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Protein

HTH-type transcriptional regulator CmtR

Gene

cmtR

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Metal-responsive transcriptional repressor for the cmt operon. Binding of cadmium or lead causes the repressor to dissociate from the DNA.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi57Cadmium1
Metal bindingi61Cadmium1
Metal bindingi102Cadmium; shared with dimeric partner1

GO - Molecular functioni

  • cadmium ion binding Source: MTBBASE
  • cadmium ion sensor activity Source: MTBBASE
  • DNA binding Source: MTBBASE
  • DNA binding transcription factor activity Source: MTBBASE
  • lead ion binding Source: MTBBASE

GO - Biological processi

  • regulation of gene expression Source: MTBBASE
  • response to cadmium ion Source: MTBBASE
  • response to lead ion Source: MTBBASE
  • transcription, DNA-templated Source: UniProtKB-KW

Keywordsi

Molecular functionDNA-binding
Biological processTranscription, Transcription regulation
LigandCadmium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
HTH-type transcriptional regulator CmtR
Gene namesi
Name:cmtR
Ordered Locus Names:Rv1994c
ORF Names:MTCY39.25
OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Taxonomic identifieri83332 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
Proteomesi
  • UP000001584 Componenti: Chromosome

Organism-specific databases

TubercuListiRv1994c.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi4C → S: No effect. 1 Publication1
Mutagenesisi24C → S: Loss of repressor activity. 1 Publication1
Mutagenesisi57C → S: Abolishes metal-induced derepression. 1 Publication1
Mutagenesisi61C → S: Abolishes metal-induced derepression. 1 Publication1
Mutagenesisi102C → S: Abolishes metal-induced derepression. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001606291 – 118HTH-type transcriptional regulator CmtRAdd BLAST118

Proteomic databases

PaxDbiP9WMI9.

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

STRINGi83332.Rv1994c.

Structurei

Secondary structure

1118
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi14 – 18Combined sources5
Helixi21 – 31Combined sources11
Turni37 – 39Combined sources3
Helixi40 – 44Combined sources5
Helixi48 – 58Combined sources11
Turni59 – 62Combined sources4
Beta strandi63 – 68Combined sources6
Beta strandi70 – 79Combined sources10
Helixi80 – 88Combined sources9
Beta strandi91 – 94Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2JSCNMR-A/B1-118[»]
ProteinModelPortaliP9WMI9.
SMRiP9WMI9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini3 – 97HTH arsR-typePROSITE-ProRule annotationAdd BLAST95

Phylogenomic databases

eggNOGiENOG4108Y4S. Bacteria.
COG0640. LUCA.
KOiK21885.
OMAiADEKGCC.
PhylomeDBiP9WMI9.

Family and domain databases

CDDicd00090. HTH_ARSR. 1 hit.
Gene3Di1.10.10.10. 1 hit.
InterProiView protein in InterPro
IPR011991. ArsR-like_HTH.
IPR001845. HTH_ArsR_DNA-bd_dom.
IPR036388. WH-like_DNA-bd_sf.
IPR036390. WH_DNA-bd_sf.
PfamiView protein in Pfam
PF01022. HTH_5. 1 hit.
PRINTSiPR00778. HTHARSR.
SMARTiView protein in SMART
SM00418. HTH_ARSR. 1 hit.
SUPFAMiSSF46785. SSF46785. 1 hit.
PROSITEiView protein in PROSITE
PS50987. HTH_ARSR_2. 1 hit.

Sequencei

Sequence statusi: Complete.

P9WMI9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLTCEMRESA LARLGRALAD PTRCRILVAL LDGVCYPGQL AAHLGLTRSN
60 70 80 90 100
VSNHLSCLRG CGLVVATYEG RQVRYALADS HLARALGELV QVVLAVDTDQ
110
PCVAERAASG EAVEMTGS
Length:118
Mass (Da):12,495
Last modified:April 16, 2014 - v1
Checksum:i1997F68DC2574989
GO

Mass spectrometryi

Molecular mass is 25211 Da from positions 1 - 118. Determined by ESI. The measured mass is that of a dimer, plus 2 cadmium ions.1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP44766.1.
PIRiH70757.
RefSeqiNP_216510.1. NC_000962.3.
WP_003410018.1. NZ_KK339370.1.

Genome annotation databases

EnsemblBacteriaiCCP44766; CCP44766; Rv1994c.
GeneIDi888889.
KEGGimtu:Rv1994c.

Similar proteinsi

Entry informationi

Entry nameiCMTR_MYCTU
AccessioniPrimary (citable) accession number: P9WMI9
Secondary accession number(s): L0T9V9, P67731, Q10864
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 16, 2014
Last sequence update: April 16, 2014
Last modified: January 31, 2018
This is version 23 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
    Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references