ID   AAS_ECO45               Reviewed;         719 AA.
AC   B7MLI2;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   RecName: Full=Bifunctional protein Aas {ECO:0000255|HAMAP-Rule:MF_01162};
DE   Includes:
DE     RecName: Full=2-acylglycerophosphoethanolamine acyltransferase {ECO:0000255|HAMAP-Rule:MF_01162};
DE              EC=2.3.1.40 {ECO:0000255|HAMAP-Rule:MF_01162};
DE     AltName: Full=2-acyl-GPE acyltransferase {ECO:0000255|HAMAP-Rule:MF_01162};
DE     AltName: Full=Acyl-[acyl-carrier-protein]--phospholipid O-acyltransferase {ECO:0000255|HAMAP-Rule:MF_01162};
DE   Includes:
DE     RecName: Full=Acyl-[acyl-carrier-protein] synthetase {ECO:0000255|HAMAP-Rule:MF_01162};
DE              EC=6.2.1.20 {ECO:0000255|HAMAP-Rule:MF_01162};
DE     AltName: Full=Acyl-ACP synthetase {ECO:0000255|HAMAP-Rule:MF_01162};
DE     AltName: Full=Long-chain-fatty-acid--[acyl-carrier-protein] ligase {ECO:0000255|HAMAP-Rule:MF_01162};
GN   Name=aas {ECO:0000255|HAMAP-Rule:MF_01162};
GN   OrderedLocusNames=ECS88_3131;
OS   Escherichia coli O45:K1 (strain S88 / ExPEC).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585035;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S88 / ExPEC;
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
CC   -!- FUNCTION: Plays a role in lysophospholipid acylation. Transfers fatty
CC       acids to the 1-position via an enzyme-bound acyl-ACP intermediate in
CC       the presence of ATP and magnesium. Its physiological function is to
CC       regenerate phosphatidylethanolamine from 2-acyl-glycero-3-
CC       phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or
CC       degradation by phospholipase A1. {ECO:0000255|HAMAP-Rule:MF_01162}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2-acyl-sn-glycero-3-phosphoethanolamine + a fatty acyl-[ACP]
CC         = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + holo-[ACP];
CC         Xref=Rhea:RHEA:10304, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:14125,
CC         ChEBI:CHEBI:64479, ChEBI:CHEBI:64612, ChEBI:CHEBI:65213,
CC         ChEBI:CHEBI:138651; EC=2.3.1.40; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01162};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a long-chain fatty acid + ATP + holo-[ACP] = a long-chain
CC         fatty acyl-[ACP] + AMP + diphosphate; Xref=Rhea:RHEA:45588,
CC         Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:12682, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57560, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:133243, ChEBI:CHEBI:456215; EC=6.2.1.20;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01162};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01162}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01162}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the 2-acyl-GPE
CC       acetyltransferase family. {ECO:0000255|HAMAP-Rule:MF_01162}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the ATP-dependent
CC       AMP-binding enzyme family. {ECO:0000255|HAMAP-Rule:MF_01162}.
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DR   EMBL; CU928161; CAR04371.1; -; Genomic_DNA.
DR   RefSeq; WP_000899024.1; NC_011742.1.
DR   AlphaFoldDB; B7MLI2; -.
DR   SMR; B7MLI2; -.
DR   KEGG; ecz:ECS88_3131; -.
DR   HOGENOM; CLU_000022_59_8_6; -.
DR   Proteomes; UP000000747; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008779; F:acyl-[acyl-carrier-protein]-phospholipid O-acyltransferase activity; IEA:UniProtKB-UniRule.
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:UniProtKB-UniRule.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:InterPro.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:InterPro.
DR   CDD; cd05909; AAS_C; 1.
DR   CDD; cd07989; LPLAT_AGPAT-like; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   HAMAP; MF_01162; Aas; 1.
DR   InterPro; IPR023775; Aas.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR   InterPro; IPR042099; ANL_N_sf.
DR   InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR   PANTHER; PTHR43201; ACYL-COA SYNTHETASE; 1.
DR   PANTHER; PTHR43201:SF5; MEDIUM-CHAIN ACYL-COA LIGASE ACSF2, MITOCHONDRIAL; 1.
DR   Pfam; PF01553; Acyltransferase; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   SMART; SM00563; PlsC; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; ATP-binding; Cell inner membrane; Cell membrane; Ligase;
KW   Membrane; Multifunctional enzyme; Nucleotide-binding; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..719
FT                   /note="Bifunctional protein Aas"
FT                   /id="PRO_1000137885"
FT   TRANSMEM        258..277
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01162"
FT   TRANSMEM        409..433
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01162"
FT   REGION          15..138
FT                   /note="Acyltransferase"
FT   REGION          233..646
FT                   /note="AMP-binding"
FT   ACT_SITE        36
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01162"
SQ   SEQUENCE   719 AA;  80826 MW;  E050AF0C2EFA93BD CRC64;
     MLFSFFRNLC RVLYRVRVTG DTKALKGERV LITPNHVSFI DGILLALFLP 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 AENIRGEMER DWYDTGDIVR
     FDEQGFVQIQ GRAKRFAKIA GEMVSLEMVE QLALGVSPDK VHATAIKSDA SKGEALVLFT
     TDNELTRDKL QQYAREHGVP ELAVPRDIRY LKQMPLLGSG KPDFVTLKSW VDEAEQHDE
//