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Literature summary for 2.7.11.1 extracted from

  • Rajpurohit, Y.; Misra, H.
    Structure-function study of deinococcal serine/threonine protein kinase implicates its kinase activity and DNA repair protein phosphorylation roles in radioresistance of Deinococcus radiodurans (2013), Int. J. Biochem. Cell Biol., 45, 2541-2552 .
No PubMed abstract available

Activating Compound

Activating Compound Comment Organism Structure
additional information the activation loop is an important regulatory domain for kinase function, and is known for conformational and functional plasticity Deinococcus radiodurans

Cloned(Commentary)

Cloned (Comment) Organism
gene rpkA, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)pLysS Deinococcus radiodurans

Protein Variants

Protein Variants Comment Organism
K42A site-directed mutagenesis, inactive mutant, the K42A mutant shows neither autophosphorylation nor phosphorylation of maltose binding protein Deinococcus radiodurans
additional information K42Aan inactive mutant of RqkA, that fails to recover the loss of gamma radiation resistance in DELTArqkA cells, while T169A and S171A proteins recover the cells partially, which decreases further in double mutant T169A/S171A. Level of complementation is nearly 3-5 fold less by T169A and S171A derivatives and more than 20folds less byT169A/S171A double mutant as compared to wild-type RqkA at10kGy gamma radiation dose Deinococcus radiodurans
S162A site-directed mutagenesis, the mutant shows activity similar to the wild-type protein kinase activity Deinococcus radiodurans
S171A site-directed mutagenesis, the mutant shows 10% of wild-type protein kinase activity Deinococcus radiodurans
T169A site-directed mutagenesis, the mutant shows 5% of wild-type protein kinase activity Deinococcus radiodurans
T169A/S171A site-directed mutagenesis, the mutant shows 1% of wild-type protein kinase activity Deinococcus radiodurans

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Deinococcus radiodurans

Organism

Organism UniProt Comment Textmining
Deinococcus radiodurans Q9RRH3
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Deinococcus radiodurans ATCC 13939 Q9RRH3
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Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein enzyme RqkA performs autophosphorylation Deinococcus radiodurans

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3)pLysS by nickel affinity chromatography Deinococcus radiodurans

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + maltose binding protein
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Deinococcus radiodurans ADP + phospho-maltose binding protein
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?
ATP + maltose binding protein
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Deinococcus radiodurans ATCC 13939 ADP + phospho-maltose binding protein
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?
ATP + PprA RqkA phosphorylates PprA at T72, S112, and T144 in vitro with the majority of it goes to T72 site. Unlike wild-type PprA and single mutants of T72, S112, and T144 residues, the T72A/S112A double and T72A/S112A/T144A triple mutant derivatives of PprA are no substrates. In vivo phosphorylation of PprA and mapping of its phosphosites, overview Deinococcus radiodurans ADP + phospho-PprA
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?
ATP + PprA RqkA phosphorylates PprA at T72, S112, and T144 in vitro with the majority of it goes to T72 site. Unlike wild-type PprA and single mutants of T72, S112, and T144 residues, the T72A/S112A double and T72A/S112A/T144A triple mutant derivatives of PprA are no substrates. In vivo phosphorylation of PprA and mapping of its phosphosites, overview Deinococcus radiodurans ATCC 13939 ADP + phospho-PprA
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?
additional information RqkA performs autophosphorylation Deinococcus radiodurans ?
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?
additional information RqkA performs autophosphorylation Deinococcus radiodurans ATCC 13939 ?
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?

Synonyms

Synonyms Comment Organism
DNA damage-responsive serine/threonine-protein kinase UniProt Deinococcus radiodurans
DR2518
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Deinococcus radiodurans
DR_2518
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Deinococcus radiodurans
eukaryotic type serine/threonine protein kinase
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Deinococcus radiodurans
pprA
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Deinococcus radiodurans
rpkA
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Deinococcus radiodurans
RqkA
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Deinococcus radiodurans

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
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assay at Deinococcus radiodurans

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
assay at Deinococcus radiodurans

Cofactor

Cofactor Comment Organism Structure
ATP
-
Deinococcus radiodurans

General Information

General Information Comment Organism
evolution enzyme RqkA has all theconserved motifs like P-loop, helix-C, DFG motif, and catalytic loop, as known in other eukaryotic STPKs, eukaryotic type serine/threonine protein kinases phosphorylation motifs, overview Deinococcus radiodurans
malfunction deletion of gene rqkA in pprA::cat background enhances radiosensitivity of the pprA mutant, which became nearly similar to DELTArqkA resistance to gamma-radiation Deinococcus radiodurans
additional information enzyme RqkA has all the conserved motifs like P-loop, helix-C, DFG motif, and catalytic loop, as known in other eukaryotic STPKs. Topology analysis predicts RqkA as an N-in, C-out membrane protein with three transmembrane domains hypothetically placing the catalytic domain in cyto-plasm and the sensory C-terminal domain possibly in periplasmic space, structure-function analysis, overview Deinococcus radiodurans
physiological function lysine 42 (K42), located in N-terminal lobe of kinase domain of RqkA, is essential for catalytic functions and the kinase activity of RqkA as well as phosphorylation of PprA. PprA is a DNA binding protein and stimulate DNA ligase activity. PprA is activated by phosphorylation. Enzyme RqkA has roles in gamma-radiation resistance of Deinococcus radiodurans. RqkA residues S162, T169 and S171 are present in the activation loop and are the possible phosphoacceptor sites Deinococcus radiodurans