EC Number   |
Natural Substrates |
|---|
   3.4.21.92 | more |
enzyme is required for the growth at elevated temperature and for virulence |
| 3.4.21.92 | antitoxin epsilon + H2O |
Epsilon is an antitoxin of the Epsilon/Zeta toxin-antitoxin system family, purified Zeta toxin protects the Epsilon protein from rapid ClpXP-catalyzed degradation |
| 3.4.21.92 | more |
physiological activation of Mu-dependent DNA rearrangements requires Clp functions. Clp plays a role in monitoring the physiological status of the cell |
| 3.4.21.92 | more |
removing of irreversibly damaged polypeptides |
| 3.4.21.92 | more |
selectivity of degradation by ClpP in vivo is determined by interaction of ClpP with different regulatory ATPase subunits |
| 3.4.21.92 | more |
stress- and starvation-induced bulk protein turnover depends virtually exclusively on enzyme, which is also essential for intracellular protein quality control |
| 3.4.21.92 | FixK2 + H2O |
substrate is a CRP-like transcription factor that controls the endosymbiotic lifestyle of Bradyrhizobium japonicum. Degradation occurs by the ClpAP1 chaperone-protease complex, but not by the ClpXP1 chaperone-protease complex, and is inhibited by the ClpS1 adaptor protein. The last 12 amino acids of FixK2 are recognized by ClpA |
| 3.4.21.92 | FlhC subunit + H2O + ATP |
subunit of the flagellar master transcriptional regulator complex, FlhD4C2. Flagellum-related protein FliT selectively increases ClpXP-dependent proteolysis of the FlhC subunit in the FlhD4C2 complex. FliT promotes the affinity of ClpX against FlhD4C2 complex, whereas FliT does not directly interact with ClpX. FliT interacts with the FlhC in FlhD4C2 complex and increases the presentation of the FlhC recognition region to ClpX. The DNA-bound form of FlhD4C2 complex is resistant to ClpXP proteolysis |
| 3.4.21.92 | Starvation proteins + H2O |
the ClpP proteolytic subunit plays a subtle but important role when cells are recovering from starvation. This enzyme is important in the selective degradation of starvation proteins when growth resumes |
| 3.4.21.92 | more |
the high degree of similarity among the ClpA-like proteins suggests that Clp-like proteases are likely to be important participants in energy-dependent proteolysis in prokaryotic and eukaryotic cells |
