EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
3.4.21.92 | S98A | inactive trapping variant | Bacillus subtilis |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
3.4.21.92 | phosphoarginine | - |
Bacillus subtilis |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.4.21.92 | Bacillus subtilis | P80244 | proteolytic subunit ClpP | - |
3.4.21.92 | Bacillus subtilis 168 | P80244 | proteolytic subunit ClpP | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.4.21.92 | beta-casein + H2O | - |
Bacillus subtilis | ? | - |
? | |
3.4.21.92 | beta-casein + H2O | - |
Bacillus subtilis 168 | ? | - |
? | |
3.4.21.92 | 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 | ? | - |
? | |
3.4.21.92 | 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 | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.4.21.92 | ClpC | - |
Bacillus subtilis |
3.4.21.92 | ClpP | - |
Bacillus subtilis |
EC Number | General Information | Comment | Organism |
---|---|---|---|
3.4.21.92 | 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 |