ID   PLSB_PHOLL              Reviewed;         818 AA.
AC   Q7MZB7;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 112.
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=plu4376;
OS   Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 /
OS   TT01).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Photorhabdus.
OX   NCBI_TaxID=243265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15139 / CIP 105565 / TT01;
RX   PubMed=14528314; DOI=10.1038/nbt886;
RA   Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA   Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA   Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C.,
RA   Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M.,
RA   Glaser P., Boemare N., Danchin A., Kunst F.;
RT   "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT   luminescens.";
RL   Nat. Biotechnol. 21:1307-1313(2003).
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; BX571873; CAE16748.1; -; Genomic_DNA.
DR   RefSeq; WP_011148466.1; NC_005126.1.
DR   AlphaFoldDB; Q7MZB7; -.
DR   SMR; Q7MZB7; -.
DR   STRING; 243265.plu4376; -.
DR   PRIDE; Q7MZB7; -.
DR   EnsemblBacteria; CAE16748; CAE16748; plu4376.
DR   GeneID; 24169177; -.
DR   KEGG; plu:plu4376; -.
DR   eggNOG; COG2937; Bacteria.
DR   HOGENOM; CLU_015407_0_0_6; -.
DR   OMA; EVIYVPC; -.
DR   OrthoDB; 580383at2; -.
DR   BioCyc; PLUM243265:PLU_RS21610-MON; -.
DR   UniPathway; UPA00557; UER00612.
DR   Proteomes; UP000002514; 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..818
FT                   /note="Glycerol-3-phosphate acyltransferase"
FT                   /id="PRO_0000195227"
FT   MOTIF           305..310
FT                   /note="HXXXXD motif"
SQ   SEQUENCE   818 AA;  93638 MW;  DCE3FD98858A0E62 CRC64;
     MSSWRKIYYK LLNLPLKILV KSKLIPTDPI TELRLDTTRP ILYVLPYHSK ADLLALRQQC
     LEQDLPDPLN LLEIGDTELP SYVFIDNGPR VFRYCAPKQE SVKIFHAYLD LHRNNPNLDI
     QLLPVSVMFG RSPGREGQNA PHLRLLNGIQ KFFAILWLGR DSFVRFSNTV SLRYMATEHG
     TDKTIAHKLA RVARMHYSRQ RLAAVGPRLP VRQELFNKLL ASKAIEKAVS DEARTKKISH
     EKARQNAINM MEEIAANFSY ETVRLSGRVL GWTWNRLYQG INVHNAERIR RLAQDGHELV
     YAPCHRSHMD YLLLSYVLYH QGLVPPHIAA GINLNFWPAG PIFRRLGAFF IRRTFKGNKL
     YATIFREYLG ELFARGYSVE YFMEGGRSRT GRLLDPKTGT LSMTLQALLR GESRPITIIP
     IYIGYEHVME VATYAKELRG ATKEKEGFFQ MIRGLRKLRN LGQGYVNFGE PIPLIQYLNN
     HVPSWRDSID PIEFHRPEWF NPTVNQLSEK IMVNINNTAA ANAINLCSTA LLASRQRALT
     REQLLEQLDC YIQLMRNAPY ATDVTVPKKT AEELLEHALQ MDKFEVDKDS MGDIIILPRD
     RAVLMTYYRN NIQHLLVLPS LIACIVIHHR RISREALLSQ VAIIYPLLKA ELFMRYSKTE
     LPEVVNTLIN ELTRQCLICN KEHGMLVLNP ARIRPLQLLA AGIRETLQRY AITLSLLNAN
     PVISRGVLEK ESRMLAQRLS VLHGINAPEF FDKAVFTTSV NTLREEGYIS DSGNAITANT
     QELYQVLGEL MSPEIRLTIE SVSLPPEHND TEESAREG