ID   PLSB_PROMH              Reviewed;         827 AA.
AC   B4EYR5;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 84.
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=PMI2751;
OS   Proteus mirabilis (strain HI4320).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Proteus.
OX   NCBI_TaxID=529507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HI4320;
RX   PubMed=18375554; DOI=10.1128/jb.01981-07;
RA   Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S.,
RA   Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T.,
RA   Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA   Rabbinowitsch E., Walker D., Whithead S., Thomson N.R., Rather P.N.,
RA   Parkhill J., Mobley H.L.T.;
RT   "Complete genome sequence of uropathogenic Proteus mirabilis, a master of
RT   both adherence and motility.";
RL   J. Bacteriol. 190:4027-4037(2008).
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; AM942759; CAR45420.1; -; Genomic_DNA.
DR   RefSeq; WP_012368492.1; NC_010554.1.
DR   AlphaFoldDB; B4EYR5; -.
DR   STRING; 529507.PMI2751; -.
DR   PRIDE; B4EYR5; -.
DR   EnsemblBacteria; CAR45420; CAR45420; PMI2751.
DR   GeneID; 6802057; -.
DR   KEGG; pmr:PMI2751; -.
DR   PATRIC; fig|529507.6.peg.2680; -.
DR   eggNOG; COG2937; Bacteria.
DR   HOGENOM; CLU_015407_0_0_6; -.
DR   OMA; EVIYVPC; -.
DR   UniPathway; UPA00557; UER00612.
DR   Proteomes; UP000008319; 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..827
FT                   /note="Glycerol-3-phosphate acyltransferase"
FT                   /id="PRO_1000123086"
FT   MOTIF           307..312
FT                   /note="HXXXXD motif"
SQ   SEQUENCE   827 AA;  94030 MW;  33074CE189BD8200 CRC64;
     MSAWRKLYYN TLNLPLKLLV KSKRVPTDPI TELGLDTSRS FLYVLPYHSK ADLLTLRQQC
     LSLGLPDPLQ PIEINGTKLP AYVFIDDGPR VFRYYSPDPR KDSVKTFHAY LDAHRNNPHL
     DIEMLPASVM FGRSPGREGH NGVPHLRLLN GIQKFIAILW LGRDSFVRFS PTVSMRQMAN
     EHGTDTSIAR KLARVARIHF SRQRLAAVGP KLPARQDLFN KLLASKAIEK AIEDEAKAKK
     ITLDKARKNA TDIMEEIAAN FSYEAVRMTD RVLSWTWNKL YQGINVFNAE RVRQLAQDGH
     EIVYVPCHRS HMDYLLLSYV LYHQGLVPPH IAAGINLNFW PAGPIFRHLG AFFIRRTFKG
     NKLYSTIFRE YLGELFSRGY SIEYFVEGGR SRTGRLLDPK TGTLSMTVQA MLRGETRPIS
     IVPIYIGYEH VMEVATYAKE LRGATKEKEG FMQMIRGLRK LRNLGQGYVN FGEPISLSQY
     LNQAVPDWRD DIDPIEPQRP SWLNPAVSAL ADNIMVNINN AASINAINLV STALLASRQR
     ALTKEQLLEQ IDCYLQLLRN VPYSSDMVVP DKSSETLLAH ALQTDKFQVE QDSLGDIIIL
     PRESAVLMTY YRNNTIHLMV TPSLIASIVL HHERIHRDDL MKQVELIFPL IKAELFIRYE
     KEELPDVVNT LISELCRQRL ICCADDGILR INPARIRPLQ LLAASVRETL QRYGITLSLL
     NFAPEISRAL LERESRILAQ RLSVLHGINA PEFFDKAVFS TLVSTLREEG YLKDNEDILK
     ADASALYQVI AKLMSPEIRL TIESVGVTED NNSAQAIEEN PESNMDK