [GO:0009319]; plasma membrane [GO:0005886] | cytochrome bo3 ubiquinol oxidase activity [GO:0009486]; cytochrome-c oxidase activity [GO:0004129]; electron transfer activity [GO:0009055]; oxidoreduction-driven active transmembrane transporter activity [GO:0015453]; proton transmembrane transporter activity [GO:0015078] | PF00510; | 1.20.120.80; | Cytochrome c oxidase subunit 3 family | null | SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. | null | null | null | null | null | FUNCTION: Cytochrome bo(3) ubiquinol terminal oxidase is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at high aeration. Has proton pump activity across the membrane in addition to electron transfer, pumping 2 protons/electron. {ECO:0000269|PubMed:19542282, ECO:0000269|... | Escherichia coli (strain K12) |
P0ABJ6 | CYOD_ECOLI | MSHSTDHSGASHGSVKTYMTGFILSIILTVIPFWMVMTGAASPAVILGTILAMAVVQVLVHLVCFLHMNTKSDEGWNMTAFVFTVLIIAILVVGSIWIMWNLNYNMMMH | null | null | aerobic electron transport chain [GO:0019646]; aerobic respiration [GO:0009060]; electron transport coupled proton transport [GO:0015990] | cytochrome o ubiquinol oxidase complex [GO:0009319]; plasma membrane [GO:0005886] | cytochrome bo3 ubiquinol oxidase activity [GO:0009486]; electron transfer activity [GO:0009055]; oxidoreduction-driven active transmembrane transporter activity [GO:0015453]; proton transmembrane transporter activity [GO:0015078] | PF03626; | null | Cytochrome c oxidase bacterial subunit 4 family | null | SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. | null | null | null | null | null | FUNCTION: Cytochrome bo(3) ubiquinol terminal oxidase is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at high aeration. Has proton pump activity across the membrane in addition to electron transfer, pumping 2 protons/electron. {ECO:0000269|PubMed:19542282, ECO:0000269|... | Escherichia coli (strain K12) |
P0ABJ9 | CYDA_ECOLI | MLDIVELSRLQFALTAMYHFLFVPLTLGMAFLLAIMETVYVLSGKQIYKDMTKFWGKLFGINFALGVATGLTMEFQFGTNWSYYSHYVGDIFGAPLAIEGLMAFFLESTFVGLFFFGWDRLGKVQHMCVTWLVALGSNLSALWILVANGWMQNPIASDFNFETMRMEMVSFSELVLNPVAQVKFVHTVASGYVTGAMFILGISAWYMLKGRDFAFAKRSFAIAASFGMAAVLSVIVLGDESGYEMGDVQKTKLAAIEAEWETQPAPAAFTLFGIPDQEEETNKFAIQIPYALGIIATRSVDTPVIGLKELMVQHEERIRN... | 7.1.1.7 | COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000269|PubMed:2656671, ECO:0000269|PubMed:3013298, ECO:0000269|PubMed:3013299, ECO:0000269|PubMed:6307994, ECO:0000269|PubMed:7577938}; Note=Binds 1 protoheme IX center (heme b558) per subunit. {ECO:0000269|PubMed:2656671, ECO:0000269|PubMed:3013298, ECO:000... | aerobic electron transport chain [GO:0019646]; oxidative phosphorylation [GO:0006119] | cytochrome complex [GO:0070069]; membrane [GO:0016020]; plasma membrane [GO:0005886] | electron transfer activity [GO:0009055]; heme binding [GO:0020037]; metal ion binding [GO:0046872]; oxidoreductase activity, acting on diphenols and related substances as donors [GO:0016679]; oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor [GO:0016682] | PF01654; | null | Cytochrome ubiquinol oxidase subunit 1 family | PTM: 86% of isolated protein was N-formylated. {ECO:0000269|PubMed:26017780, ECO:0000269|PubMed:3281937}. | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15013751, ECO:0000269|PubMed:16079137}; Multi-pass membrane protein {ECO:0000269|PubMed:15013751, ECO:0000269|PubMed:16079137}. | CATALYTIC ACTIVITY: Reaction=2 a ubiquinol + 4 H(+)(in) + O2(in) = 2 a ubiquinone + 4 H(+)(out) + 2 H2O(in); Xref=Rhea:RHEA:40527, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976; EC=7.1.1.7; Evidence={ECO:0000269|PubMed:1850294, EC... