AAS_SALPA
ID AAS_SALPA Reviewed; 719 AA.
AC Q5PEN7;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 25-MAY-2022, entry version 90.
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=SPA2875;
OS Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=295319;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9150 / SARB42;
RX PubMed=15531882; DOI=10.1038/ng1470;
RA McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA Warren W., Florea L., Spieth J., Wilson R.K.;
RT "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT restricted serovars of Salmonella enterica that cause typhoid.";
RL Nat. Genet. 36:1268-1274(2004).
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; CP000026; AAV78720.1; -; Genomic_DNA.
DR RefSeq; WP_000896086.1; NC_006511.1.
DR AlphaFoldDB; Q5PEN7; -.
DR SMR; Q5PEN7; -.
DR EnsemblBacteria; AAV78720; AAV78720; SPA2875.
DR KEGG; spt:SPA2875; -.
DR HOGENOM; CLU_000022_59_8_6; -.
DR OMA; ANWVYLE; -.
DR Proteomes; UP000008185; 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_0000193051"
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; 80511 MW; 7CEB9BAEF7475651 CRC64;
MLFGFFRNLF RVLYRVRVTG DVRALQGNRV LITPNHVSFI DGMLLALFLP VRPVFAVYTS
ISQQWYMRWL TPLIDFVPLD PTKPMSIKHL MRLVEQGRPV VIFPEGRISV TGSLMKIYDG
AGFVAAKSGA TVIPLRIDGA ELTPFSRLKG LVKRRLFPRI QLHILPPTQI PMPEAPRARD
RRKIAGEMLH QIMMEARMAV RPRETLYESL LAAQYRYGAG KNCIEDINFT PDTYRKLLTK
TLFVGRILEK YSVEGEKIGL MLPNAAISAA VIFGAVSRRR IPAMMNYTAG VKGLTSAIAA
AEIKTIFTSR QFLDKGKLWH LPEQLTQVRW VYLEDLKADV TLADKLWIFA HLLAPRLAQV
KQQPEDAAII LFTSGSEGHP KGVVHSHKSI LANVEQIKTI ADFTANDRFM SALPLFHSFG
LTVGLFTPLL TGAEVFLYPS PLHYRIVPEL VYDRNCTVLF GTSTFLGNYA RFANPYDFYR
LRYVVAGAEK LQESTKQLWQ DKFGLRILEG YGVTECAPVV SINVPMAAKP GTVGRILPGM
DARLLAVPGI ENGGRLQLKG PNIMNGYLRV EKPGVLEVPS AENARGETER GWYDTGDIVR
FDENGFVQIQ GRAKRFAKIA GEMVSLEMVE QLALGVSADK MHATAIKSDA SKGEALVLFT
TDSELTREKL QHYAREHGIP ELAVPRDIRY LKQLPLLGSG KPDFVTLKSW VDAPEQHHE
