ID   PLSB_MYCTA              Reviewed;         789 AA.
AC   A5U5H8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   25-MAY-2022, entry version 76.
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=MRA_2507;
OS   Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=419947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25177 / H37Ra;
RX   PubMed=18584054; DOI=10.1371/journal.pone.0002375;
RA   Zheng H., Lu L., Wang B., Pu S., Zhang X., Zhu G., Shi W., Zhang L.,
RA   Wang H., Wang S., Zhao G., Zhang Y.;
RT   "Genetic basis of virulence attenuation revealed by comparative genomic
RT   analysis of Mycobacterium tuberculosis strain H37Ra versus H37Rv.";
RL   PLoS ONE 3:E2375-E2375(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 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; CP000611; ABQ74278.1; -; Genomic_DNA.
DR   RefSeq; WP_003917012.1; NZ_CP016972.1.
DR   AlphaFoldDB; A5U5H8; -.
DR   SMR; A5U5H8; -.
DR   STRING; 419947.MRA_2507; -.
DR   EnsemblBacteria; ABQ74278; ABQ74278; MRA_2507.
DR   KEGG; mra:MRA_2507; -.
DR   eggNOG; COG2937; Bacteria.
DR   HOGENOM; CLU_015407_1_0_11; -.
DR   OMA; EVIYVPC; -.
DR   OrthoDB; 580383at2; -.
DR   UniPathway; UPA00557; UER00612.
DR   Proteomes; UP000001988; 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_1000049439"
FT   MOTIF           275..280
FT                   /note="HXXXXD motif"
SQ   SEQUENCE   789 AA;  88315 MW;  B78D7D8F8296EA22 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 EHAAAFYRNS VIHAFLETSI VELALAHAKH
     AEGDRVAAFW AQAMRLRDLL KFDFYFADST AFRANIAQEM AWHQDWEDHL GVGGNEIDAM
     LYAKRPLMSD AMLRVFFEAY EIVADVLRDA PPDIGPEELT ELALGLGRQF VAQGRVRSSE
     PVSTLLFATA RQVAVDQELI APAADLAERR VAFRRELRNI LRDFDYVEQI ARNQFVACEF
     KARQGRDRI