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.1 mM for ubiquinol-1 {ECO:0000269|PubMed:6307994}; KM=0.28 mM for 2,3,5,6-tetramethyl-p-phenylenediamine {ECO:0000269|PubMed:6307994}; KM=0.68 mM for N,N,N',N'-tetramethyl-p-phenylenediamine {ECO:0000269|PubMed:6307994}; Vmax=383 umol/min/mg enzyme for ubiquinol-... | PATHWAY: Energy metabolism; oxidative phosphorylation. | null | null | FUNCTION: A terminal oxidase that produces a proton motive force by the vectorial transfer of protons across the inner membrane. It is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at low aeration. Generates a proton motive force using protons and electrons from opposit... | Escherichia coli (strain K12) |
P0ABK2 | CYDB_ECOLI | MIDYEVLRFIWWLLVGVLLIGFAVTDGFDMGVGMLTRFLGRNDTERRIMINSIAPHWDGNQVWLITAGGALFAAWPMVYAAAFSGFYVAMILVLASLFFRPVGFDYRSKIEETRWRNMWDWGIFIGSFVPPLVIGVAFGNLLQGVPFNVDEYLRLYYTGNFFQLLNPFGLLAGVVSVGMIITQGATYLQMRTVGELHLRTRATAQVAALVTLVCFALAGVWVMYGIDGYVVKSTMDHYAASNPLNKEVVREAGAWLVNFNNTPILWAIPALGVVLPLLTILTARMDKAAWAFVFSSLTLACIILTAGIAMFPFVMPSSTM... | 7.1.1.7 | COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000269|PubMed:2656671, ECO:0000269|PubMed:3013299, ECO:0000269|PubMed:6307994}; Note=Binds 1 protoheme IX center (heme b595, originally called cytochrome a1) per heterodimer, in conjunction with CydA. {ECO:0000269|PubMed:2656671, ECO:0000269|PubMed:3013299, ... | aerobic electron transport chain [GO:0019646]; oxidative phosphorylation [GO:0006119] | cytochrome complex [GO:0070069]; membrane [GO:0016020]; plasma membrane [GO:0005886] | electron transfer activity [GO:0009055]; metal ion binding [GO:0046872]; oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor [GO:0016682] | PF02322; | null | Cytochrome ubiquinol oxidase subunit 2 family | PTM: The N-terminus is blocked. | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15013751, ECO:0000269|PubMed:16079137}; Multi-pass membrane protein {ECO:0000269|PubMed:15013751, ECO:0000269|PubMed:16079137}. Note=The displayed topology is based on (PubMed:15013751) not the large scale studies (PubMed:15919996). {ECO:0000269|PubMed:15013... | CATALYTIC ACTIVITY: Reaction=2 a ubiquinol + 4 H(+)(in) + O2(in) = 2 a ubiquinone + 4 H(+)(out) + 2 H2O(in); Xref=Rhea:RHEA:40527, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976; EC=7.1.1.7; Evidence={ECO:0000269|PubMed:1850294}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.1 mM for ubiquinol-1 {ECO:0000269|PubMed:6307994}; KM=0.28 mM for 2,3,5,6-tetramethyl-p-phenylenediamine {ECO:0000269|PubMed:6307994}; KM=0.68 mM for N,N,N',N'-tetramethyl-p-phenylenediamine {ECO:0000269|PubMed:6307994}; Vmax=383 umol/min/mg enzyme for ubiquinol-... | PATHWAY: Energy metabolism; oxidative phosphorylation. | null | null | FUNCTION: A terminal oxidase that produces a proton motive force by the vectorial transfer of protons across the inner membrane. It is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at low aeration. Generates a proton motive force using protons and electrons from opposit... | Escherichia coli (strain K12) |
P0ABK5 | CYSK_ECOLI | MSKIFEDNSLTIGHTPLVRLNRIGNGRILAKVESRNPSFSVKCRIGANMIWDAEKRGVLKPGVELVEPTSGNTGIALAYVAAARGYKLTLTMPETMSIERRKLLKALGANLVLTEGAKGMKGAIQKAEEIVASNPEKYLLLQQFSNPANPEIHEKTTGPEIWEDTDGQVDVFIAGVGTGGTLTGVSRYIKGTKGKTDLISVAVEPTDSPVIAQALAGEEIKPGPHKIQGIGAGFIPANLDLKLVDKVIGITNEEAISTARRLMEEEGILAGISSGAAVAAALKLQEDESFTNKNIVVILPSSGERYLSTALFADLFTEKE... | 2.5.1.47; 4.5.1.5 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:27531961, ECO:0000269|Ref.6}; | amino acid biosynthetic process [GO:0008652]; cysteine biosynthetic process from serine [GO:0006535] | cysteine synthase complex [GO:0009333]; cytoplasm [GO:0005737]; cytosol [GO:0005829] | cystathionine beta-synthase activity [GO:0004122]; cysteine synthase activity [GO:0004124]; identical protein binding [GO:0042802]; L-cysteine desulfhydrase activity [GO:0080146]; protein homodimerization activity [GO:0042803]; pyridoxal phosphate binding [GO:0030170]; S-carboxymethylcysteine synthase activity [GO:0050... | PF00291; | 3.40.50.1100; | Cysteine synthase/cystathionine beta-synthase family | null | null | CATALYTIC ACTIVITY: Reaction=hydrogen sulfide + O-acetyl-L-serine = acetate + L-cysteine; Xref=Rhea:RHEA:14829, ChEBI:CHEBI:29919, ChEBI:CHEBI:30089, ChEBI:CHEBI:35235, ChEBI:CHEBI:58340; EC=2.5.1.47; Evidence={ECO:0000269|Ref.6}; CATALYTIC ACTIVITY: Reaction=3-chloro-L-alanine + thioglycolate = chloride + H(+) + S-car... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=40 mM for 3-chloro-L-alanine {ECO:0000269|Ref.6}; KM=15.4 mM for thioglycolate {ECO:0000269|Ref.6}; | PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine from L-serine: step 2/2. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9-10.5. {ECO:0000269|Ref.6}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius. {ECO:0000269|Ref.6}; | FUNCTION: (Microbial infection) In addition to its role in cysteine synthesis, stimulates the tRNase activity of CdiA-CT from E.coli strain 536 / UPEC; stimulation does not require O-acetylserine sulfhydrylase activity. CdiA is the toxic component of a toxin-immunity protein module, which functions as a cellular contac... | Escherichia coli (strain K12) |
P0ABK7 | CSGB_ECOLI | MKNKLLFMMLTILGAPGIAAAAGYDLANSEYNFAVNELSKSSFNQAAIIGQAGTNNSAQLRQGGSKLLAVVAQEGSSNRAKIDQTGDYNLAYIDQAGSANDASISQGAYGNTAMIIQKGSGNKANITQYGTQKTAIVVQRQSQMAIRVTQR | null | null | amyloid fibril formation [GO:1990000]; cell adhesion [GO:0007155]; curli assembly [GO:0098775]; regulation of amyloid fibril formation [GO:1905906]; single-species biofilm formation [GO:0044010] | cell outer membrane [GO:0009279]; pilus [GO:0009289] | identical protein binding [GO:0042802] | PF07012; | null | CsgA/CsgB family | null | SUBCELLULAR LOCATION: Fimbrium. Note=Part of the curli surface structure. | null | null | null | null | null | FUNCTION: Curlin is the structural subunit of the curli fimbriae. Curli are coiled surface structures that assemble preferentially at growth temperatures below 37 degrees Celsius. Curli can bind to fibronectin. The minor subunit is the nucleation component of curlin monomers. Coexpression of cellulose and thin aggregat... | Escherichia coli (strain K12) |
P0ABK9 | NRFA_ECOLI | MTRIKINARRIFSLLIPFFFFTSVHAEQTAAPAKPVTVEAKNETFAPQHPDQYLSWKATSEQSERVDALAEDPRLVILWAGYPFSRDYNKPRGHAFAVTDVRETLRTGAPKNAEDGPLPMACWSCKSPDVARLIQKDGEDGYFHGKWARGGPEIVNNLGCADCHNTASPEFAKGKPELTLSRPYAARAMEAIGKPFEKAGRFDQQSMVCGQCHVEYYFDGKNKAVKFPWDDGMKVENMEQYYDKIAFSDWTNSLSKTPMLKAQHPEYETWTAGIHGKNNVTCIDCHMPKVQNAEGKLYTDHKIGNPFDNFAQTCANCHTQ... | 1.7.2.2 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:11863430, ECO:0000269|PubMed:18311941, ECO:0000269|PubMed:20629638, ECO:0000269|PubMed:22103542}; Note=Binds 1 Ca(2+) ion per monomer. {ECO:0000269|PubMed:11863430, ECO:0000269|PubMed:18311941, ECO:0000269|PubMed:20629638, ECO:0000269|PubMed:22... | anaerobic electron transport chain [GO:0019645]; nitrate assimilation [GO:0042128] | outer membrane-bounded periplasmic space [GO:0030288] | calcium ion binding [GO:0005509]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; nitric oxide reductase activity [GO:0016966]; nitrite reductase (cytochrome, ammonia-forming) activity [GO:0042279] | PF02335; | 1.20.140.10; | Cytochrome c-552 family | null | SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:11863430, ECO:0000269|PubMed:7934939, ECO:0000269|PubMed:9593308}. | CATALYTIC ACTIVITY: Reaction=6 Fe(III)-[cytochrome c] + 2 H2O + NH4(+) = 6 Fe(II)-[cytochrome c] + 8 H(+) + nitrite; Xref=Rhea:RHEA:13089, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16301, ChEBI:CHEBI:28938, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.7.2.2; Evidence={E... