Cloned (Comment) | Organism |
---|---|
expressed in Escherichia coli as a His-tagged fusion protein | Streptomyces coelicolor |
Protein Variants | Comment | Organism |
---|---|---|
K42N | in vitro phosphorylation assay shows that mutant protein is not able to phosphorylate itself | Streptomyces coelicolor |
K42R | in vitro phosphorylation assay shows that mutant protein is not able to phosphorylate itself | Streptomyces coelicolor |
additional information | disruption of chromosomal pkaD results in a significant loss of actinorhodin production. This result implies the involvement of pkaD in the regulation of secondary metabolism | Streptomyces coelicolor |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | a hydrophobicity plot indicates the presence of a putative transmembrane spanning sequence downstream of the catalytic domain, suggesting that PkaD is a transmembrane protein kinase | Streptomyces coelicolor | 16020 | - |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
63900 | - |
deduced from cDNA | Streptomyces coelicolor |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Streptomyces coelicolor | O83032 | - |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
phosphoprotein | PkaD is found to be phosphorylated by itsself at the threonine and tyrosine residues | Streptomyces coelicolor |
Purification (Comment) | Organism |
---|---|
using Ni-NTA chromatography | Streptomyces coelicolor |
Synonyms | Comment | Organism |
---|---|---|
PkaD | - |
Streptomyces coelicolor |
serine-threonine kinase | - |
Streptomyces coelicolor |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Streptomyces coelicolor |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Streptomyces coelicolor |