ID   AAS_YERPY               Reviewed;         718 AA.
AC   B1JQC1;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 73.
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=YPK_1027;
OS   Yersinia pseudotuberculosis serotype O:3 (strain YPIII).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=502800;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YPIII;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C.,
RA   Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Challacombe J.F., Green L., Lindler L.E., Nikolich M.P., Richardson P.;
RT   "Complete sequence of Yersinia pseudotuberculosis YPIII.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000950; ACA67328.1; -; Genomic_DNA.
DR   RefSeq; WP_011192876.1; NZ_CP009792.1.
DR   AlphaFoldDB; B1JQC1; -.
DR   SMR; B1JQC1; -.
DR   GeneID; 66844526; -.
DR   KEGG; ypy:YPK_1027; -.
DR   PATRIC; fig|502800.11.peg.1659; -.
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; 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; IPR025110; AMP-bd_C.
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; PTHR43767; LONG-CHAIN-FATTY-ACID--COA LIGASE; 1.
DR   PANTHER; PTHR43767:SF1; NONRIBOSOMAL PEPTIDE SYNTHASE PES1 (EUROFUNG)-RELATED; 1.
DR   Pfam; PF01553; Acyltransferase; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 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; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..718
FT                   /note="Bifunctional protein Aas"
FT                   /id="PRO_1000137906"
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   718 AA;  79416 MW;  A3C7873868B30645 CRC64;
     MAYRLLRALF RGLFRVTIDG VTDQFKHEKL IITPNHVSFL DGALLALFLP IKPVFAVYTS
     ITDTWYMRWL KPYVDFVALD PTNPMAIKHL VRMVEQGRPV VIFPEGRITV TGSLMKIYDG
     AAFVAAKSGA AVVPIRLDGP EFTHFGRLQG VLKTRWFPKI SIHVLPATTI PMPQAPRSRE
     RRVLAGEHLH TIMMAARMAT VPRETLFEAL LSAQTRYGRF KPCIEDVSFK EDSYQTLLKK
     TLGVSRILQR FTVPGEHVGM LLPNATITAA AIFGASLRGR IPALLNYTSG AKGLQSAIIA
     ASLKTIVTSR QFLEKGKLTH LPEQVNEVNW VYLEDLKDTV TLTDKLWILF HLCFPRRAML
     PQQADDSALI LFTSGSEGNP KGVVHSHASL LANVEQIRTI ADFTPRDRFM SSLPLFHAFG
     LTVGLFTPLM TGSRVFLYPS PLHYRVVPEL VYDRNCTVLF GTSTFLGNYA RFAHPYDFAR
     VRYVVAGAEK LAESTKQIWQ DKFGIRILEG YGVTECAPVV AINVPMAAKV NTVGRILPGM
     EARLINVPGI AQGGRLQLRG PNIMRGYLRV ENPGVLEQPS AENAQGELDA NWYDTGDIVT
     LDEQGFCAIR GRVKRFAKLA GEMVSLESVE QLAISLSPEG QHAAAAKTDS AKGEALVLFT
     TDSEITRERL IKAARENGVP ELAVPRDIRV VKALPLLGSG KPDFVTLGKM AQDPEMSV
//