ID   PLSB_SHESR              Reviewed;         807 AA.
AC   Q0HPW7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 83.
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=Shewmr7_3861;
OS   Shewanella sp. (strain MR-7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=60481;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR-7;
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   Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Nealson K.,
RA   Konstantinidis K., Klappenbach J., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Shewanella sp. MR-7.";
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000444; ABI44838.1; -; Genomic_DNA.
DR   RefSeq; WP_011627579.1; NC_008322.1.
DR   AlphaFoldDB; Q0HPW7; -.
DR   SMR; Q0HPW7; -.
DR   EnsemblBacteria; ABI44838; ABI44838; Shewmr7_3861.
DR   KEGG; shm:Shewmr7_3861; -.
DR   HOGENOM; CLU_015407_0_0_6; -.
DR   OMA; EVIYVPC; -.
DR   OrthoDB; 580383at2; -.
DR   UniPathway; UPA00557; UER00612.
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_1000049462"
FT   MOTIF           308..313
FT                   /note="HXXXXD motif"
SQ   SEQUENCE   807 AA;  91348 MW;  FFC469A8ABE7F1A4 CRC64;
     MPKQDSLWLK SLRWIQKHLV HTIVVPQDPF ADLNLDASRP LAYVMKTESL SDIAALSEIT
     TKLGLPSPYE PLVVNGVVAP RVVCLEGRKP LFGERASNEP FLECFMRLLA VHKEKPELDI
     QLVPVSLYWG RTPGKEDDTM KAAVLERENP TWLRKCLMIL FLGRHNFVQF SNAVSLRYMA
     DEHGTDMGIA HKLARVARVH FRRQRKVMTG PVLPNRQALF HSLLKSESLR KAIQEEAASK
     KISETQARET AIEYLDEIAA NYSDSLVRIA ERFLTWLWNK LYSGINIKGA EQIRQLHHDG
     HEIVYVPCHR SHMDYLLLSY ILYYQGMVPP HIAAGINLNF WPAGPLFRRG GAFFIRRSFN
     GNKLYTAVFR EYLDQLFAKG YSVEYFSEGG RSRTGRLLAP KTGMIAMTIN SVLRGIERPV
     TLVPVYLGYD HVMEVATYHK ELSGKKKQKE SVWQVFGAIR KLGNFGQGYV NFGEPITLQN
     FLNETAPNWR TEVADDPEQK PTWLTPAVNV LANRVMTRIN DAAAASSITL TSLVLLASEQ
     NALERCLLER QLDLYLTLLK RVPYTSFTSV AEGDGKHLVQ QGLELNKFSI SADPLGEIVS
     IDANQAITMT YYRNNIIHLF IIPSLIASCL TNNKQISRAS ILGIVNDFYP LLKAELFMGI
     KDLPSYVNQV LDLFIEQGLV QESDTLSVVT ERTSQMLLLA GSVSETLQRY AIIFNLLAHR
     PKMERSELES ESHLLAQRLG ALHGITAPEF YDKKLYNTLS VKLKELGYFS EKEDKSDVER
     IRDQANSLLR ASVRQTIVAS VTAEHIV