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Literature summary for 2.7.11.1 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)

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

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

Metals/Ions Comment Organism Structure
Mn2+ activates Bacillus anthracis

Organism

Organism UniProt Comment Textmining
Bacillus anthracis
-
-
-
Bacillus anthracis 7702
-
-
-

Posttranslational Modification

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 (Commentary)

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

Source Tissue

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 and Products (Substrate)

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

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

Temperature Optimum [°C]

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

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
ATP
-
Bacillus anthracis

General Information

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