Tag | Content |
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CPLM ID | CPLM-005947 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Bifunctional protein aas |
Protein Synonyms/Alias | 2-acylglycerophosphoethanolamine acyltransferase; 2-acyl-GPE acyltransferase; Acyl-[acyl-carrier-protein]--phospholipid O-acyltransferase; Acyl-[acyl-carrier-protein] synthetase; Acyl-ACP synthetase; Long-chain-fatty-acid--[acyl-carrier-protein] ligase |
Gene Name | aas |
Gene Synonyms/Alias | b2836; JW2804 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
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88 | PTQPMAIKHLVRLVE | acetylation | [1] | 250 | FVGRILEKYSVEGER | acetylation | [1] | 317 | RQFLDKGKLWHLPEQ | acetylation | [1] | 337 | WVYLEDLKADVTTAD | 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 | Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1. |
Sequence Annotation | REGION 15 138 Acyltransferase. REGION 233 646 AMP-binding. ACT_SITE 36 36 |
Keyword | Acyltransferase; ATP-binding; Cell inner membrane; Cell membrane; Complete proteome; Ligase; Membrane; Multifunctional enzyme; Nucleotide-binding; Reference proteome; Transferase; Transmembrane; Transmembrane helix. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 719 AA |
Protein Sequence | MLFSFFRNLC RVLYRVRVTG DTQALKGERV LITPNHVSFI DGILLGLFLP VRPVFAVYTS 60 ISQQWYMRWL KSFIDFVPLD PTQPMAIKHL VRLVEQGRPV VIFPEGRITT TGSLMKIYDG 120 AGFVAAKSGA TVIPVRIEGA ELTHFSRLKG LVKRRLFPQI TLHILPPTQV AMPDAPRARD 180 RRKIAGEMLH QIMMEARMAV RPRETLYESL LSAMYRFGAG KKCVEDVNFT PDSYRKLLTK 240 TLFVGRILEK YSVEGERIGL MLPNAGISAA VIFGAIARRR MPAMMNYTAG VKGLTSAITA 300 AEIKTIFTSR QFLDKGKLWH LPEQLTQVRW VYLEDLKADV TTADKVWIFA HLLMPRLAQV 360 KQQPEEEALI LFTSGSEGHP KGVVHSHKSI LANVEQIKTI ADFTTNDRFM SALPLFHSFG 420 LTVGLFTPLL TGAEVFLYPS PLHYRIVPEL VYDRSCTVLF GTSTFLGHYA RFANPYDFYR 480 LRYVVAGAEK LQESTKQLWQ DKFGLRILEG YGVTECAPVV SINVPMAAKP GTVGRILPGM 540 DARLLSVPGI EEGGRLQLKG PNIMNGYLRV EKPGVLEVPT AENVRGEMER GWYDTGDIVR 600 FDEQGFVQIQ GRAKRFAKIA GEMVSLEMVE QLALGVSPDK VHATAIKSDA SKGEALVLFT 660 TDNELTRDKL QQYAREHGVP ELAVPRDIRY LKQMPLLGSG KPDFVTLKSW VDEAEQHDE 719 |
Gene Ontology | GO:0016021; C:integral to membrane; IDA:EcoliWiki. GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. GO:0008779; F:acyl-[acyl-carrier-protein]-phospholipid O-acyltransferase activity; IDA:EcoliWiki. GO:0005524; F:ATP binding; IEA:UniProtKB-KW. GO:0008922; F:long-chain fatty acid [acyl-carrier-protein] ligase activity; IDA:EcoliWiki. GO:0006631; P:fatty acid metabolic process; IGI:EcoliWiki. GO:0008654; P:phospholipid biosynthetic process; IGI:EcoliWiki. |
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