Cloned (Comment) | Organism |
---|---|
recombinant expression of wild-type and mutant enzymes in Escherichia coli | Streptomyces coelicolor |
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 | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | transmembrane protein | Streptomyces coelicolor | 16020 | - |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Streptomyces coelicolor | Q9KZ83 | - |
- |
Streptomyces coelicolor ATCC BAA-471 | Q9KZ83 | - |
- |
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 | Comment | Organism |
---|---|---|
Drak | - |
Streptomyces coelicolor |
SCO3062 | gene name, UniProt | Streptomyces coelicolor |
two-component system histidine kinase | UniProt | Streptomyces coelicolor |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
additional information | - |
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 | 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 |