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Results 1 - 10 of 20 > >>
EC Number Natural Substrates Commentary (Nat. Sub.)
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.92antitoxin 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
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.92central competence regulator sigmax + H2O adaptor protein MecA ultimately targets sigmaX for its degradation by the ClpCP protease in an ATP-dependent manner
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.92FixK2 + 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
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.92FlhC 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
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.92more -
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.92more physiological activation of Mu-dependent DNA rearrangements requires Clp functions. Clp plays a role in monitoring the physiological status of the cell
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.92more ClpXP appears to be involved in plasmid maintenance and in phage Mu virulence
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.92more 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
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.92more selectivity of degradation by ClpP in vivo is determined by interaction of ClpP with different regulatory ATPase subunits
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.92more ClpP is present in a wide range of prokaryotic and eukaryotic cells and is highly conserved in plant chloroplasts
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