ID   PLSB_VIBCH              Reviewed;         811 AA.
AC   Q9KVP8;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Glycerol-3-phosphate acyltransferase;
DE            Short=GPAT;
DE            EC=2.3.1.15;
GN   Name=plsB; OrderedLocusNames=VC_0093;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
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   -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC       diacylglycerol from sn-glycerol 3-phosphate: step 1/3.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Peripheral
CC       membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
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:0000250}.
CC   -!- SIMILARITY: Belongs to the GPAT/DAPAT family. {ECO:0000305}.
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DR   EMBL; AE003852; AAF93271.1; -; Genomic_DNA.
DR   PIR; B82365; B82365.
DR   AlphaFoldDB; Q9KVP8; -.
DR   SMR; Q9KVP8; -.
DR   STRING; 243277.VC_0093; -.
DR   DNASU; 2615770; -.
DR   EnsemblBacteria; AAF93271; AAF93271; VC_0093.
DR   KEGG; vch:VC_0093; -.
DR   eggNOG; COG2937; Bacteria.
DR   HOGENOM; CLU_015407_0_0_6; -.
DR   OMA; EVIYVPC; -.
DR   BioCyc; VCHO:VC0093-MON; -.
DR   UniPathway; UPA00557; UER00612.
DR   Proteomes; UP000000584; Chromosome 1.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0004366; F:glycerol-3-phosphate O-acyltransferase activity; IBA:GO_Central.
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   GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR   GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IBA:GO_Central.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IBA:GO_Central.
DR   GO; GO:0019432; P:triglyceride biosynthetic process; IBA:GO_Central.
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; Reference proteome; Transferase.
FT   CHAIN           1..811
FT                   /note="Glycerol-3-phosphate acyltransferase"
FT                   /id="PRO_0000195235"
FT   MOTIF           309..314
FT                   /note="HXXXXD motif"
SQ   SEQUENCE   811 AA;  90825 MW;  B076969A30BCFC8D CRC64;
     MNSMSSGHLL SRSLLKLPMS VLVKGTAIPS NPIQDLDIDT HKPVIYALPF RSNVDLLTLQ
     THAKEAGLPD PLEPLMLNGK AFQRYVFIAS RPTLLSSDQH VPSDSIALFS ELLTEHKLDS
     ELDVQVIPAT VLWGRKPGKE GQERPYLQAL NGPEKALAVL ASGRDCLVRF SPVVSMRYMA
     DTHGTDASIA HKLARVARIH FSRQKLAASG PNLPQRAQLF ARLMNSPAIE KAIADEAKSK
     QIPLEKARKE AHDILDEIAA DFSYSLVKKG DRILGWLWNR IYQGLNINNA ATVRRLAQDG
     HEIVYVPCHR SHMDYLLLSY VLYHEGMVPP HIAAGINLNF FPAGPIFRRG GAFFIRRSFK
     GAPLYSTIFR EYLAELFAKG YSVEYFSEGG RSRTGRLLPA KTGMLAMTIQ AMLRGLNRPV
     TLVPVYIGYE HVMEVGTYAK ELRGKRKEKE NAGLVLRTLR KLRNFGQGYV NFGEPIPLNQ
     FLNETVPQWT QDIDPMGESK PQWMTPTVNK LANRMMTHIN DAAAVNAMTL CATALLASRQ
     RALARDNLIK QVDCYLSLLR NVPYSATSTL PSESAEKLVE HAESLDKFVV ETDTMGDIIS
     LDRNQSILMT YYRNNIIHLL ALPSLIAQLL IRQQSVSLEK VQATVAQIYP FLKQELFLRF
     EAEELNDLVL RYVAELARQG LVTVEGKTVT LNQAQTQVLM LLGRIISETL QRYAIALNLL
     VSCPHLGKAE LEEKSQEVAQ RLGRLHGINA PEFFDKGVFA SLFVTLQEQG YLDDQGRCVL
     ETAKPLSRQL YALIYPEVRM TIQESLCQVD A