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ADP + a [protein]-Nomega-phospho-L-arginine
ATP + a [protein]-L-arginine
ADP + [Ac-KIVQSKRGGGGYIK-NH2]-Nomega-phospho-L-arginine
ATP + [Ac-KIVQSKRGGGGYIK-NH2]-L-arginine
peptide substrate derived from the CtsR protein
-
-
r
ATP + a [protein]-L-arginine
ADP + a [protein]-Nomega-phospho-L-arginine
ATP + [ClpC]-L-arginine
ADP + [ClpC]-Nomega-phospho-L-arginine
Bacillus subtilis gene repressor, model substrate
-
-
?
ATP + [CtsR]-L-arginine
ADP + [CtsR]-Nomega-phospho-L-arginine
Geobacillus stearothermophilus heat-shock protein, model substrate
-
-
?
ATP + [CtsR]-L-arginine62
ADP + [CtsR]-Nomega-phospho-L-arginine62
-
enzyme specifically phosphorylates arginine residues in the DNA binding domain of heat-shock regulator protein CtsR, thereby impairing its function as a repressor of stress response genes. Modification occurs at residue R62
-
?
ATP + [McsB]-L-arginine
ADP + [McsB]-Nomega-phospho-L-arginine
autophosphorylation of enzyme
-
-
?
ADP + a [protein]-Nomega-phospho-L-arginine
ATP + a [protein]-L-arginine
-
-
-
r
ADP + a [protein]-Nomega-phospho-L-arginine
ATP + a [protein]-L-arginine
the enzyme can dephosphorylate phosphoarginine residues to produce ATP from ADP, implicating the dynamic control of protein pArg levels by the kinase even without a phosphatase. The enzyme can also mediate the dephosphorylation of the pArg residue to generate ATP
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-
r
ATP + a [protein]-L-arginine
ADP + a [protein]-Nomega-phospho-L-arginine
-
-
-
-
?
ATP + a [protein]-L-arginine
ADP + a [protein]-Nomega-phospho-L-arginine
-
-
-
?
ATP + a [protein]-L-arginine
ADP + a [protein]-Nomega-phospho-L-arginine
-
protein arginine phosphorylation is a physiological significant protein modification in wild-type Bacillus subtilis cells
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-
?
ATP + a [protein]-L-arginine
ADP + a [protein]-Nomega-phospho-L-arginine
-
-
-
?
ATP + a [protein]-L-arginine
ADP + a [protein]-Nomega-phospho-L-arginine
-
-
-
r
ATP + a [protein]-L-arginine
ADP + a [protein]-Nomega-phospho-L-arginine
the enzyme can dephosphorylate phosphoarginine residues to produce ATP from ADP, implicating the dynamic control of protein pArg levels by the kinase even without a phosphatase. The enzyme can also mediate the dephosphorylation of the pArg residue to generate ATP
-
-
r
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ADP + a [protein]-Nomega-phospho-L-arginine
ATP + a [protein]-L-arginine
the enzyme can dephosphorylate phosphoarginine residues to produce ATP from ADP, implicating the dynamic control of protein pArg levels by the kinase even without a phosphatase. The enzyme can also mediate the dephosphorylation of the pArg residue to generate ATP
-
-
r
ATP + a [protein]-L-arginine
ADP + a [protein]-Nomega-phospho-L-arginine
ATP + a [protein]-L-arginine
ADP + a [protein]-Nomega-phospho-L-arginine
-
-
-
?
ATP + a [protein]-L-arginine
ADP + a [protein]-Nomega-phospho-L-arginine
-
protein arginine phosphorylation is a physiological significant protein modification in wild-type Bacillus subtilis cells
-
-
?
ATP + a [protein]-L-arginine
ADP + a [protein]-Nomega-phospho-L-arginine
-
-
-
?
