AAS_ECOUT
ID AAS_ECOUT Reviewed; 719 AA.
AC Q1R7H5;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 25-MAY-2022, entry version 84.
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}; OrderedLocusNames=UTI89_C3240;
OS Escherichia coli (strain UTI89 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=364106;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UTI89 / UPEC;
RX PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S.,
RA Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J.,
RA Gordon J.I.;
RT "Identification of genes subject to positive selection in uropathogenic
RT strains of Escherichia coli: a comparative genomics approach.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006).
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; CP000243; ABE08689.1; -; Genomic_DNA.
DR RefSeq; WP_000899024.1; NC_007946.1.
DR AlphaFoldDB; Q1R7H5; -.
DR SMR; Q1R7H5; -.
DR EnsemblBacteria; ABE08689; ABE08689; UTI89_C3240.
DR KEGG; eci:UTI89_C3240; -.
DR HOGENOM; CLU_000022_59_8_6; -.
DR OMA; ANWVYLE; -.
DR Proteomes; UP000001952; Chromosome.
DR GO; GO:0016021; C:integral component of 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: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 Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 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.
DR InterPro; IPR042099; ANL_N_sf.
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; Ligase;
KW Membrane; Multifunctional enzyme; Nucleotide-binding; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..719
FT /note="Bifunctional protein Aas"
FT /id="PRO_1000065638"
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
