Literature summary for 3.9.1.2 extracted from

Schmidt, A.; Trentini, D.B.; Spiess, S.; Fuhrmann, J.; Ammerer, G.; Mechtler, K.; Clausen, T.
Quantitative phosphoproteomics reveals the role of protein arginine phosphorylation in the bacterial stress response (2014), Mol. Cell. Proteomics, 13, 537-550.

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Organism

Organism	UniProt	Comment	Textmining
Bacillus subtilis	P39155	-	-
Bacillus subtilis 168	P39155	-	-

General Information

General Information	Comment	Organism
physiological function	a mutant lacking the YwlE arginine phosphatase accumulates a strikingly large number of arginine phosphorylations i.e. 217 sites in 134 proteins, however only a minor fraction of these sites is increasingly modified during heat shock or oxidative stress. The main proteins accumulating comprise central factors of the stress response system including the CtsR and HrcA heat shock repressors, as well as major components of the protein quality control system such as the ClpCP protease and the GroEL chaperonine	Bacillus subtilis

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Release 2023.1 (January 2023)