CRLS_MYCTU
ID CRLS_MYCTU Reviewed; 209 AA.
AC P9WPG5; L0T801; P63753; Q50611;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 37.
DE RecName: Full=Putative cardiolipin synthase {ECO:0000303|PubMed:10889206};
DE EC=2.7.8.41 {ECO:0000303|PubMed:10889206};
GN Name=pgsA2 {ECO:0000303|PubMed:10889206, ECO:0000312|EMBL:CCP44588.1};
GN OrderedLocusNames=Rv1822; ORFNames=MTCY1A11.21c;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, 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: May catalyze the biosynthesis of cardiolipin from
CC phosphatidylglycerol (PG) and CDP-diacylglycerol. May also catalyze the
CC synthesis of phosphatidylinositol. {ECO:0000303|PubMed:10889206}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + a CDP-1,2-
CC diacyl-sn-glycerol = a cardiolipin + CMP + H(+);
CC Xref=Rhea:RHEA:32931, ChEBI:CHEBI:15378, ChEBI:CHEBI:58332,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:62237, ChEBI:CHEBI:64716; EC=2.7.8.41;
CC Evidence={ECO:0000303|PubMed:10889206};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-CDP + myo-inositol = 1,2-
CC dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol) + CMP + H(+);
CC Xref=Rhea:RHEA:40411, ChEBI:CHEBI:15378, ChEBI:CHEBI:17268,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:72835, ChEBI:CHEBI:77190;
CC Evidence={ECO:0000303|PubMed:10889206};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40412;
CC Evidence={ECO:0000303|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; CCP44588.1; -; Genomic_DNA.
DR PIR; G70720; G70720.
DR RefSeq; NP_216338.1; NC_000962.3.
DR RefSeq; WP_003409227.1; NZ_NVQJ01000013.1.
DR AlphaFoldDB; P9WPG5; -.
DR SMR; P9WPG5; -.
DR STRING; 83332.Rv1822; -.
DR SwissLipids; SLP:000001157; -.
DR PaxDb; P9WPG5; -.
DR DNASU; 885126; -.
DR GeneID; 45425796; -.
DR GeneID; 885126; -.
DR KEGG; mtu:Rv1822; -.
DR TubercuList; Rv1822; -.
DR eggNOG; COG0558; Bacteria.
DR OMA; GTTLYWW; -.
DR PhylomeDB; P9WPG5; -.
DR UniPathway; UPA00085; -.
DR Proteomes; UP000001584; 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; ISS:UniProtKB.
DR GO; GO:0043337; F:CDP-diacylglycerol-phosphatidylglycerol phosphatidyltransferase activity; IEA:RHEA.
DR GO; GO:0046474; P:glycerophospholipid biosynthetic process; IBA:GO_Central.
DR GO; GO:0008654; P:phospholipid biosynthetic process; ISS: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 PROSITE; PS00379; CDP_ALCOHOL_P_TRANSF; 1.
PE 1: Evidence at protein level;
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="Putative cardiolipin synthase"
FT /id="PRO_0000056779"
FT TRANSMEM 27..47
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 209 AA; 22911 MW; 36079C2FD2D6F91B CRC64;
MEPVLTQNRV LTVPNMLSVI RLALIPAFVY VVLSAHANGW GVAILVFSGV SDWADGKIAR
LLNQSSRLGA LLDPAVDRLY MVTVPIVFGL SGIVPWWFVL TLLTRDALLA GTLPLLWSRG
LSALPVTYVG KAATFGFMVG FPTILLGQCD PLWSHVLLAC GWAFLIWGMY AYLWAFVLYA
VQMTMVVRQM PKLKGRAHRP AAQNAGERG