ATP + a [protein]-L-arginine
ADP + a [protein]-Nomega-phospho-L-arginine
the enzyme can dephosphorylate phosphoarginine residues to produce ATP from ADP, implicating the dynamic control of protein pArg levels by the kinase even without a phosphatase. The enzyme can also mediate the dephosphorylation of the pArg residue to generate ATP
-
-
r
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physiological function
-
protein arginine phosphorylation is a physiological significant protein modification in wild-type Bacillus subtilis cells
physiological function
in addition to its kinase activity and adaptor function for the ClpC ATPase, McsB might also serve as a proteolytic adaptor for the ClpX ATPase in the degradation mechanism of MgsR
physiological function
protein arginine phosphorylation regulates stress responses and virulence in bacteria. It can dephosphorylate phosphoarginine residues to produce ATP from ADP, implicating the dynamic control of protein pArg levels by the kinase even without a phosphatase
physiological function
-
in addition to its kinase activity and adaptor function for the ClpC ATPase, McsB might also serve as a proteolytic adaptor for the ClpX ATPase in the degradation mechanism of MgsR
-
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analysis
analysis of the fragmentation behavior of peptides with arginine phosphorylation in mass spectrometry and its influence on phospho-site localization
analysis
use of a Bacillus subtilis ywlE- strain lacking the phosphatase activity corresponding to protein arginine kinase MscB as a source for arginine-phosphorylated proteins and mass spectrometry protocols to analyze the arginine modification. A substrate-trapping mutant of the YwlE phosphatase retains binding affinity toward arginine-phosphorylated proteins but cannot hydrolyze the captured substrates
analysis
-
detection of protein arginine kinase McsB via a sequential turn-off surface enhance Raman scattering (SERS) assay platform. The positive charged peptide initiates the aggregation of labelled Au nanoparticles to form hot spots, resulting to a higher SERS intensity. The SERS biosensor shows high sensitivity, selectivity and simplicity, detection limit for McsB is 46 pM
analysis
reversible fluorescent activity probes for protein Arg kinases and phosphatases to allow real-time kinetic assays, probe is based on the chelation-enhanced fluorescence (CHEF) effect of the cysteine-sulfonamido-oxine fluorophore
analysis
-
use of a Bacillus subtilis ywlE- strain lacking the phosphatase activity corresponding to protein arginine kinase MscB as a source for arginine-phosphorylated proteins and mass spectrometry protocols to analyze the arginine modification. A substrate-trapping mutant of the YwlE phosphatase retains binding affinity toward arginine-phosphorylated proteins but cannot hydrolyze the captured substrates
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Fuhrmann, J.; Schmidt, A.; Spiess, S.; Lehner, A.; Turgay, K.; Mechtler, K.; Charpentier, E.; Clausen, T.
McsB is a protein arginine kinase that phosphorylates and inhibits the heat-shock regulator CtsR
Science
324
1323-1327
2009
Geobacillus stearothermophilus (P0DMM5)
brenda
Elsholz, A.K.; Turgay, K.; Michalik, S.; Hessling, B.; Gronau, K.; Oertel, D.; Mader, U., Bernhardt, J., Becher, D., Hecker, M. and Gerth, U.
Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis
Proc. Natl. Acad. Sci. USA
109
7451-7456
2012
Bacillus subtilis
brenda
Trentini, D.; Fuhrmann, J.; Mechtler, K.; Clausen, T.
Chasing phosphoarginine proteins: Development of a selective enrichment method using a phosphatase trap
Mol. Cell. Proteomics
13
1953-1964
2014
Bacillus subtilis (P37570), Bacillus subtilis, Bacillus subtilis 168 (P37570)
brenda
Schmidt, A.; Ammerer, G.; Mechtler, K.
Studying the fragmentation behavior of peptides with arginine phosphorylation and its influence on phospho-site localization
Proteomics
13
945-954
2013
Geobacillus stearothermophilus (P0DMM5)
brenda
Jung, H.; Choi, Y.; Lee, D.; Seo, J.K.; Kee, J.M.
Distinct phosphorylation and dephosphorylation dynamics of protein arginine kinases revealed by fluorescent activity probes
Chem. Commun. (Camb.)
55
7482-7485
2019
Geobacillus stearothermophilus (P0DMM5)
brenda
Lilge, L.; Reder, A.; Tippmann, F.; Morgenroth, F.; Grohmann, J.; Becher, D.; Riedel, K.; Voelker, U.; Hecker, M.; Gerth, U.
The involvement of the McsB arginine kinase in Clp-dependent degradation of the MgsR regulator in Bacillus subtilis
Front. Microbiol.
11
900
2020
Bacillus subtilis (P37570), Bacillus subtilis, Bacillus subtilis 168 (P37570)
brenda
Cai, H.; Huang, B.; Lin, R.; Xu, P.; Liu, Y.; Zhao, Y.
A turn-off SERS assay for kinase detection based on arginine N-phosphorylation process
Talanta
189
353-358
2018
Bacillus subtilis
brenda