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 (Comment) | Organism |
---|---|
gene rpkA, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)pLysS | Deinococcus radiodurans |
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 | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Deinococcus radiodurans |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Deinococcus radiodurans | Q9RRH3 | - |
- |
Deinococcus radiodurans ATCC 13939 | Q9RRH3 | - |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
phosphoprotein | enzyme RqkA performs autophosphorylation | Deinococcus radiodurans |
Purification (Comment) | Organism |
---|---|
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3)pLysS by nickel affinity chromatography | Deinococcus radiodurans |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + maltose binding protein | - |
Deinococcus radiodurans | ADP + phospho-maltose binding protein | - |
? | |
ATP + maltose binding protein | - |
Deinococcus radiodurans ATCC 13939 | ADP + phospho-maltose binding protein | - |
? | |
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 | - |
? | |
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 | - |
? | |
additional information | RqkA performs autophosphorylation | Deinococcus radiodurans | ? | - |
? | |
additional information | RqkA performs autophosphorylation | Deinococcus radiodurans ATCC 13939 | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
DNA damage-responsive serine/threonine-protein kinase | UniProt | Deinococcus radiodurans |
DR2518 | - |
Deinococcus radiodurans |
DR_2518 | - |
Deinococcus radiodurans |
eukaryotic type serine/threonine protein kinase | - |
Deinococcus radiodurans |
pprA | - |
Deinococcus radiodurans |
rpkA | - |
Deinococcus radiodurans |
RqkA | - |
Deinococcus radiodurans |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Deinococcus radiodurans |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
assay at | Deinococcus radiodurans |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Deinococcus radiodurans |
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 |