ID   PLSB_MYCLE              Reviewed;         775 AA.
AC   Q9X7B0;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 115.
DE   RecName: Full=Glycerol-3-phosphate acyltransferase;
DE            Short=GPAT;
DE            EC=2.3.1.15;
GN   Name=plsB; OrderedLocusNames=ML1246; ORFNames=MLCB1610.07;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
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   -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC       diacylglycerol from sn-glycerol 3-phosphate: step 1/3.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
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:0000250}.
CC   -!- SIMILARITY: Belongs to the GPAT/DAPAT family. {ECO:0000305}.
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DR   EMBL; AL049913; CAB43153.1; -; Genomic_DNA.
DR   EMBL; AL583921; CAC31627.1; -; Genomic_DNA.
DR   PIR; T45238; T45238.
DR   RefSeq; NP_301900.1; NC_002677.1.
DR   RefSeq; WP_010908221.1; NC_002677.1.
DR   AlphaFoldDB; Q9X7B0; -.
DR   SMR; Q9X7B0; -.
DR   STRING; 272631.ML1246; -.
DR   EnsemblBacteria; CAC31627; CAC31627; CAC31627.
DR   KEGG; mle:ML1246; -.
DR   PATRIC; fig|272631.5.peg.2298; -.
DR   Leproma; ML1246; -.
DR   eggNOG; COG2937; Bacteria.
DR   HOGENOM; CLU_015407_1_0_11; -.
DR   OMA; EVIYVPC; -.
DR   UniPathway; UPA00557; UER00612.
DR   Proteomes; UP000000806; 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.
PE   3: Inferred from homology;
KW   Acyltransferase; Cell membrane; Lipid biosynthesis; Lipid metabolism;
KW   Membrane; Phospholipid biosynthesis; Phospholipid metabolism;
KW   Reference proteome; Transferase.
FT   CHAIN           1..775
FT                   /note="Glycerol-3-phosphate acyltransferase"
FT                   /id="PRO_0000195224"
FT   MOTIF           268..273
FT                   /note="HXXXXD motif"
SQ   SEQUENCE   775 AA;  87364 MW;  03DD77C778293CDF CRC64;
     MTEPDVEISS VLTGEDTLVL ASMDTPAEIE LVMDWLCQQR NRNPDIKFDV LKLPSRNLAP
     AALTALVEQL ESDEDRSVVP VRVFWMPPAE RSKLAKLAGL LPGRDPYHPN RRQQRHILKT
     DARRALVIAG DSAKVSELRQ YWRDTTVGEN ECDFAQFVTR RAILAMERAE SRILGPQYKS
     PRLVKPEILA STRFRAGLEK ISGATVEEAG KMLDELATGW SRASVDLVSV LGRMLSRGFE
     PEIDYDEYQV AAMRAALEAH PAVLLFSHRS YIDGAVVPVA MQENRLPPVH VFAGINLSFG
     LMGPLLRRSG VIFIRRNIGD NPLYKYVLRE YVGYIVEKRF NLSWSIEGTR SRTGKMLPPK
     LGLLTYVADA YLDGRSEDIL LQPVSISFDQ LHETAEYAAY ARGGEKTPEG VAWLYSFIKA
     QGERNYGKIY VRFPEAVSMR QYLGAPHGAL VQDQDAKRLA LQKMSFEVAW RILCATPVTA
     TALVSALLLT TRGVALTLDQ LHHTLQESLD YLERKQTPVS KSALRLRSRE GVRAAVDALS
     SGHPITRVDS GREPVWYITP GNEHAAAFYR NSVIHAFLET SIVELALAHA RHVEGDRMKV
     FWAQAMRLRD LLKFDFYFAD SAAFRANIAE EIAWHQNWED RVSGDGDDID AMLLTKRPLI
     SDAMLRVFFE AYDIVADVLR DAPADVGQKE LTELALGVGR QYVAQGRVRS GESVSTLLFA
     TAYQVVVDQN LIAPAPDLAE RRMVFRRELR DIRRDFDYVE QIARSRFIVR EFKSR