ID   PLSB_SHESW              Reviewed;         807 AA.
AC   A1RE94;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 80.
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=Sputw3181_0136;
OS   Shewanella sp. (strain W3-18-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=351745;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W3-18-1;
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   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Lykidis A., Tiedje J., Richardson P.;
RT   "Complete sequence of Shewanella sp. W3-18-1.";
RL   Submitted (DEC-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; CP000503; ABM22989.1; -; Genomic_DNA.
DR   RefSeq; WP_011787556.1; NC_008750.1.
DR   AlphaFoldDB; A1RE94; -.
DR   SMR; A1RE94; -.
DR   KEGG; shw:Sputw3181_0136; -.
DR   HOGENOM; CLU_015407_0_0_6; -.
DR   OMA; EVIYVPC; -.
DR   UniPathway; UPA00557; UER00612.
DR   Proteomes; UP000002597; 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; Transferase.
FT   CHAIN           1..807
FT                   /note="Glycerol-3-phosphate acyltransferase"
FT                   /id="PRO_1000049463"
FT   MOTIF           308..313
FT                   /note="HXXXXD motif"
SQ   SEQUENCE   807 AA;  91375 MW;  B2329DB2B660F8C1 CRC64;
     MPKQDSLWLK SLRWIQKHLV HTIVVPQDPF ADLNLDTSRP LAYVMKTESL SDIAALSEVT
     EKLGLPSPYE PLVVNGVVAP RVVCLQGRKP LFGERAGNEP FLECFMRLLA VHKERPELDI
     QLVPVSLYWG RTPGKEDDTM KAAVLERENP TWLRKCFMIL FLGRHNFVQF SNAVSLRYMA
     DEHGTDMGIA HKLARVARVH FRRQRKVMTG PLLPNRQALF DSLLKSESLR KAIQEEAVSK
     KISETQSRET AIEYLDEIAA NYSDSLVRIA ERFLTWLWNK LYSGINIKGA EHIRQLHHDG
     HEIVYVPCHR SHMDYLLLSY ILYYQGMVPP HIAAGINLNF WPAGPLFRRG GAFFIRRSFN
     GNKLYTAVFR EYLDQLFAKG YSVEYFSEGG RSRTGRLLAP KTGMIAMTMN SVLRGIERPV
     TLVPVYLGYD HVMEVATYHK ELSGKKKQKE SVWQVFGAIR KLGNFGQGYV NFGEPITLQT
     FLNEMAPNWR AELADDPEQK PTWLTPAVNV LANRVMTRIN DAAAASSVTL TSLALLASEQ
     NALERCLLER QLDLYLTLLK RVPYTSFTSV AEGDGKHLVQ QGIDLNKFSV SSDPLGEIVS
     IDANQAISMT YYRNNIIHLF IIPSLIASCL THNEQSQRQQ IVAIVNDFYP LLKAELFMGI
     KDIPSYVNQV LDLFIEQGLI TESDNLSVVT EHSSQLVLLS GSVSETLQRY AIIFNLLAHR
     PKMERSELES ESHLLAQRLG ALHGITAPEF YDKKLYGTLS VKLKELGYLS DKDDKSDVKR
     IRDQANSLLR ASVRQTIVAS VTAEHIS