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Protein

HTH-type transcriptional regulator KmtR

Gene

kmtR

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Represses expression of Rv2025c and its own expression. Acts by binding to the promoter regions.1 Publication

Miscellaneous

KmtR has tighter affinities for nickel and cobalt than NmtR.1 Publication

Enzyme regulationi

Binding to DNA is inhibited by nickel and cobalt ions.1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi44 – 67H-T-H motifPROSITE-ProRule annotationAdd BLAST24

GO - Molecular functioni

  • DNA binding Source: MTBBASE
  • transcription factor activity, sequence-specific DNA binding Source: InterPro

GO - Biological processi

  • response to cobalt ion Source: MTBBASE
  • response to nickel cation Source: MTBBASE
  • transcription, DNA-templated Source: UniProtKB-KW

Keywordsi

Molecular functionDNA-binding, Repressor
Biological processTranscription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
HTH-type transcriptional regulator KmtR
Gene namesi
Name:kmtR
Ordered Locus Names:Rv0827c
OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Taxonomic identifieri83332 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
Proteomesi
  • UP000001584 Componenti: Chromosome

Organism-specific databases

TubercuListiRv0827c.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi16C → S: No change in activity. Does not affect regulation by metal ions. 1 Publication1
Mutagenesisi88H → Q: No change in activity. Lack of regulation by metal ions. 1 Publication1
Mutagenesisi101E → Q: No change in activity. Lack of regulation by metal ions. 1 Publication1
Mutagenesisi102H → Q: No change in activity. Lack of regulation by metal ions. 1 Publication1
Mutagenesisi110H → Q: No change in activity. Lack of regulation by metal ions. 1 Publication1
Mutagenesisi111H → Q: No change in activity. Lack of regulation by metal ions. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004191781 – 130HTH-type transcriptional regulator KmtRAdd BLAST130

Proteomic databases

PaxDbiO53838.

Expressioni

Inductioni

Negatively autoregulated.1 Publication

Interactioni

Protein-protein interaction databases

STRINGi83332.Rv0827c.

Structurei

3D structure databases

ProteinModelPortaliO53838.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini10 – 104HTH arsR-typePROSITE-ProRule annotationAdd BLAST95

Phylogenomic databases

eggNOGiENOG41082SX. Bacteria.
COG0640. LUCA.
HOGENOMiHOG000144506.
InParanoidiO53838.
OMAiEGKHIYY.
PhylomeDBiO53838.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiView protein in InterPro
IPR001845. HTH_ArsR_DNA-bd_dom.
IPR011991. WHTH_DNA-bd_dom.
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.

O53838-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYADSGPDPL PDDQVCLVVE VFRMLADATR VQVLWSLADR EMSVNELAEQ
60 70 80 90 100
VGKPAPSVSQ HLAKLRMARL VRTRRDGTTI FYRLENEHVR QLVIDAVFNA
110 120 130
EHAGPGIPRH HRAAGGLQSV AKASATKDVG
Length:130
Mass (Da):14,296
Last modified:July 5, 2004 - v3
Checksum:iDC6C2FD5B599D1A2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP43575.1.
PIRiC70811.
RefSeqiNP_215342.1. NC_000962.3.
WP_003404335.1. NZ_KK339370.1.

Genome annotation databases

EnsemblBacteriaiCCP43575; CCP43575; Rv0827c.
GeneIDi885375.
KEGGimtu:Rv0827c.
mtv:RVBD_0827c.
PATRICifig|83332.111.peg.914.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP43575.1.
PIRiC70811.
RefSeqiNP_215342.1. NC_000962.3.
WP_003404335.1. NZ_KK339370.1.

3D structure databases

ProteinModelPortaliO53838.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi83332.Rv0827c.

Proteomic databases

PaxDbiO53838.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCCP43575; CCP43575; Rv0827c.
GeneIDi885375.
KEGGimtu:Rv0827c.
mtv:RVBD_0827c.
PATRICifig|83332.111.peg.914.

Organism-specific databases

TubercuListiRv0827c.

Phylogenomic databases

eggNOGiENOG41082SX. Bacteria.
COG0640. LUCA.
HOGENOMiHOG000144506.
InParanoidiO53838.
OMAiEGKHIYY.
PhylomeDBiO53838.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiView protein in InterPro
IPR001845. HTH_ArsR_DNA-bd_dom.
IPR011991. WHTH_DNA-bd_dom.
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.
ProtoNetiSearch...

Entry informationi

Entry nameiKMTR_MYCTU
AccessioniPrimary (citable) accession number: O53838
Secondary accession number(s): F2GNU2, L0T4V7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 3, 2012
Last sequence update: July 5, 2004
Last modified: June 7, 2017
This is version 116 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.