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=28 uM for nitrite {ECO:0000269|PubMed:11863430}; KM=30 uM for nitrite {ECO:0000269|PubMed:18311941}; KM=22 uM for nitrite {ECO:0000269|PubMed:20629638}; KM=70 uM for sulfite {ECO:0000269|PubMed:20629638}; KM=30 mM for hydroxylamine {ECO:0000269|PubMed:11863430}; | PATHWAY: Nitrogen metabolism; nitrate reduction (assimilation). {ECO:0000305|PubMed:7934939}. | null | null | FUNCTION: Catalyzes the reduction of nitrite to ammonia, consuming six electrons in the process (PubMed:11863430, PubMed:18311941, PubMed:20629638, PubMed:9593308). Has very low activity toward hydroxylamine (PubMed:11863430). Has even lower activity toward sulfite (PubMed:20629638). Sulfite reductase activity is maxim... | Escherichia coli (strain K12) |
P0ABL3 | NAPB_ECOLI | MKSHDLKKALCQWTAMLALVVSGAVWAANGVDFSQSPEVSGTQEGAIRMPKEQDRMPLNYVNQPPMIPHSVEGYQVTTNTNRCLQCHGVESYRTTGAPRISPTHFMDSDGKVGAEVAPRRYFCLQCHVPQADTAPIVGNTFTPSKGYGK | null | null | anaerobic respiration [GO:0009061]; nitrate assimilation [GO:0042128] | nitrate reductase complex [GO:0009325]; periplasmic space [GO:0042597] | metal ion binding [GO:0046872] | PF03892; | null | NapB family | PTM: Binds 2 heme C groups per subunit. | SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:10234835, ECO:0000269|PubMed:10548535, ECO:0000269|PubMed:17130127}. | null | null | null | null | null | FUNCTION: Electron transfer subunit of the periplasmic nitrate reductase complex NapAB. Receives electrons from the membrane-anchored tetraheme c-type NapC protein and transfers these to NapA subunit, thus allowing electron flow between membrane and periplasm. Essential for periplasmic nitrate reduction with nitrate as... | Escherichia coli (strain K12) |
P0ABN1 | KDGL_ECOLI | MANNTTGFTRIIKAAGYSWKGLRAAWINEAAFRQEGVAVLLAVVIACWLDVDAITRVLLISSVMLVMIVEILNSAIEAVVDRIGSEYHELSGRAKDMGSAAVLIAIIVAVITWCILLWSHFG | 2.7.1.107 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:3009449}; Note=Mn(2+), Zn(2+), Cd(2+) and Co(2+) support activity to lesser extents. {ECO:0000269|PubMed:3009449}; | phosphatidic acid biosynthetic process [GO:0006654]; phosphorylation [GO:0016310]; response to UV [GO:0009411] | membrane [GO:0016020]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; ATP-dependent diacylglycerol kinase activity [GO:0004143]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872] | PF01219; | 1.10.287.3610; | Bacterial diacylglycerol kinase family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:217867, ECO:0000269|PubMed:2984194, ECO:0000269|PubMed:8071224}; Multi-pass membrane protein {ECO:0000255, ECO:0000269|PubMed:8071224}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycerol + ATP = a 1,2-diacyl-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:10272, ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:30616, ChEBI:CHEBI:58608, ChEBI:CHEBI:456216; EC=2.7.1.107; Evidence={ECO:0000269|PubMed:218816, ECO:0000269|PubMed:2828054, ECO:0000269... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=62 uM for sn-1,2-dipalmitate {ECO:0000269|PubMed:218816}; KM=230 uM for ceramide {ECO:0000269|PubMed:218816}; KM=1400 uM for ATP {ECO:0000269|PubMed:218816}; KM=300 uM for ATP {ECO:0000269|PubMed:3009449}; KM=120 uM for ATP {ECO:0000269|PubMed:10220339}; Vmax=10.4 ... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.3-8.3. {ECO:0000269|PubMed:218816}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Apoprotein in organic solution has an unusual stability towards heating to 100 degrees Celsius. {ECO:0000269|PubMed:2828054}; | FUNCTION: Catalyzes the ATP-dependent phosphorylation of sn-l,2-diacylglycerol (DAG) to phosphatidic acid (PubMed:218816, PubMed:2828054, PubMed:2984194, PubMed:3009449, PubMed:6277376, PubMed:6303781, PubMed:9305868). Involved in the recycling of diacylglycerol produced as a by-product during membrane-derived oligosac... | Escherichia coli (strain K12) |
