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Literature summary for 2.7.13.3 extracted from

  • Yeo, K.J.; Kim, E.H.; Hwang, E.; Han, Y.H.; Eo, Y.; Kim, H.J.; Kwon, O.; Hong, Y.S.; Cheong, C.; Cheong, H.K.
    pH-Dependent structural change of the extracellular sensor domain of the DraK histidine kinase from Streptomyces coelicolor (2013), Biochem. Biophys. Res. Commun., 431, 554-559.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene SCO3062, recombinant expression of N-terminally GST-tagged extracellular sensing domain (residues 28E-124R), and cytoplasmic domain (residues 146R-424R) of DraK in Escherichia coli strain BL21. Because the extracellular sensing domain of DraK is sensitive to proteolysis during purification, the C-terminal truncated short form (residues 28E-115R) is also constructed without the unstable C-terminal sequence (residues 116S-124R) after determination of the cleavage site (residues 115R-116S) in the extracellular sensing domain Streptomyces coelicolor

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Streptomyces coelicolor

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + DraR L-histidine Streptomyces coelicolor
-
ADP + DraR N-phospho-L-histidine
-
?
ATP + DraR L-histidine Streptomyces coelicolor A3(2)
-
ADP + DraR N-phospho-L-histidine
-
?
ATP + protein L-histidine Streptomyces coelicolor
-
ADP + protein N-phospho-L-histidine
-
?
ATP + protein L-histidine Streptomyces coelicolor A3(2)
-
ADP + protein N-phospho-L-histidine
-
?
additional information Streptomyces coelicolor a histidine kinase plays a role not only in the phosphorylation of its cognate response regulator but also in the dephosphorylation of the phosphorylated response regulator, acting as both kinase and phosphatase ?
-
?
additional information Streptomyces coelicolor A3(2) a histidine kinase plays a role not only in the phosphorylation of its cognate response regulator but also in the dephosphorylation of the phosphorylated response regulator, acting as both kinase and phosphatase ?
-
?

Organism

Organism UniProt Comment Textmining
Streptomyces coelicolor Q9KZ83
-
-
Streptomyces coelicolor A3(2) Q9KZ83
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant GST-tagged extracellular sensing domain proteins from Escherichia coli strain BL21 by glutathione affinity chromatography, tag cleavage by thrombin Streptomyces coelicolor

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + DraR L-histidine
-
Streptomyces coelicolor ADP + DraR N-phospho-L-histidine
-
?
ATP + DraR L-histidine autophosphorylation of DraK and subsequent phosphotransfer to its cognate response regulator protein DraR Streptomyces coelicolor ADP + DraR N-phospho-L-histidine
-
?
ATP + DraR L-histidine
-
Streptomyces coelicolor A3(2) ADP + DraR N-phospho-L-histidine
-
?
ATP + DraR L-histidine autophosphorylation of DraK and subsequent phosphotransfer to its cognate response regulator protein DraR Streptomyces coelicolor A3(2) ADP + DraR N-phospho-L-histidine
-
?
ATP + protein L-histidine
-
Streptomyces coelicolor ADP + protein N-phospho-L-histidine
-
?
ATP + protein L-histidine
-
Streptomyces coelicolor A3(2) ADP + protein N-phospho-L-histidine
-
?
additional information a histidine kinase plays a role not only in the phosphorylation of its cognate response regulator but also in the dephosphorylation of the phosphorylated response regulator, acting as both kinase and phosphatase Streptomyces coelicolor ?
-
?
additional information a histidine kinase plays a role not only in the phosphorylation of its cognate response regulator but also in the dephosphorylation of the phosphorylated response regulator, acting as both kinase and phosphatase Streptomyces coelicolor A3(2) ?
-
?

Subunits

Subunits Comment Organism
homodimer histidine kinases are composed of an N-terminal sensory (or input) domain, which senses external stimuli, and a conserved kinase domain, which contains an N-terminal dimerization and histidine phosphotransfer domain and a catalytic and ATP binding (CA) domain Streptomyces coelicolor
More monomer-dimer equilibrium of the shortened extracellular sensing domain of DraK in solution, with MWs of 9.7 kDa for the monomeric and 19.4 kDa for the dimeric form Streptomyces coelicolor

Synonyms

Synonyms Comment Organism
Drak
-
Streptomyces coelicolor
SCO3062
-
Streptomyces coelicolor
two-component system histidine kinase
-
Streptomyces coelicolor

Cofactor

Cofactor Comment Organism Structure
ATP
-
Streptomyces coelicolor

General Information

General Information Comment Organism
physiological function the DraR/DraK two-component system (TCS) of Streptomyces coelicolor is involved in the differential regulation of antibiotic biosynthesis. The extracellular sensory domain of histidine kinase DraK shows a pH-dependent conformational change involved in signal transduction process of DraR/DraK TCS. At low pH, the extracellular sensory domain is more structured than that at high pH. In particular, the glutamate at position 83 is an important residue for the pH-dependent conformational change Streptomyces coelicolor