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	central competence regulator sigmax + H2O	adaptor protein MecA ultimately targets sigmaX for its degradation by the ClpCP protease in an ATP-dependent manner	
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	additional information	-	
3.4.21.92	additional information	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	additional information	ClpXP appears to be involved in plasmid maintenance and in phage Mu virulence	
3.4.21.92	additional information	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	
3.4.21.92	additional information	selectivity of degradation by ClpP in vivo is determined by interaction of ClpP with different regulatory ATPase subunits	
3.4.21.92	additional information	ClpP is present in a wide range of prokaryotic and eukaryotic cells and is highly conserved in plant chloroplasts	
3.4.21.92	additional information	ClpP linked to many activities, including sporulation, cell competence, stress tolerance and regulation of gene expression	
3.4.21.92	additional information	removing of irreversibly damaged polypeptides	
3.4.21.92	additional information	enzyme complex ClpPRS consisting of five ClpP protease molecules, four nonproteolytic ClpR molecules, and two associated ClpS molecules, is central to chloroplast biogenesis, thylakoid protein homeostasis, and plant development	
3.4.21.92	additional information	enzyme is required for release of autolysin A and pneumolysin. In vivo, it is required for growth of pneumococcus in the lungs and blood in a murine model of disease	
3.4.21.92	additional information	enzyme is required for the growth at elevated temperature and for virulence	
3.4.21.92	additional information	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	additional information	ClpP associates with ClpX or ClpA to form the AAA+ ClpXP or ClpAP proteases	
3.4.21.92	additional information	ClpP binds to AAA+ ATPase/unfoldase, ClpA or ClpX	
3.4.21.92	additional information	ClpP requires association with ClpA or ClpX to unfold and thread protein substrates through the axial pore into the inner chamber where degradation occurs	
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