ID   PLSB_ALISL              Reviewed;         807 AA.
AC   B6ENU1;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   25-MAY-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=VSAL_I2894;
OS   Aliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain
OS   LFI1238)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=316275;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LFI1238;
RX   PubMed=19099551; DOI=10.1186/1471-2164-9-616;
RA   Hjerde E., Lorentzen M.S., Holden M.T., Seeger K., Paulsen S., Bason N.,
RA   Churcher C., Harris D., Norbertczak H., Quail M.A., Sanders S.,
RA   Thurston S., Parkhill J., Willassen N.P., Thomson N.R.;
RT   "The genome sequence of the fish pathogen Aliivibrio salmonicida strain
RT   LFI1238 shows extensive evidence of gene decay.";
RL   BMC Genomics 9:616-616(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; FM178379; CAQ80578.1; -; Genomic_DNA.
DR   RefSeq; WP_012551312.1; NC_011312.1.
DR   AlphaFoldDB; B6ENU1; -.
DR   SMR; B6ENU1; -.
DR   STRING; 316275.VSAL_I2894; -.
DR   EnsemblBacteria; CAQ80578; CAQ80578; VSAL_I2894.
DR   KEGG; vsa:VSAL_I2894; -.
DR   eggNOG; COG2937; Bacteria.
DR   HOGENOM; CLU_015407_0_0_6; -.
DR   OMA; EVIYVPC; -.
DR   OrthoDB; 580383at2; -.
DR   UniPathway; UPA00557; UER00612.
DR   Proteomes; UP000001730; Chromosome 1.
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..807
FT                   /note="Glycerol-3-phosphate acyltransferase"
FT                   /id="PRO_1000123073"
FT   MOTIF           305..310
FT                   /note="HXXXXD motif"
SQ   SEQUENCE   807 AA;  91258 MW;  91EFE90897A1151C CRC64;
     MSTGQTIYHS LLKLPLSVMV KSTPIPSNPI EDLNIDIERP IIYALPFRSH VDLLTLQKSA
     KELGLPDPLS PIEIDGVSYP RYVFTSIGPK MFDTDDDLPQ ESLDLFKIVL KHHADNPDAD
     FQLIPTSILW GRRPGKEGTS RPHLMPLNGP QKFVTLIKAG RDSTVRISPV VSLRYMADNH
     GADDAIAHKL ARVAKIHFSR QKLAASGPNL PNRQALFNRL LKSQAIEKVI LEEARIRNVD
     VEKVRKEAMG IMEEIATNFS YSLIKNGNRI LKWLWNRLYQ GLNINNAATV RKLAQEGHEI
     VYVPCHRSHM DYLLLSYVLY HEGLVPPHIA AGINLNFFPA GPIFRRGGAF FIRRSFKGNR
     LYSTIFREYL AELFAKGYSV EYFSEGGRSR TGRLLQAKTG MLAMTVQAML RGLNRPVTLV
     PVYIGYEHVM EVTTYAKELQ GKRKEKENAG QVLRTLRKLR NFGQGYVNFG EPISLNHYLN
     EHAPNWSESI NPIEPQKPEW MSPVVNGIAN KMMTHINDAV AANALTLCAT ALLAARQRAL
     SKEDLTEQLD CYLQLLRNIP YSNTATVPTQ DAEALLEHAI ALDKFVIEKD TLGEIISLDR
     NQSILMTYYR NNIIHLFALP SLIAKLVVQY RSISIDNVQA QIQQIYPFLK AELFLHYDES
     ELNDVVSQHI DELVRQKLIE RENDVLQLNA TNILKVHLLA HTISETLQRY AIALTHLQAS
     PKLGKNDLEE QSQIMAQRLS RLHGINAPEF FDKGVFGILF NTLKAEGYLN SDGVAVISKV
     EPFSRDMSRL LNPEIKLTIQ AVMTKED