CMTR_MYCTO
ID CMTR_MYCTO Reviewed; 118 AA.
AC P9WMI8; 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 39.
DE RecName: Full=HTH-type transcriptional regulator CmtR;
GN Name=cmtR; OrderedLocusNames=MT2050;
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: Metal-responsive transcriptional repressor for the cmt
CC operon. Binding of cadmium or lead causes the repressor to dissociate
CC from the DNA (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
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DR EMBL; AE000516; AAK46327.1; -; Genomic_DNA.
DR PIR; H70757; H70757.
DR RefSeq; WP_003410018.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WMI8; -.
DR BMRB; P9WMI8; -.
DR SMR; P9WMI8; -.
DR EnsemblBacteria; AAK46327; AAK46327; MT2050.
DR GeneID; 45425973; -.
DR KEGG; mtc:MT2050; -.
DR PATRIC; fig|83331.31.peg.2207; -.
DR HOGENOM; CLU_097806_5_2_11; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Cadmium; DNA-binding; Metal-binding; Transcription;
KW Transcription regulation.
FT CHAIN 1..118
FT /note="HTH-type transcriptional regulator CmtR"
FT /id="PRO_0000427296"
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 /evidence="ECO:0000255|PROSITE-ProRule:PRU00340"
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 /evidence="ECO:0000255|PROSITE-ProRule:PRU00340"
FT BINDING 102
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00340"
SQ SEQUENCE 118 AA; 12495 MW; 1997F68DC2574989 CRC64;
MLTCEMRESA LARLGRALAD PTRCRILVAL LDGVCYPGQL AAHLGLTRSN VSNHLSCLRG
CGLVVATYEG RQVRYALADS HLARALGELV QVVLAVDTDQ PCVAERAASG EAVEMTGS
