Cloned (Comment) | Organism |
---|---|
expression of His-tagged wild-type and mutant BA-Stk1cats in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain JM109 | Bacillus anthracis |
Protein Variants | Comment | Organism |
---|---|---|
S173A | site-directed mutagenesis of a phosphorylation site, the mutant shows 40% reduced ATP hydrolysis and almost completely reduced phosphorylation activity compared to the wild-type enzyme | Bacillus anthracis |
S173D | site-directed mutagenesis of a phosphorylation site, the mutant shows 55% increased ATP hydrolysis and almost completely reduced phosphorylation activity compared to the wild-type enzyme | Bacillus anthracis |
S214A | site-directed mutagenesis of a phosphorylation site, the mutant shows 40% reduced ATP hydrolysis and 70% reduced phosphorylation activity compared to the wild-type enzyme | Bacillus anthracis |
S214D | site-directed mutagenesis of a phosphorylation site, the mutant shows 5% increased ATP hydrolysis and 20% increased phosphorylation activity compared to the wild-type enzyme | Bacillus anthracis |
T165A | site-directed mutagenesis of a phosphorylation site, the mutant shows 10% reduced ATP hydrolysis and 80% reduced phosphorylation activity compared to the wild-type enzyme | Bacillus anthracis |
T165D | site-directed mutagenesis of a phosphorylation site, the mutant shows 14% reduced ATP hydrolysis and 80% reduced phosphorylation activity compared to the wild-type enzyme | Bacillus anthracis |
T290A | site-directed mutagenesis of a phosphorylation site, the mutant shows 5% increased ATP hydrolysis and 20% reduced phosphorylation activity compared to the wild-type enzyme | Bacillus anthracis |
T290D | site-directed mutagenesis of a phosphorylation site, the mutant shows 15% increased ATP hydrolysis and slightly reduced phosphorylation activity compared to the wild-type enzyme | Bacillus anthracis |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mn2+ | activates | Bacillus anthracis |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus anthracis | - |
- |
- |
Bacillus anthracis 7702 | - |
- |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
phosphoprotein | three phosphorylated residues, T165, S173, and S214, dephosphorylation of the regulatory sites by the endogenous serine/threonine phosphatase BA-Stp1 reduces the enzyme kinase activity. Phospshorylated T165 and S173 are necessary for optimal substrate phosphorylation, while phosphorylated S214 is necessary for complete ATP hydrolysis, autophosphorylation, and substrate phosphorylation | Bacillus anthracis |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged wild-type and mutant BA-Stk1cats from Escherichia coli strain BL21(DE3) | Bacillus anthracis |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
additional information | the bacteria are propagated in Abelson murine leukemia virus-transformed murine macrophages derived from ascites of BALB/c mice | Bacillus anthracis | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + myelin basic protein | - |
Bacillus anthracis | ADP + phosphorylated myelin basic protein | - |
? | |
ATP + myelin basic protein | - |
Bacillus anthracis 7702 | ADP + phosphorylated myelin basic protein | - |
? |
Synonyms | Comment | Organism |
---|---|---|
BA-Stk1 | - |
Bacillus anthracis |
serine/threonine kinase | - |
Bacillus anthracis |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Bacillus anthracis |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.2 | - |
assay at | Bacillus anthracis |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Bacillus anthracis |
General Information | Comment | Organism |
---|---|---|
malfunction | Bacillus anthracis STPK101, a null mutant lacking serine/threonine phosphatase, BA-Stp1, EC 3.1.3.16, and serine/threonine kinase, BA-Stk1, is impaired in its ability to survive within macrophages, and this correlates with an observed reduction in virulence in a mouse model of pulmonary anthrax | Bacillus anthracis |
metabolism | regulatory interactions of a serine/threonine phosphatase, BA-Stp1, EC 3.1.3.16, and serine/threonine kinase, BA-Stk1, pair in Bacillus anthracis: dephosphorylation of BA-Stk1 by BA-Stp1 alters the BA-Stk1 kinase activity | Bacillus anthracis |