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Literature summary 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

EC Number Activating Compound Comment Organism Structure
2.7.11.1 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)

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

Protein Variants

EC Number Protein Variants Comment Organism
2.7.11.1 K42A site-directed mutagenesis, inactive mutant, the K42A mutant shows neither autophosphorylation nor phosphorylation of maltose binding protein Deinococcus radiodurans
2.7.11.1 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
2.7.11.1 S162A site-directed mutagenesis, the mutant shows activity similar to the wild-type protein kinase activity Deinococcus radiodurans
2.7.11.1 S171A site-directed mutagenesis, the mutant shows 10% of wild-type protein kinase activity Deinococcus radiodurans
2.7.11.1 T169A site-directed mutagenesis, the mutant shows 5% of wild-type protein kinase activity Deinococcus radiodurans
2.7.11.1 T169A/S171A site-directed mutagenesis, the mutant shows 1% of wild-type protein kinase activity Deinococcus radiodurans

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.11.1 Mg2+ required Deinococcus radiodurans

Organism

EC Number Organism UniProt Comment Textmining
2.7.11.1 Deinococcus radiodurans Q9RRH3
-
-
2.7.11.1 Deinococcus radiodurans ATCC 13939 Q9RRH3
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.7.11.1 phosphoprotein enzyme RqkA performs autophosphorylation Deinococcus radiodurans

Purification (Commentary)

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.11.1 ATP + maltose binding protein
-
 Deinococcus radiodurans ADP + phospho-maltose binding protein
-
 ?
2.7.11.1 ATP + maltose binding protein
-
 Deinococcus radiodurans ATCC 13939 ADP + phospho-maltose binding protein
-
 ?
2.7.11.1 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
-
 ?
2.7.11.1 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
-
 ?
2.7.11.1 additional information RqkA performs autophosphorylation Deinococcus radiodurans ?
-
 ?
2.7.11.1 additional information RqkA performs autophosphorylation Deinococcus radiodurans ATCC 13939 ?
-
 ?

Synonyms

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

Temperature Optimum [°C]

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

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.11.1 7
-
 assay at Deinococcus radiodurans

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.11.1 ATP
-
 Deinococcus radiodurans

General Information

EC Number General Information Comment Organism
2.7.11.1 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
2.7.11.1 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
2.7.11.1 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
2.7.11.1 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