P0DJL7 · DTXR_CORDI

Function

function

Iron-binding repressor of the dipheteria toxin gene expression. May serve as a global regulator of gene expression. Represses ripA under iron excess.

Miscellaneous

The N-terminal region may be involved in iron binding and may associate with the tox operator. Binding of dtxR to tox operator requires a divalent metal ion such as cobalt, ferric, manganese, and nickel ions whereas zinc ions show weak activation.
The dtxR gene was functional in the non-toxygenic strains CD95/211-, CD95/305- and CD95/407- isolated in the United Kingdom. These findings demonstrate that, if lysogenised by a bacteriophage, non-toxygenic strains could produce toxin and therefore represent a potential reservoir for toxygenic C.diphtheriae.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytoplasm
Molecular FunctionDNA binding
Molecular FunctionDNA-binding transcription factor activity
Molecular Functionidentical protein binding
Molecular Functionprotein dimerization activity
Molecular FunctionSH3 domain binding
Molecular Functiontransition metal ion binding
Biological Processnegative regulation of DNA-templated transcription

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Diphtheria toxin repressor
  • Alternative names
    • Iron-dependent diphtheria tox regulatory element
    • Tox regulatory factor

Gene names

    • Name
      dtxR
    • Ordered locus names
      DIP1414

Organism names

Accessions

  • Primary accession
    P0DJL7
  • Secondary accessions
    • P33120
    • Q5XQ41
    • Q5XQ42
    • Q5XQ43

Proteomes

Subcellular Location

Keywords

Phenotypes & Variants

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variant47in iron-insensitive tox constitutive mutant C7hm723
Natural variant141in strain: CD95/211-
Natural variant147in strain: C7-, C7hm723-, 1030-, CD95/305-, CD95/211- and CD95/407-
Natural variant165in strain: 1030-
Natural variant174in strain: 1030-
Natural variant191in strain: 1030-
Natural variant199in strain: CD95/407-
Natural variant201in strain: CD95/305-
Natural variant205in strain: 1030-
Natural variant214in strain: C7-, C7hm723-, CD95/305-, CD95/211- and CD95/407-
Natural variant214in strain: 1030-
Natural variant218in strain: 1030-
Natural variant221in strain: CD95/211-
Natural variant221in strain: CD95/407-

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 14 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Miscellaneous

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00002011061-226Diphtheria toxin repressor

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain4-65HTH dtxR-type

Sequence similarities

Belongs to the DtxR/MntR family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    226
  • Mass (Da)
    25,344
  • Last updated
    2012-09-05 v1
  • Checksum
    A14F89FDB8719D5C
MKDLVDTTEMYLRTIYELEEEGVTPLRARIAERLEQSGPTVSQTVARMERDGLVVVASDRSLQMTPTGRTLATAVMRKHRLAERLLTDIIGLDINKVHDEACRWEHVMSDEVERRLVKVLKDVSRSPFGNPIPGLDELGVGNSDAAVPGTRVIDAATSMPRKVRIVQINEIFQVETDQFTQLLDADIRVGSEVEIVDRDGHITLSHNGKDVELIDDLAHTIRIEEL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
M34239
EMBL· GenBank· DDBJ
AAA23296.1
EMBL· GenBank· DDBJ
Genomic DNA
M80336
EMBL· GenBank· DDBJ
AAA23302.1
EMBL· GenBank· DDBJ
Genomic DNA
M80337
EMBL· GenBank· DDBJ
AAA23301.1
EMBL· GenBank· DDBJ
Genomic DNA
AY741368
EMBL· GenBank· DDBJ
AAU93781.1
EMBL· GenBank· DDBJ
Genomic DNA
AY741369
EMBL· GenBank· DDBJ
AAU93782.1
EMBL· GenBank· DDBJ
Genomic DNA
AY741370
EMBL· GenBank· DDBJ
AAU93783.1
EMBL· GenBank· DDBJ
Genomic DNA
BX248358
EMBL· GenBank· DDBJ
CAE49945.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
Help