PGSA_MYCTU
ID PGSA_MYCTU Reviewed; 209 AA.
AC P9WPG3; 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 39.
DE RecName: Full=Probable phosphatidylglycerophosphate synthase {ECO:0000303|PubMed:10889206};
DE Short=PGP synthase {ECO:0000303|PubMed:10889206};
DE Short=PGPS {ECO:0000303|PubMed:10889206};
DE EC=2.7.8.5 {ECO:0000305|PubMed:10889206};
DE AltName: Full=CDP-diacylglycerol--glycerol-3-phosphate phosphatidyltransferase;
GN Name=pgsA3 {ECO:0000303|PubMed:10889206, ECO:0000312|EMBL:CCP45545.1};
GN OrderedLocusNames=Rv2746c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP SEQUENCE REVISION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=12368430; DOI=10.1099/00221287-148-10-2967;
RA Camus J.-C., Pryor M.J., Medigue C., Cole S.T.;
RT "Re-annotation of the genome sequence of Mycobacterium tuberculosis
RT H37Rv.";
RL Microbiology 148:2967-2973(2002).
RN [3]
RP FUNCTION, AND PATHWAY.
RC STRAIN=H37Rv;
RX PubMed=10889206; DOI=10.1074/jbc.m004658200;
RA Jackson M., Crick D.C., Brennan P.J.;
RT "Phosphatidylinositol is an essential phospholipid of mycobacteria.";
RL J. Biol. Chem. 275:30092-30099(2000).
CC -!- FUNCTION: Probably catalyzes the synthesis of
CC phosphatidylglycerophosphate by transferring a phosphatidyl group from
CC CDP-diacylglycerol to glycerol 3-phosphate.
CC {ECO:0000305|PubMed:10889206}.
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:0000305|PubMed:10889206};
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC {ECO:0000305|PubMed:10889206}.
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; AL123456; CCP45545.1; -; Genomic_DNA.
DR PIR; A70879; A70879.
DR RefSeq; NP_217262.1; NC_000962.3.
DR RefSeq; WP_003414035.1; NC_000962.3.
DR AlphaFoldDB; P9WPG3; -.
DR SMR; P9WPG3; -.
DR STRING; 83332.Rv2746c; -.
DR PaxDb; P9WPG3; -.
DR DNASU; 888375; -.
DR GeneID; 888375; -.
DR KEGG; mtu:Rv2746c; -.
DR PATRIC; fig|83332.111.peg.3057; -.
DR TubercuList; Rv2746c; -.
DR eggNOG; COG0558; Bacteria.
DR OMA; WSMVYYL; -.
DR PhylomeDB; P9WPG3; -.
DR UniPathway; UPA00085; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008444; F:CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase activity; IDA:UniProtKB.
DR GO; GO:0046474; P:glycerophospholipid biosynthetic process; IMP:MTBBASE.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IDA:UniProtKB.
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; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..209
FT /note="Probable phosphatidylglycerophosphate synthase"
FT /id="PRO_0000393110"
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
