ID   PLSB_SHESH              Reviewed;         807 AA.
AC   A8FPP1;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-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=Ssed_0201;
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) 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; CP000821; ABV34814.1; -; Genomic_DNA.
DR   RefSeq; WP_012004340.1; NC_009831.1.
DR   AlphaFoldDB; A8FPP1; -.
DR   SMR; A8FPP1; -.
DR   STRING; 425104.Ssed_0201; -.
DR   EnsemblBacteria; ABV34814; ABV34814; Ssed_0201.
DR   KEGG; sse:Ssed_0201; -.
DR   eggNOG; COG2937; Bacteria.
DR   HOGENOM; CLU_015407_0_0_6; -.
DR   OMA; EVIYVPC; -.
DR   OrthoDB; 580383at2; -.
DR   UniPathway; UPA00557; UER00612.
DR   Proteomes; UP000002015; 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_1000080294"
FT   MOTIF           308..313
FT                   /note="HXXXXD motif"
SQ   SEQUENCE   807 AA;  91667 MW;  6DB8A335BE6119B1 CRC64;
     MSKQDSLWFK SLRWLQNKLV HTIVVPHEPF KDLNLDPDKP LAYVMKTESV SDIAALSEIT
     ADLGLPSPYQ PLEVGGESAP RVVCLEGAKP LMGKRESNHF FLNSFMSLLK IHKERPELDI
     QLVPVSLYWG RTPGKEDDTM KAAVLERENP TWLRKCLMIL FLGRHNFVQF SSAVSLRYMA
     DEHGTDKRIA QKLARVARVH FSRQRKVMTG PVLPKRQALF HALINSETLK KAIQEEAASK
     KITEVEARAK AMEYLDEIAA DYSDSLVRIA ERFLTWLWNK LYKGINIKGA EEVRRLHHDG
     HEIIYVPCHR SHMDYLLLSY ILYYQGMVPP HIAAGINLNF WPAGPMFRRG GAFFIRRSFR
     GNKLYTTVFR EYLDQLFTKG YSVEYFTEGG RSRTGRLLAP KTGMLAMTLN SVLRGMKRPV
     TLVPVYLGYD HVMEVATYHK ELSGKKKKKE SVWQVFGALR KLGNFGQGYV NFGKPITLHS
     FLNEQKPDWK EEIAKEPEQR PKWLTPMVNT LANQVMTNIN DAAAVSSVTL TSLVLLASEQ
     NALERSQLEK QLDLYLKLLK DLPYTSYTSV VEGDGKSLVQ QGLELKKIKL DSDPLGDIIS
     IDESIAVAMT YYRNNIIHLM VIPSLVASCL TQHEHISRDE IIDIIKDFYP LLQAELFMGV
     EDTDKLVGQI LDLFIAQGLV TEDDGFSIIE TEVNQLLLLA GTVGETLQRY AIIFNLLAVC
     PKMERSDLER ESHKLAQRLG ALHGITAPEF YDKKLYGALS VKLKELGYLS DNGNKVDVQR
     IRERANGLLR SSVRQTIVDS VTAEHKD