ID   PLSB_PECAS              Reviewed;         825 AA.
AC   Q6D9I7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 91.
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=ECA0628;
OS   Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS   carotovora subsp. atroseptica).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=218491;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCRI 1043 / ATCC BAA-672;
RX   PubMed=15263089; DOI=10.1073/pnas.0402424101;
RA   Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J.,
RA   Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K.,
RA   Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J.,
RA   Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Norbertczak H.,
RA   Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S.,
RA   Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.;
RT   "Genome sequence of the enterobacterial phytopathogen Erwinia carotovora
RT   subsp. atroseptica and characterization of virulence factors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004).
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; BX950851; CAG73543.1; -; Genomic_DNA.
DR   RefSeq; WP_011092246.1; NC_004547.2.
DR   AlphaFoldDB; Q6D9I7; -.
DR   SMR; Q6D9I7; -.
DR   STRING; 218491.ECA0628; -.
DR   EnsemblBacteria; CAG73543; CAG73543; ECA0628.
DR   GeneID; 57207377; -.
DR   KEGG; eca:ECA0628; -.
DR   PATRIC; fig|218491.5.peg.623; -.
DR   eggNOG; COG2937; Bacteria.
DR   HOGENOM; CLU_015407_0_0_6; -.
DR   OMA; EVIYVPC; -.
DR   OrthoDB; 580383at2; -.
DR   UniPathway; UPA00557; UER00612.
DR   Proteomes; UP000007966; 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..825
FT                   /note="Glycerol-3-phosphate acyltransferase"
FT                   /id="PRO_1000049432"
FT   REGION          802..825
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           306..311
FT                   /note="HXXXXD motif"
SQ   SEQUENCE   825 AA;  93499 MW;  4CD1B8F2E4FF8DFE CRC64;
     MSGWRKIYYK LLNLPLKLLV KSKVIPADPV VELGLDPSRP ILYVLPYNSQ ADLLTLRAKC
     LALGLPDPSQ SFEFNGVELP SHVFINDGPR VFRYYVPKQK SVKLFHDYLD LHRANPDLDV
     QMVPVSVMFG RSPGREGHTQ AAPHLRLLNG IEKFFAVLWL GRDSFVRFSS PVSLRYMATE
     HGTDKTIAHK LARVARMHFS RQRLAAVGPR LPVRQELFNK LLDSKAIKKA VDDEARSKKI
     SHEKAQQNAI ALMEEIAADF SYEAVRLSDR VLSWTWNRLY QGINVHNAER VRQLAQDGHG
     IVYVPCHRSH MDYLLLSYVL YHQGLVPPHI AAGINLNFWP AGPIFRRLGA FFIRRTFKGN
     KLYSTIFREY LGELFARGYS VEYFMEGGRS RTGRLLDPKT GTLAMTIQAM LRGGTRPITL
     VPIYVGYEHV MEVGTYAKEL RGAVKEKEGF MQMVRGLRKL RNLGQGYVNF GEPLPLTTYL
     NQHVPQWRDA IDPIEAQRPS WLTPTVQDIS MDIMVRINNS AAANAMNLCS TALLASRQRS
     LTREQMHEQL DCYLQLLRQV PYHKDITAPK KTADELLEHA LGMNKFEVEK DSIGDIIILP
     REQAVLMTYY RNNIQHLLIL PSLIASIVIH HRRITLAEVV RQITLIYPLL QAELFLHYSN
     EQLPRVLETL ANELTRQELL CSRDGQLAIN PPRIRTLQLL SAGVRETLQR YAITLSLLCA
     NPEINRGTLE KESRNMAQRL SVLHGINAPE FFDKAVFSTL VATLRTEGYI TDSAEAAQGD
     IVTIYNILGD LITPEVRLTI ESASSSTEME ASTSSSQTAE ETTQG