P0ABN5 | DCUA_ECOLI | MLVVELIIVLLAIFLGARLGGIGIGFAGGLGVLVLAAIGVKPGNIPFDVISIIMAVIAAISAMQVAGGLDYLVHQTEKLLRRNPKYITILAPIVTYFLTIFAGTGNISLATLPVIAEVAKEQGVKPCRPLSTAVVSAQIAITASPISAAVVYMSSVMEGHGISYLHLLSVVIPSTLLAVLVMSFLVTMLFNSKLSDDPIYRKRLEEGLVELRGEKQIEIKSGAKTSVWLFLLGVVGVVIYAIINSPSMGLVEKPLMNTTNAILIIMLSVATLTTVICKVDTDNILNSSTFKAGMSACICILGVAWLGDTFVSNNIDWIKD... | null | null | C4-dicarboxylate transport [GO:0015740]; cellular nitrogen compound biosynthetic process [GO:0044271]; L-aspartate import across plasma membrane [GO:0140009] | plasma membrane [GO:0005886] | C4-dicarboxylate transmembrane transporter activity [GO:0015556]; succinate:fumarate antiporter activity [GO:0005469]; symporter activity [GO:0015293] | PF03605; | null | DcuA/DcuB transporter (TC 2.A.13.1) family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:9733683}; Multi-pass membrane protein {ECO:0000269|PubMed:9733683}. | CATALYTIC ACTIVITY: Reaction=fumarate(in) + L-aspartate(out) = fumarate(out) + L-aspartate(in); Xref=Rhea:RHEA:72459, ChEBI:CHEBI:29806, ChEBI:CHEBI:29991; Evidence={ECO:0000269|PubMed:29995997}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72460; Evidence={ECO:0000269|PubMed:29995997}; CATALYTIC ACTIVITY: Reac... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=43.3 uM for L-aspartate {ECO:0000269|PubMed:29995997}; KM=844 uM for succinate {ECO:0000269|PubMed:29995997}; | null | null | null | FUNCTION: Responsible for the transport of C4-dicarboxylates during aerobic and anaerobic growth (PubMed:29995997, PubMed:7961398, PubMed:8131924, PubMed:8955408). Required for the uptake of L-aspartate as a nitrogen source during aerobic growth (PubMed:29995997). The uptake of L-aspartate in aerobic conditions is coup... | Escherichia coli (strain K12) |
P0ABN9 | DCUB_ECOLI | MLFTIQLIIILICLFYGARKGGIALGLLGGIGLVILVFVFHLQPGKPPVDVMLVIIAVVAASATLQASGGLDVMLQIAEKLLRRNPKYVSIVAPFVTCTLTILCGTGHVVYTILPIIYDVAIKNNIRPERPMAASSIGAQMGIIASPVSVAVVSLVAMLGNVTFDGRHLEFLDLLAITIPSTLIGILAIGIFSWFRGKDLDKDEEFQKFISVPENREYVYGDTATLLDKKLPKSNWLAMWIFLGAIAVVALLGADSDLRPSFGGKPLSMVLVIQMFMLLTGALIIILTKTNPASISKNEVFRSGMIAIVAVYGIAWMAET... | null | null | C4-dicarboxylate transport [GO:0015740] | plasma membrane [GO:0005886] | C4-dicarboxylate transmembrane transporter activity [GO:0015556]; succinate:fumarate antiporter activity [GO:0005469]; symporter activity [GO:0015293] | PF03605; | null | DcuA/DcuB transporter (TC 2.A.13.1) family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:21634397}; Multi-pass membrane protein {ECO:0000269|PubMed:21634397}. | 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:7961398, ECO:0000269|PubMed:8955408}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29325; Evidence={ECO:0000269|PubMed:7961398, ECO... | null | null | null | null | FUNCTION: Bifunctional protein with a transport and a regulatory function (PubMed:18957436, PubMed:27318186). Responsible for the transport of C4-dicarboxylates during anaerobic growth (PubMed:17643228, PubMed:7961398, PubMed:8131924, PubMed:8955408). Catalyzes the uptake of fumarate, malate, aspartate or D-tartrate co... | Escherichia coli (strain K12) |
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