ID AAS_ECOSE Reviewed; 719 AA.
AC B6I6W1;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 29-MAY-2013, entry version 33.
DE RecName: Full=Bifunctional protein aas;
DE Includes:
DE RecName: Full=2-acylglycerophosphoethanolamine acyltransferase;
DE EC=2.3.1.40;
DE AltName: Full=2-acyl-GPE acyltransferase;
DE AltName: Full=Acyl-[acyl-carrier-protein]--phospholipid O-acyltransferase;
DE Includes:
DE RecName: Full=Acyl-[acyl-carrier-protein] synthetase;
DE EC=6.2.1.20;
DE AltName: Full=Acyl-ACP synthetase;
DE AltName: Full=Long-chain-fatty-acid--[acyl-carrier-protein] ligase;
GN Name=aas; OrderedLocusNames=ECSE_3093;
OS Escherichia coli (strain SE11).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=409438;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SE11;
RX PubMed=18931093; DOI=10.1093/dnares/dsn026;
RA Oshima K., Toh H., Ogura Y., Sasamoto H., Morita H., Park S.-H.,
RA Ooka T., Iyoda S., Taylor T.D., Hayashi T., Itoh K., Hattori M.;
RT "Complete genome sequence and comparative analysis of the wild-type
RT commensal Escherichia coli strain SE11 isolated from a healthy
RT adult.";
RL DNA Res. 15:375-386(2008).
CC -!- FUNCTION: Plays a role in lysophospholipid acylation. Transfers
CC fatty acids to the 1-position via an enzyme-bound acyl-ACP
CC intermediate in the presence of ATP and magnesium. Its
CC physiological function is to regenerate phosphatidylethanolamine
CC from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by
CC transacylation reactions or degradation by phospholipase A1 (By
CC similarity).
CC -!- CATALYTIC ACTIVITY: Acyl-[acyl-carrier-protein] + O-(2-acyl-sn-
CC glycero-3-phospho)ethanolamine = [acyl-carrier-protein] + O-(1-
CC beta-acyl-2-acyl-sn-glycero-3-phospho)ethanolamine.
CC -!- CATALYTIC ACTIVITY: ATP + an acid + [acyl-carrier-protein] = AMP +
CC diphosphate + acyl-[acyl-carrier-protein].
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane
CC protein (By similarity).
CC -!- SIMILARITY: In the N-terminal section; belongs to the 2-acyl-GPE
CC acetyltransferase family.
CC -!- SIMILARITY: In the C-terminal section; belongs to the ATP-
CC dependent AMP-binding enzyme family.
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DR EMBL; AP009240; BAG78617.1; -; Genomic_DNA.
DR RefSeq; YP_002294368.1; NC_011415.1.
DR ProteinModelPortal; B6I6W1; -.
DR STRING; 409438.ECSE_3093; -.
DR EnsemblBacteria; BAG78617; BAG78617; ECSE_3093.
DR GeneID; 7001478; -.
DR KEGG; ecy:ECSE_3093; -.
DR PATRIC; 18424800; VBIEscCol83070_3265.
DR eggNOG; COG0318; -.
DR HOGENOM; HOG000004907; -.
DR KO; K05939; -.
DR OMA; ANWVYLE; -.
DR ProtClustDB; PRK08043; -.
DR BioCyc; ECOL409438:GHUU-3148-MONOMER; -.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008779; F:acyl-[acyl-carrier-protein]-phospholipid O-acyltransferase activity; IEA:HAMAP.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008922; F:long-chain fatty acid [acyl-carrier-protein] ligase activity; IEA:HAMAP.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:InterPro.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:InterPro.
DR HAMAP; MF_01162; Aas; 1; -.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR023775; Bifunctional_Aas.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR Pfam; PF01553; Acyltransferase; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR SMART; SM00563; PlsC; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 3: Inferred from homology;
KW Acyltransferase; ATP-binding; Cell inner membrane; Cell membrane;
KW Complete proteome; Ligase; Membrane; Multifunctional enzyme;
KW Nucleotide-binding; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1 719 Bifunctional protein aas.
FT /FTId=PRO_1000137890.
FT TRANSMEM 258 277 Helical; (Potential).
FT TRANSMEM 409 433 Helical; (Potential).
FT REGION 15 138 Acyltransferase.
FT REGION 233 646 AMP-binding.
FT ACT_SITE 36 36 By similarity.
SQ SEQUENCE 719 AA; 80740 MW; 139EBA7043BE21FB CRC64;
MLFSFFRNLC RVLYRVRVTG DTQALKGERV LITPNHVSFI DGILLGLFLP VRPVFAVYTS
ISQQWYMRWL KSFIDFVPLD PTQPMAIKHL VRLVEQGRPV VIFPEGRITT TGSLMKIYDG
AGFVAAKSGA TVIPVRIEGA ELTHFSRLKG LVKRRLFPQI TLHILPPTQV EMPDAPRARD
RRKIAGEMLH QIMMEARMAV RPRETLYESL LSAMYRFGAG KKCVEDVNFT PDSYRKLLTK
TLFVGRILEK YSVEGERIGL MLPNAGISAA VIFGAIARRR IPAMMNYTAG VKGLTSAITA
AEIKTIFTSR QFLDKGKLWH LPEQLTQVRW VYLEDLKADV TTADKVWIFA HLLMPRLAQV
KQQPEEEALI LFTSGSEGHP KGVVHSHKSI LANVEQIKTI ADFTTNDRFM SALPLFHSFG
LTVGLFTPLL TGAEVFLYPS PLHYRIVPEL VYDRSCTVLF GTSTFLGHYA RFANPYDFYR
LRYVVAGAEK LQESTKQLWQ DKFGLRILEG YGVTECAPVV SINVPMAAKP GTVGRILPGM
DARLLSVPGI EEGGRLQLKG PNIMNGYLRV EKPGVLEVPT AENVRGEMER GWYDTGDIVR
FDEQGFVQIQ GRAKRFAKIA GEMVSLEMVE QLALGVSPDK VHATAIKSDA SKGEALVLFT
TDNELTRDKL QQYAREHGVP ELAVPRDIRY LKQMPLLGSG KPDFVTLKSW VDEAEQHDE
//
