Tag | Content |
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CPLM ID | CPLM-010333 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Protein YdeP |
Protein Synonyms/Alias | |
Gene Name | ydeP |
Gene Synonyms/Alias | b1501; JW1495 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
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335 | DVLNSEWKDIERISG | acetylation | [1] |
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Reference | [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli. Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C. Mol Cell. 2013 Jul 25;51(2):265-72. [ PMID: 23830618] |
Functional Description | Probably involved in acid resistance. |
Sequence Annotation | METAL 49 49 Iron-sulfur (4Fe-4S) (By similarity). METAL 52 52 Iron-sulfur (4Fe-4S) (By similarity). |
Keyword | 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Metal-binding; Molybdenum; Oxidoreductase; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 759 AA |
Protein Sequence | MKKKIESYQG AAGGWGAVKS VANAVRKQMD IRQDVIAMFD MNKPEGFDCP GCAWPDPKHS 60 ASFDICENGA KAIAWEVTDK QVNASFFAEN TVQSLLTWGD HELEAAGRLT QPLKYDAVSD 120 CYKPLSWQQA FDEIGARLQS YSDPNQVEFY TSGRTSNEAA FLYQLFAREY GSNNFPDCSN 180 MCHEPTSVGL AASIGVGKGT VLLEDFEKCD LVICIGHNPG TNHPRMLTSL RALVKRGAKM 240 IAINPLQERG LERFTAPQNP FEMLTNSETQ LASAYYNVRI GGDMALLKGM MRLLIERDDA 300 ASAAGRPSLL DDEFIQTHTV GFDELRRDVL NSEWKDIERI SGLSQTQIAE LADAYAAAER 360 TIICYGMGIT QHEHGTQNVQ QLVNLLLMKG NIGKPGAGIC PLRGHSNVQG DRTVGITEKP 420 SAEFLARLGE RYGFTPPHAP GHAAIASMQA ICTGQARALI CMGGNFALAM PDREASAVPL 480 TQLDLAVHVA TKLNRSHLLT ARHSYILPVL GRSEIDMQKN GAQAVTVEDS MSMIHASRGV 540 LKPAGVMLKS ECAVVAGIAQ AALPQSVVAW EYLVEDYDRI RNDIEAVLPE FADYNQRIRH 600 PGGFHLINAA AERRWMTPSG KANFITSKGL LEDPSSAFNS KLVMATVRSH DQYNTTIYGM 660 DDRYRGVFGQ RDVVFMSAKQ AKICRVKNGE RVNLIALTPD GKRSSRRMDR LKVVIYPMAD 720 RSLVTYFPES NHMLTLDNHD PLSGIPGYKS IPVELEPSN 759 |
Gene Ontology | GO:0016020; C:membrane; IBA:RefGenome. GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. GO:0008863; F:formate dehydrogenase (NAD+) activity; IEA:InterPro. GO:0030151; F:molybdenum ion binding; IEA:InterPro. GO:0016491; F:oxidoreductase activity; IBA:RefGenome. GO:0010447; P:response to acidity; IMP:EcoCyc. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |