ID   PGSA_MYCTO              Reviewed;         209 AA.
AC   P9WPG2; L0TAI5; O33288; Q7D6N5;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 36.
DE   RecName: Full=Probable phosphatidylglycerophosphate synthase {ECO:0000250|UniProtKB:P9WPG3};
DE            Short=PGP synthase {ECO:0000250|UniProtKB:P9WPG3};
DE            Short=PGPS {ECO:0000250|UniProtKB:P9WPG3};
DE            EC=2.7.8.5 {ECO:0000250|UniProtKB:P9WPG3};
DE   AltName: Full=CDP-diacylglycerol--glycerol-3-phosphate phosphatidyltransferase;
GN   Name=pgsA-2 {ECO:0000312|EMBL:AAK47137.1}; OrderedLocusNames=MT2817;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: Probably catalyzes the synthesis of
CC       phosphatidylglycerophosphate by transferring a phosphatidyl group from
CC       CDP-diacylglycerol to glycerol 3-phosphate.
CC       {ECO:0000250|UniProtKB:P9WPG3}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a CDP-1,2-diacyl-sn-glycerol + sn-glycerol 3-phosphate = 1,2-
CC         diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate) + CMP +
CC         H(+); Xref=Rhea:RHEA:12593, ChEBI:CHEBI:15378, ChEBI:CHEBI:57597,
CC         ChEBI:CHEBI:58332, ChEBI:CHEBI:60110, ChEBI:CHEBI:60377; EC=2.7.8.5;
CC         Evidence={ECO:0000250|UniProtKB:P9WPG3};
CC   -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC       {ECO:0000250|UniProtKB:P9WPG3}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I
CC       family. {ECO:0000305}.
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DR   EMBL; AE000516; AAK47137.1; -; Genomic_DNA.
DR   PIR; A70879; A70879.
DR   RefSeq; WP_003414035.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WPG2; -.
DR   SMR; P9WPG2; -.
DR   EnsemblBacteria; AAK47137; AAK47137; MT2817.
DR   KEGG; mtc:MT2817; -.
DR   PATRIC; fig|83331.31.peg.3037; -.
DR   HOGENOM; CLU_051314_2_0_11; -.
DR   UniPathway; UPA00085; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008444; F:CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.120.1760; -; 1.
DR   InterPro; IPR000462; CDP-OH_P_trans.
DR   InterPro; IPR043130; CDP-OH_PTrfase_TM_dom.
DR   InterPro; IPR004570; Phosphatidylglycerol_P_synth.
DR   Pfam; PF01066; CDP-OH_P_transf; 1.
DR   PIRSF; PIRSF000847; Phos_ph_gly_syn; 1.
DR   TIGRFAMs; TIGR00560; pgsA; 1.
DR   PROSITE; PS00379; CDP_ALCOHOL_P_TRANSF; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Lipid biosynthesis; Lipid metabolism; Membrane;
KW   Phospholipid biosynthesis; Phospholipid metabolism; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..209
FT                   /note="Probable phosphatidylglycerophosphate synthase"
FT                   /id="PRO_0000426957"
FT   TRANSMEM        32..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        105..125
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        147..167
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        171..191
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   209 AA;  22136 MW;  1D71D83D3F36B48A CRC64;
     MSRSTRYSVA VSAQPETGQI AGRARIANLA NILTLLRLVM VPVFLLALFY GGGHHSAARV
     VAWAIFATAC ITDRFDGLLA RNYGMATEFG AFVDPIADKT LIGSALIGLS MLGDLPWWVT
     VLILTRELGV TVLRLAVIRR GVIPASWGGK LKTFVQAVAI GLFVLPLSGP LHVAAVVVMA
     AAILLTVITG VDYVARALRD IGGIRQTAS