ID   PLSB_MYCBO              Reviewed;         789 AA.
AC   Q7TYH5; A0A1R3Y1A3; X2BKY7;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 104.
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=BQ2027_MB2507C;
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=233413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA   Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA   Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA   Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA   Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA   Robbe-Austerman S., Gordon S.V.;
RT   "Updated reference genome sequence and annotation of Mycobacterium bovis
RT   AF2122/97.";
RL   Genome Announc. 5:E00157-E00157(2017).
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 membrane {ECO:0000255|HAMAP-Rule:MF_00393};
CC       Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_00393};
CC       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; LT708304; SIU01123.1; -; Genomic_DNA.
DR   RefSeq; NP_856154.1; NC_002945.3.
DR   RefSeq; WP_010950725.1; NC_002945.4.
DR   AlphaFoldDB; Q7TYH5; -.
DR   SMR; Q7TYH5; -.
DR   EnsemblBacteria; SIU01123; SIU01123; BQ2027_MB2507C.
DR   PATRIC; fig|233413.5.peg.2759; -.
DR   OMA; EVIYVPC; -.
DR   UniPathway; UPA00557; UER00612.
DR   Proteomes; UP000001419; 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; Transferase.
FT   CHAIN           1..789
FT                   /note="Glycerol-3-phosphate acyltransferase"
FT                   /id="PRO_0000195223"
FT   MOTIF           276..281
FT                   /note="HXXXXD motif"
SQ   SEQUENCE   789 AA;  88341 MW;  85ACA549B9B1CFF1 CRC64;
     MTKPAADASA VLTAEDTLVL ASTATPVEME LIMGWLGQQR ARHPDSKFDI LKLPPRNAPP
     AALTALVEQL EPGFASSPQS GEDRSIVPVR VIWLPPADRS RAGKVAALLP GRDPYHPSQR
     QQRRILRTDP RRARVVAGES AKVSELRQQW RDTTVAEHKR DFAQFVSRRA LLALARAEYR
     ILGPQYKSPR LVKPEMLASA RFRAGLDRIP GATVEDAGKM LDELSTGWSQ VSVDLVSVLG
     RLASRGFDPE FDYDEYQVAA MRAALEAHPA VLLFSHRSYI DGVVVPVAMQ DNRLPPVHMF
     GGINLSFGLM GPLMRRSGMI FIRRNIGNDP LYKYVLKEYV GYVVEKRFNL SWSIEGTRSR
     TGKMLPPKLG LMSYVADAYL DGRSDDILLQ GVSICFDQLH EITEYAAYAR GAEKTPEGLR
     WLYNFIKAQG ERNFGKIYVR FPEAVSMRQY LGAPHGELTQ DPAAKRLALQ KMSFEVAWRI
     LQATPVTATG LVSALLLTTR GTALTLDQLH HTLQDSLDYL ERKQSPVSTS ALRLRSREGV
     RAAADALSNG HPVTRVDSGR EPVWYIAPDD EHAAAFYRSS VIHAFLETSI VELALAHAKH
     AEGDRVAAFW AQAMRLRDLL KFDFYFADST AFRANIAQEM AWHQDWEDHL GVGGNEIDAM
     LYAKRPLMSD AMLRVFFEAY EIVADVLRDA PPDIGPEELT ELALGLGRQF VAQGRVRSSE
     PVSTLLFATA RQVAVDQELI APAADLAERR VAFRRELRNI LRDFDYVEQI ARNQFVAREF
     KARQGRDRI