CMTR_MYCTU
ID CMTR_MYCTU Reviewed; 118 AA.
AC P9WMI9; L0T9V9; P67731; Q10864;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=HTH-type transcriptional regulator CmtR;
GN Name=cmtR; OrderedLocusNames=Rv1994c; ORFNames=MTCY39.25;
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 FUNCTION, AND MUTAGENESIS OF CYS-4; CYS-24; CYS-57; CYS-61 AND CYS-102.
RX PubMed=12939264; DOI=10.1074/jbc.m307877200;
RA Cavet J.S., Graham A.I., Meng W., Robinson N.J.;
RT "A cadmium-lead-sensing ArsR-SmtB repressor with novel sensory sites.
RT Complementary metal discrimination by NmtR AND CmtR in a common cytosol.";
RL J. Biol. Chem. 278:44560-44566(2003).
RN [3]
RP FUNCTION, AND SUBUNIT.
RX PubMed=15966722; DOI=10.1021/bi050094v;
RA Wang Y., Hemmingsen L., Giedroc D.P.;
RT "Structural and functional characterization of Mycobacterium tuberculosis
RT CmtR, a PbII/CdII-sensing SmtB/ArsR metalloregulatory repressor.";
RL Biochemistry 44:8976-8988(2005).
RN [4]
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 [5]
RP STRUCTURE BY NMR, CADMIUM BINDING, MASS SPECTROMETRY, AND SUBUNIT.
RX PubMed=17599915; DOI=10.1074/jbc.m701119200;
RA Banci L., Bertini I., Cantini F., Ciofi-Baffoni S., Cavet J.S.,
RA Dennison C., Graham A.I., Harvie D.R., Robinson N.J.;
RT "NMR structural analysis of cadmium sensing by winged helix repressor
RT CmtR.";
RL J. Biol. Chem. 282:30181-30188(2007).
CC -!- FUNCTION: Metal-responsive transcriptional repressor for the cmt
CC operon. Binding of cadmium or lead causes the repressor to dissociate
CC from the DNA. {ECO:0000269|PubMed:12939264,
CC ECO:0000269|PubMed:15966722}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15966722,
CC ECO:0000269|PubMed:17599915}.
CC -!- MASS SPECTROMETRY: Mass=25211; Method=Electrospray; Note=The measured
CC mass is that of a dimer, plus 2 cadmium ions.;
CC Evidence={ECO:0000269|PubMed:17599915};
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DR EMBL; AL123456; CCP44766.1; -; Genomic_DNA.
DR PIR; H70757; H70757.
DR RefSeq; NP_216510.1; NC_000962.3.
DR RefSeq; WP_003410018.1; NZ_NVQJ01000043.1.
DR PDB; 2JSC; NMR; -; A/B=1-118.
DR PDBsum; 2JSC; -.
DR AlphaFoldDB; P9WMI9; -.
DR BMRB; P9WMI9; -.
DR SMR; P9WMI9; -.
DR STRING; 83332.Rv1994c; -.
DR PaxDb; P9WMI9; -.
DR DNASU; 888889; -.
DR GeneID; 45425973; -.
DR GeneID; 888889; -.
DR KEGG; mtu:Rv1994c; -.
DR TubercuList; Rv1994c; -.
DR eggNOG; COG0640; Bacteria.
DR OMA; ADEKGCC; -.
DR PhylomeDB; P9WMI9; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0046870; F:cadmium ion binding; IDA:MTBBASE.
DR GO; GO:0097063; F:cadmium ion sensor activity; IDA:MTBBASE.
DR GO; GO:0003677; F:DNA binding; IDA:MTBBASE.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IMP:MTBBASE.
DR GO; GO:0032791; F:lead ion binding; IDA:MTBBASE.
DR GO; GO:0010468; P:regulation of gene expression; IDA:MTBBASE.
DR GO; GO:0046686; P:response to cadmium ion; IMP:MTBBASE.
DR GO; GO:0010288; P:response to lead ion; IMP:MTBBASE.
DR CDD; cd00090; HTH_ARSR; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR011991; ArsR-like_HTH.
DR InterPro; IPR001845; HTH_ArsR_DNA-bd_dom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF01022; HTH_5; 1.
DR PRINTS; PR00778; HTHARSR.
DR SMART; SM00418; HTH_ARSR; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS50987; HTH_ARSR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cadmium; DNA-binding; Metal-binding; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..118
FT /note="HTH-type transcriptional regulator CmtR"
FT /id="PRO_0000160629"
FT DOMAIN 3..97
FT /note="HTH arsR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00340"
FT BINDING 57
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT BINDING 61
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT BINDING 102
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_note="ligand shared between dimeric partners"
FT MUTAGEN 4
FT /note="C->S: No effect."
FT /evidence="ECO:0000269|PubMed:12939264"
FT MUTAGEN 24
FT /note="C->S: Loss of repressor activity."
FT /evidence="ECO:0000269|PubMed:12939264"
FT MUTAGEN 57
FT /note="C->S: Abolishes metal-induced derepression."
FT /evidence="ECO:0000269|PubMed:12939264"
FT MUTAGEN 61
FT /note="C->S: Abolishes metal-induced derepression."
FT /evidence="ECO:0000269|PubMed:12939264"
FT MUTAGEN 102
FT /note="C->S: Abolishes metal-induced derepression."
FT /evidence="ECO:0000269|PubMed:12939264"
FT HELIX 14..18
FT /evidence="ECO:0007829|PDB:2JSC"
FT HELIX 21..31
FT /evidence="ECO:0007829|PDB:2JSC"
FT TURN 37..39
FT /evidence="ECO:0007829|PDB:2JSC"
FT HELIX 40..44
FT /evidence="ECO:0007829|PDB:2JSC"
FT HELIX 48..58
FT /evidence="ECO:0007829|PDB:2JSC"
FT TURN 59..62
FT /evidence="ECO:0007829|PDB:2JSC"
FT STRAND 63..68
FT /evidence="ECO:0007829|PDB:2JSC"
FT STRAND 70..79
FT /evidence="ECO:0007829|PDB:2JSC"
FT HELIX 80..88
FT /evidence="ECO:0007829|PDB:2JSC"
FT STRAND 91..94
FT /evidence="ECO:0007829|PDB:2JSC"
SQ SEQUENCE 118 AA; 12495 MW; 1997F68DC2574989 CRC64;
MLTCEMRESA LARLGRALAD PTRCRILVAL LDGVCYPGQL AAHLGLTRSN VSNHLSCLRG
CGLVVATYEG RQVRYALADS HLARALGELV QVVLAVDTDQ PCVAERAASG EAVEMTGS
