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Literature summary for 2.7.11.1 extracted from

  • Urabe, H.; Ogawara, H.; Motojima, K.
    Expression and characterization of Streptomyces coelicolor serine/threonine protein kinase PkaE (2015), Biosci. Biotechnol. Biochem., 79, 855-862 .
No PubMed abstract available

Activating Compound

Activating Compound Comment Organism Structure
additional information recombinant PkaE is activated by autophosphorylation at threonine residues only, but not serine or tyrosine residues Streptomyces coelicolor

Cloned(Commentary)

Cloned (Comment) Organism
gene pkaE, recombinant expression of GST-tagged wild-type enzyme and mutant enzymes, and of His-tagged enzyme mutant K42N in Escherichia coli strain BL21(DE3)plysS Streptomyces coelicolor

Protein Variants

Protein Variants Comment Organism
K42N site-directed mutagenesis, inactive mutant Streptomyces coelicolor
K42Q site-directed mutagenesis, inactive mutant Streptomyces coelicolor
additional information construction of a gene disruption mutant of pkaE Streptomyces coelicolor

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
-
Streptomyces coelicolor 5737
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Streptomyces coelicolor
Mn2+ required Streptomyces coelicolor

Organism

Organism UniProt Comment Textmining
Streptomyces coelicolor Q9ZNB6
-
-
Streptomyces coelicolor A3(2) M145 Q9ZNB6
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein recombinant PkaE autophosphorylates at threonine residues only, but not serine or tyrosine residues Streptomyces coelicolor

Purification (Commentary)

Purification (Comment) Organism
recombinant GST-tagged wild-type enzyme and mutant enzymes, and His-tagged enzyme mutant K42N from Escherichia coli strain BL21(DE3)plysS by glutathione or nickel affinity chromatography, and gel filtration Streptomyces coelicolor

Source Tissue

Source Tissue Comment Organism Textmining
additional information gene pkaE is expressed during the late growth phase in Streptomyces coelicolor A3 (2) M145, which corresponds to the production time of blue pigments, pkaE is expressed during the late growth phase (60 to 84 h), but not the early growth phase (36 to 48 h) Streptomyces coelicolor
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + KbpA recombinant His-tagged substrate, 28 kDa Streptomyces coelicolor ADP + phospho-KbpA
-
?
ATP + KbpA recombinant His-tagged substrate, 28 kDa Streptomyces coelicolor A3(2) M145 ADP + phospho-KbpA
-
?
additional information recombinant PkaE autophosphorylates at threonine residues only, but not serine or tyrosine residues Streptomyces coelicolor ?
-
?
additional information recombinant PkaE autophosphorylates at threonine residues only, but not serine or tyrosine residues Streptomyces coelicolor A3(2) M145 ?
-
?

Subunits

Subunits Comment Organism
? x * 89000-94000, recombinant GST-tagged wild-type autophosphorylated enzyme PkaE, SDS-PAGE, x * 79500-80000, recombinant GST-tagged mutant enzymes, SDS-PAGE Streptomyces coelicolor

Synonyms

Synonyms Comment Organism
PkaE
-
Streptomyces coelicolor

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Streptomyces coelicolor

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.2
-
assay at Streptomyces coelicolor

Cofactor

Cofactor Comment Organism Structure
ATP
-
Streptomyces coelicolor

General Information

General Information Comment Organism
evolution the N-terminal region of PkaE is similar to the catalytic domains of several bacterial serine/ threonine protein kinases. In contrast, the C-terminal region of PkaE has no significant sequence similarity to any proteins Streptomyces coelicolor
malfunction disruption of chromosomal pkaE results in the overproduction of the actinorhodin-related blue pigment antibiotics Streptomyces coelicolor
physiological function enzyme PkaE acts as a negative regulator for production of the secondary metabolites. In addition, PkaE is able to phosphorylate KbpA, a regulator involved in the AfsK–AfsR regulatory pathway Streptomyces coelicolor