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Literature summary extracted from

  • Shakir, S.; Bryant, K.; Larabee, J.; Hamm, E.; Lovchik, J.; Lyons, C.; Ballard, J.
    Regulatory interactions of a virulence-associated serine/threonine phosphatase-kinase pair in Bacillus anthracis (2010), J. Bacteriol., 192, 400-409.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.11.1 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

EC Number Protein Variants Comment Organism
2.7.11.1 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
2.7.11.1 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
2.7.11.1 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
2.7.11.1 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
2.7.11.1 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
2.7.11.1 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
2.7.11.1 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
2.7.11.1 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

EC Number Metals/Ions Comment Organism Structure
2.7.11.1 Mn2+ activates Bacillus anthracis

Organism

EC Number Organism UniProt Comment Textmining
2.7.11.1 Bacillus anthracis
-
-
-
2.7.11.1 Bacillus anthracis 7702
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.7.11.1 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 (Commentary)

EC Number Purification (Comment) Organism
2.7.11.1 recombinant His-tagged wild-type and mutant BA-Stk1cats from Escherichia coli strain BL21(DE3) Bacillus anthracis

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.7.11.1 additional information the bacteria are propagated in Abelson murine leukemia virus-transformed murine macrophages derived from ascites of BALB/c mice Bacillus anthracis
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.11.1 ATP + myelin basic protein
-
 Bacillus anthracis ADP + phosphorylated myelin basic protein
-
 ?
2.7.11.1 ATP + myelin basic protein
-
 Bacillus anthracis 7702 ADP + phosphorylated myelin basic protein
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.7.11.1 BA-Stk1
-
 Bacillus anthracis
2.7.11.1 serine/threonine kinase
-
 Bacillus anthracis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.11.1 37
-
 assay at Bacillus anthracis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.11.1 7.2
-
 assay at Bacillus anthracis

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.11.1 ATP
-
 Bacillus anthracis

General Information

EC Number General Information Comment Organism
2.7.11.1 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
2.7.11.1 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