ID   PLSB_ALIF1              Reviewed;         807 AA.
AC   Q5E208;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 89.
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=VF_2443;
OS   Aliivibrio fischeri (strain ATCC 700601 / ES114) (Vibrio fischeri).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=312309;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700601 / ES114;
RX   PubMed=15703294; DOI=10.1073/pnas.0409900102;
RA   Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R.,
RA   Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E.,
RA   Stevens A., Visick K., Whistler C., Greenberg E.P.;
RT   "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with
RT   pathogenic congeners.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005).
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; CP000020; AAW86938.1; -; Genomic_DNA.
DR   RefSeq; WP_011262810.1; NC_006840.2.
DR   RefSeq; YP_205826.1; NC_006840.2.
DR   AlphaFoldDB; Q5E208; -.
DR   SMR; Q5E208; -.
DR   STRING; 312309.VF_2443; -.
DR   EnsemblBacteria; AAW86938; AAW86938; VF_2443.
DR   KEGG; vfi:VF_2443; -.
DR   PATRIC; fig|312309.11.peg.2471; -.
DR   eggNOG; COG2937; Bacteria.
DR   HOGENOM; CLU_015407_0_0_6; -.
DR   OMA; EVIYVPC; -.
DR   OrthoDB; 580383at2; -.
DR   UniPathway; UPA00557; UER00612.
DR   Proteomes; UP000000537; Chromosome I.
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; Reference proteome; Transferase.
FT   CHAIN           1..807
FT                   /note="Glycerol-3-phosphate acyltransferase"
FT                   /id="PRO_1000049469"
FT   MOTIF           305..310
FT                   /note="HXXXXD motif"
SQ   SEQUENCE   807 AA;  91138 MW;  778B5C675DBC262E CRC64;
     MSTGHTIYHS LLKLPLSVMV KSSSIPSNPI EDLKIDLERP IIYALPFRSH VDLLTLQKSA
     LELGLPDPLS PIEIEGVKYP RYVFTSIGPK MFDTDDDLPQ ESLDLFKIVL KHHADNPDAD
     FQLIPTSILW GRKPGKEGTS KPHLMPLNGP QKFVTLIKAG RDSTVRISPV VSLRYMADNH
     GSDEAIAHKL ARVAKIHFSR QKLAASGPNL PNRQALFNRL LKSQAIEKVI LEEAKSRNVD
     VEKVRKEAMG IMEEIATNFS YSLIKNGNRI LKWLWNRLYQ GLNINNASTV RKLAQEGHEI
     VYVPCHRSHM DYLLLSYVLY HEGLVPPHIA AGINLNFFPA GPIFRRGGAF FIRRSFKGNR
     LYSTIFREYL AELFAKGYSV EYFSEGGRSR TGRLLQAKTG MLAMTVQAML RGLNRPVTLV
     PVYIGYEHVM EVTTYAKELR GKRKEKENAG QVLRTLRKLR NFGQGYVNFG EPISLNHYLN
     EHAPNWSESI NPIEPQKPEW MTPVVNGIAN KMMTHINDAA AANALTLCAT ALLAANQRAL
     SKEDLTEQLD CYLQILRNVP YSATATVPSE DADALLEHAI KLDKFVIEKD TLGEIVSLDR
     NQSLLMTYYR NNIIHLFALP SLIAKLVVHH DTITVEQIQD QIKLIYPFLK AELFLHYKEE
     ELTSIVNNHI DELVQQNLIL RDGDTLQLCN ANIRKLHLLA HTISETLQRY AIALTHLQAS
     PDLGKDELEE QSQIMAQRLS RLHGINAPEF FDKGVFCILF NTLKTEGYLD EDGAAVLSKV
     EPLSQDIAHL LTPEIKLTIH AVMTKED