CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
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
88PTQPMAIKHLVRLVEacetylation[1]
250FVGRILEKYSVEGERacetylation[1]
317RQFLDKGKLWHLPEQacetylation[1]
337WVYLEDLKADVTTADacetylation[1]
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. 
Interpro
 IPR020845; AMP-binding_CS.
 IPR000873; AMP-dep_Synth/Lig.
 IPR023775; Bifunctional_Aas.
 IPR002123; Plipid/glycerol_acylTrfase. 
Pfam
 PF01553; Acyltransferase
 PF00501; AMP-binding 
SMART
 SM00563; PlsC 
PROSITE
 PS00455; AMP_BINDING 
PRINTS