ID   PLSB_VIBC3              Reviewed;         811 AA.
AC   A5F4F5; C3M2F1;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   25-MAY-2022, entry version 81.
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};
GN   OrderedLocusNames=VC0395_A2422, VC395_0087;
OS   Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 /
OS   O395).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=345073;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RA   Heidelberg J.;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX   PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA   Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA   Wang W., Wang J., Qian W., Li D., Wang L.;
RT   "A recalibrated molecular clock and independent origins for the cholera
RT   pandemic clones.";
RL   PLoS ONE 3:E4053-E4053(2008).
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; CP000627; ABQ21912.1; -; Genomic_DNA.
DR   EMBL; CP001235; ACP08115.1; -; Genomic_DNA.
DR   AlphaFoldDB; A5F4F5; -.
DR   SMR; A5F4F5; -.
DR   STRING; 345073.VC395_0087; -.
DR   EnsemblBacteria; ABQ21912; ABQ21912; VC0395_A2422.
DR   KEGG; vco:VC0395_A2422; -.
DR   KEGG; vcr:VC395_0087; -.
DR   PATRIC; fig|345073.21.peg.79; -.
DR   eggNOG; COG2937; Bacteria.
DR   HOGENOM; CLU_015407_0_0_6; -.
DR   OMA; EVIYVPC; -.
DR   UniPathway; UPA00557; UER00612.
DR   Proteomes; UP000000249; Chromosome 2.
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..811
FT                   /note="Glycerol-3-phosphate acyltransferase"
FT                   /id="PRO_1000072228"
FT   MOTIF           308..313
FT                   /note="HXXXXD motif"
SQ   SEQUENCE   811 AA;  90812 MW;  8B10EBBCC374EA67 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 LATRMMTHIN 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