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AAS_SALPK
ID   AAS_SALPK               Reviewed;         719 AA.
AC   B5BFH6;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 68.
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=SSPA2680;
OS   Salmonella paratyphi A (strain AKU_12601).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=554290;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AKU_12601;
RX   PubMed=19159446; DOI=10.1186/1471-2164-10-36;
RA   Holt K.E., Thomson N.R., Wain J., Langridge G.C., Hasan R., Bhutta Z.A.,
RA   Quail M.A., Norbertczak H., Walker D., Simmonds M., White B., Bason N.,
RA   Mungall K., Dougan G., Parkhill J.;
RT   "Pseudogene accumulation in the evolutionary histories of Salmonella
RT   enterica serovars Paratyphi A and Typhi.";
RL   BMC Genomics 10:36-36(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; FM200053; CAR60921.1; -; Genomic_DNA.
DR   RefSeq; WP_000896086.1; NC_011147.1.
DR   AlphaFoldDB; B5BFH6; -.
DR   SMR; B5BFH6; -.
DR   KEGG; sek:SSPA2680; -.
DR   HOGENOM; CLU_000022_59_8_6; -.
DR   OMA; ANWVYLE; -.
DR   Proteomes; UP000001869; 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_1000137901"
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
 
 
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