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Literature summary for 2.7.13.3 extracted from

  • Yeo, K.J.; Hong, Y.S.; Jee, J.G.; Lee, J.K.; Kim, H.J.; Park, J.W.; Kim, E.H.; Hwang, E.; Kim, S.Y.; Lee, E.G.; Kwon, O.; Cheong, H.K.
    Mechanism of the pH-induced conformational change in the sensor domain of the DraK histidine kinase via the E83, E105, and E107 residues (2014), PLoS ONE, 9, e107168.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of wild-type and mutant enzymes in Escherichia coli Streptomyces coelicolor

Protein Variants

Protein Variants Comment Organism
E105A site-directed mutagenesis, altered conformational change of the extracellular domain compared to wild-type Streptomyces coelicolor
E105L site-directed mutagenesis, altered conformational change of the extracellular domain compared to wild-type Streptomyces coelicolor
E105Q site-directed mutagenesis, altered conformational change of the extracellular domain compared to wild-type Streptomyces coelicolor
E107A site-directed mutagenesis, altered conformational change of the extracellular domain compared to wild-type Streptomyces coelicolor
E107L site-directed mutagenesis, altered conformational change of the extracellular domain compared to wild-type Streptomyces coelicolor
E107Q site-directed mutagenesis, altered conformational change of the extracellular domain compared to wild-type Streptomyces coelicolor
E83A site-directed mutagenesis, altered conformational change of the extracellular domain compared to wild-type Streptomyces coelicolor
E83L site-directed mutagenesis, altered conformational change of the extracellular domain compared to wild-type Streptomyces coelicolor
E83L/E105L/E107A site-directed mutagenesis, the mutant is pH-independent and mimics the low pH structure Streptomyces coelicolor
E83Q site-directed mutagenesis, altered conformational change of the extracellular domain compared to wild-type Streptomyces coelicolor
additional information generation of and draK gene deletion mutants, the gene disruption plasmids pKC-3063A and pKC-3062B are delivered into Streptomyces coelicolor A3(2) cells by conjugation with Escherichia coli ET12567(pUZ8002), and intergeneric conjugation between Escherichia coli and Streptomyces is performed, altered pH profile after acidic pH shock cultivation of the draR and draK gene deletion mutants, overview Streptomyces coelicolor

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane transmembrane protein Streptomyces coelicolor 16020
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Organism

Organism UniProt Comment Textmining
Streptomyces coelicolor Q9KZ83
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Streptomyces coelicolor ATCC BAA-471 Q9KZ83
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Subunits

Subunits Comment Organism
More mechanism for the pH-dependent conformational change of the the extracellular sensor domain protein of DraK, overview. The structure contains a mixed alpha-beta fold, adopting a fold similar to the ubiquitous sensor domain of histidine kinase Streptomyces coelicolor

Synonyms

Synonyms Comment Organism
Drak
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Streptomyces coelicolor
SCO3062 gene name, UniProt Streptomyces coelicolor
two-component system histidine kinase UniProt Streptomyces coelicolor

pH Range

pH Minimum pH Maximum Comment Organism
additional information
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mechanism for the pH-dependent conformational change of the extracellular sensor domain of the DraK protein involving residues E83, E105, and E107 with very high pKa values, overview Streptomyces coelicolor

General Information

General Information Comment Organism
additional information mechanism for the pH-dependent conformational change of the extracellular sensor domain of DraK protein involving residues E83, E105, and E107 with very high pKa values, overview Streptomyces coelicolor
physiological function the DraR/DraK two-component system is involved in the differential regulation of antibiotic biosynthesis in a medium-dependent manner, the DraR/DraK two-component system plays an important role in the pH regulation of Streptomyces coelicolor growth medium. The enzyme and the DraR/DraK two-component system are essential for the recovery of the pH of Streptomyces coelicolor growth medium after acid shock, overview Streptomyces coelicolor