Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.4.21.92 extracted from

  • Trentini, D.B.; Suskiewicz, M.J.; Heuck, A.; Kurzbauer, R.; Deszcz, L.; Mechtler, K.; Clausen, T.
    Arginine phosphorylation marks proteins for degradation by a Clp protease (2016), Nature, 539, 48-53 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.21.92

Protein Variants

Protein Variants Comment Organism
S98A inactive trapping variant Bacillus subtilis

Inhibitors

Inhibitors Comment Organism Structure
phosphoarginine
-
 Bacillus subtilis

Organism

Organism UniProt Comment Textmining
Bacillus subtilis P80244 proteolytic subunit ClpP
-
Bacillus subtilis 168 P80244 proteolytic subunit ClpP
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
beta-casein + H2O
-
 Bacillus subtilis ?
-
 ?
beta-casein + H2O
-
 Bacillus subtilis 168 ?
-
 ?
additional information after phosphorylation by the McsB arginine kinase, phosphoarginine-tagged proteins are targeted to the ClpCP protease. Binding of phophoarginine proteins to one of the 12 N-terminal domain binding pockets stimulates the ATPase activity of ClpC, leading to the translocation of the captured substrate into the ClpP protease cage and to protein degradation Bacillus subtilis ?
-
 ?
additional information after phosphorylation by the McsB arginine kinase, phosphoarginine-tagged proteins are targeted to the ClpCP protease. Binding of phophoarginine proteins to one of the 12 N-terminal domain binding pockets stimulates the ATPase activity of ClpC, leading to the translocation of the captured substrate into the ClpP protease cage and to protein degradation Bacillus subtilis 168 ?
-
 ?

Synonyms

Synonyms Comment Organism
ClpC
-
 Bacillus subtilis
ClpP
-
 Bacillus subtilis

General Information

General Information Comment Organism
physiological function proteins phosphorylated on arginine residues are selectively targeted to ClpC-ClpP. Arginine phosphorylation by the McsB kinase is required and sufficient for the degradation of substrate proteins. The ClpCP protease complex alone is not active. The docking site for phosphoarginine is located in the amino-terminal domain of the ClpC ATPase Bacillus subtilis