ID   PLSB_SHEFN              Reviewed;         807 AA.
AC   Q089E1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 82.
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=Sfri_0261;
OS   Shewanella frigidimarina (strain NCIMB 400).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=318167;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCIMB 400;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Fredrickson J.K., Kolker E., McCuel L.A., DiChristina T., Nealson K.H.,
RA   Newman D., Tiedje J.M., Zhou J., Romine M.F., Culley D.E., Serres M.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT   "Complete sequence of Shewanella frigidimarina NCIMB 400.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000447; ABI70124.1; -; Genomic_DNA.
DR   RefSeq; WP_011635751.1; NC_008345.1.
DR   AlphaFoldDB; Q089E1; -.
DR   SMR; Q089E1; -.
DR   STRING; 318167.Sfri_0261; -.
DR   EnsemblBacteria; ABI70124; ABI70124; Sfri_0261.
DR   KEGG; sfr:Sfri_0261; -.
DR   eggNOG; COG2937; Bacteria.
DR   HOGENOM; CLU_015407_0_0_6; -.
DR   OMA; EVIYVPC; -.
DR   OrthoDB; 580383at2; -.
DR   UniPathway; UPA00557; UER00612.
DR   Proteomes; UP000000684; Chromosome.
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_1000049457"
FT   MOTIF           308..313
FT                   /note="HXXXXD motif"
SQ   SEQUENCE   807 AA;  91990 MW;  F3AAA95E1FBB6CED CRC64;
     MSKPDSIFLR ALRWIQKWMV QTIVVPHDPF DDLNIDPTKP LVYLMKTESI SDIAALSEIT
     EGFGLPSPYE PLQLDGLTVP RVVCLEGRKP LFGKRESGDK FLNYFTSLLS LHSESPELDI
     QLVPVCLYWG RTPGKEEDSM KAAVFERENP TWLRKWLMIL FLGRHNFVQF SNALSLRHMA
     DEHGTDKRIA HKLTRVARVH FRRQRKVMTG PQLPNRQALF ASLLKSESIK KAIEEESANK
     KVTVEKARET AIEYLDEIAA DYSDSLVRIA ERFLTWLWNK LYSGINIKGA EQVRQLHHDG
     HEIVYVPCHR SHMDYLLLSY ILYYQGMVPP HIAAGINLNF WPAGPMFRRG GAFFIRRSFN
     GNKLYTAVFR EYLDQLFAKG YAVEYFTEGG RSRTGRLLAP KTGMLAMTIN SVLRGIERPV
     TLVPVYLGYD HVMEVATYHK ELSGKKKKKE SVWQVFGAIR KLGNFGQGYV NFGEPINLQQ
     FLNQQAPEWR DELAKDPDQK PSWFTPSVNL LANRVMTNIN GAAAASSVTL TSLVLLASEQ
     NALERSQLER QLDLYLALLK TVPYTEYASV AEGNGKSIVD HCLSLNKFVS TKDLIGEIIS
     VDEKIAITMS YYRNNIIHLM ALPSLIASCL VHYDVCDRQR IHAIVMDFYP LLKAELFMSI
     DDVPKHVDCI LDFMVEQGLL TGSDQFEITP RHITQVLLLA ETISETLQRY AIIFNLLAIK
     PDLERSELER DSHLLAQRLG ALHGITAPEF YDKKLYNTLS VKLKELGYLC SDEHRAEVIR
     IRDNANKLLS SLVRQTIVDS VEAEHGQ