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Information on EC 2.7.14.1 - protein arginine kinase and Organism(s) Bacillus subtilis and UniProt Accession P37570

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EC Tree
     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.14 Protein-arginine kinases
                2.7.14.1 protein arginine kinase
IUBMB Comments
The enzyme, characterized from Gram-positive bacteria, is involved in the regulation of the bacterial stress response.
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This record set is specific for:
Bacillus subtilis
UNIPROT: P37570
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Word Map
The taxonomic range for the selected organisms is: Bacillus subtilis
The enzyme appears in selected viruses and cellular organisms
Synonyms
protein arginine kinase, mcsb arginine kinase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
McsB arginine kinase
-
SYSTEMATIC NAME
IUBMB Comments
ATP:[protein]-L-arginine N?-phosphotransferase
The enzyme, characterized from Gram-positive bacteria, is involved in the regulation of the bacterial stress response.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + a [protein]-L-arginine
ADP + a [protein]-Nomega-phospho-L-arginine
show the reaction diagram
-
-
-
?
ATP + a [protein]-L-arginine
ADP + a [protein]-Nomega-phospho-L-arginine
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + a [protein]-L-arginine
ADP + a [protein]-Nomega-phospho-L-arginine
show the reaction diagram
-
-
-
?
ATP + a [protein]-L-arginine
ADP + a [protein]-Nomega-phospho-L-arginine
show the reaction diagram
-
protein arginine phosphorylation is a physiological significant protein modification in wild-type Bacillus subtilis cells
-
-
?
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
McsA
activator
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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 is a physiological significant protein modification in wild-type Bacillus subtilis cells
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team