ID   PLSB_PSEA8              Reviewed;         834 AA.
AC   B7V2U0;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Glycerol-3-phosphate acyltransferase {ECO:0000255|HAMAP-Rule:MF_00393};
DE            Short=GPAT {ECO:0000255|HAMAP-Rule:MF_00393};
DE            EC=2.3.1.15 {ECO:0000255|HAMAP-Rule:MF_00393};
GN   Name=plsB {ECO:0000255|HAMAP-Rule:MF_00393}; OrderedLocusNames=PLES_13111;
OS   Pseudomonas aeruginosa (strain LESB58).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=557722;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LESB58;
RX   PubMed=19047519; DOI=10.1101/gr.086082.108;
RA   Winstanley C., Langille M.G.I., Fothergill J.L., Kukavica-Ibrulj I.,
RA   Paradis-Bleau C., Sanschagrin F., Thomson N.R., Winsor G.L., Quail M.A.,
RA   Lennard N., Bignell A., Clarke L., Seeger K., Saunders D., Harris D.,
RA   Parkhill J., Hancock R.E.W., Brinkman F.S.L., Levesque R.C.;
RT   "Newly introduced genomic prophage islands are critical determinants of in
RT   vivo competitiveness in the Liverpool epidemic strain of Pseudomonas
RT   aeruginosa.";
RL   Genome Res. 19:12-23(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an acyl-CoA + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-
CC         phosphate + CoA; Xref=Rhea:RHEA:15325, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57597, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342; EC=2.3.1.15;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00393};
CC   -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC       diacylglycerol from sn-glycerol 3-phosphate: step 1/3.
CC       {ECO:0000255|HAMAP-Rule:MF_00393}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00393}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00393}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_00393}.
CC   -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity and
CC       may constitute the binding site for the phosphate moiety of the
CC       glycerol-3-phosphate. {ECO:0000255|HAMAP-Rule:MF_00393}.
CC   -!- SIMILARITY: Belongs to the GPAT/DAPAT family. {ECO:0000255|HAMAP-
CC       Rule:MF_00393}.
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DR   EMBL; FM209186; CAW26038.1; -; Genomic_DNA.
DR   RefSeq; WP_003113856.1; NC_011770.1.
DR   AlphaFoldDB; B7V2U0; -.
DR   PRIDE; B7V2U0; -.
DR   KEGG; pag:PLES_13111; -.
DR   HOGENOM; CLU_015407_0_0_6; -.
DR   OMA; EVIYVPC; -.
DR   UniPathway; UPA00557; UER00612.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004366; F:glycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0102420; F:sn-1-glycerol-3-phosphate C16:0-DCA-CoA acyl transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd07993; LPLAT_DHAPAT-like; 1.
DR   HAMAP; MF_00393; Glyc3P_acyltrans; 1.
DR   InterPro; IPR022284; GPAT/DHAPAT.
DR   InterPro; IPR041728; GPAT/DHAPAT_LPLAT.
DR   InterPro; IPR045520; GPAT_C.
DR   InterPro; IPR028354; GPAT_PlsB.
DR   InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR   PANTHER; PTHR12563; PTHR12563; 1.
DR   Pfam; PF01553; Acyltransferase; 1.
DR   Pfam; PF19277; GPAT_C; 1.
DR   PIRSF; PIRSF500064; GPAT; 1.
DR   PIRSF; PIRSF000437; GPAT_DHAPAT; 1.
DR   SMART; SM00563; PlsC; 1.
DR   TIGRFAMs; TIGR03703; plsB; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Cell inner membrane; Cell membrane; Lipid biosynthesis;
KW   Lipid metabolism; Membrane; Phospholipid biosynthesis;
KW   Phospholipid metabolism; Transferase.
FT   CHAIN           1..834
FT                   /note="Glycerol-3-phosphate acyltransferase"
FT                   /id="PRO_1000123087"
FT   MOTIF           309..314
FT                   /note="HXXXXD motif"
SQ   SEQUENCE   834 AA;  94816 MW;  C668FB7242B3681D CRC64;
     MPRYPFRRFG FGALRRLLYL WVRSETINQS AFTLKIDRSK PVLYVLQQPS VSDLAVVDTE
     CRKAGLPRPV MPVAVGDAIE PAAFFYLTPE PDWLGRQDKR GASPTLVRML AAVGQNGLDD
     AQIIPVSVFW GQSPDSESSP WKLLFADNWA VTGRLRKLAR ILILGRKTRV QFSAPIHLRE
     LVEQGKGHER TLRMVNRILR VHFRNLKTAV IGPDLSHRRN LVKGLLRAPL VRQAISEECE
     SERISQEKAE GIALRYANEI ASDFSYPVIR FLEVILSWFW NKLYEGVKVN HIERVQDVAQ
     GNEIVYVPCH RSHIDYLLLS YLLFRNGLTP PHIAAGINLN MPVIGSILRR GGAFFMRRSF
     KGNQLYTAVF NEYLHTLFSR GFSTEYFVEG GRSRTGRMLH PRTGMLAITL RSFLRDSRRP
     IVFVPVYIGY ERVLEGRTYL GELRGATKKK ESIFDLFKVV GALKQRFGQV WVNFGEPIHL
     DQFLDRHQPD WQDQDLGPEY RPDWLPQTTN LLAKDVARHL NDAAAINPVN LVALALLSTS
     RQALDESALA RILDLYLALL RKVPYSPSAT LPDGDGQALI EYVKSMNLLA EQKDALGRIL
     YLDEQNAVLA TYYRNNVLHV FALPALIASF FQSNSRISRE QLLRFARALY PYLQAELFIR
     WSLDELDAVI DQWLAALVEQ DLLRQENDTF IRPAPSSRQY VLLILLARSV TQTLQRFYMA
     IALLLNAGQN ALTAEELENL CTVMAQRLSI LHGLNAPEFF DKSLFRHFIQ TLLDLRVLRK
     DEAGKLSYHE LLGELAEGAA KRVLPAEIRL SIRQVALERP AEEAAAESND AAAN