EC Number   |
General Information |
Reference |
|---|
   3.4.21.92 | physiological function |
adaptor protein MecA specifically interacts with both central competence regulator sigmax and protease ClpC, suggesting the formation of a ternary sigmaX-MecA-ClpC complex. MecA ultimately targets sigmaX for its degradation by the ClpCP protease in an ATP-dependent manner. A short sequence of 18 amino acids in the N-terminal domain of sigmaX is essential for the interaction with MecA and subsequent sigmaX degradation. Increased transformability of a MecA-deficient strain in the presence of subinducing SigX-inducing peptide concentrations suggests that the MecA-ClpCP proteolytic complex acts as an additional locking device to prevent competence under inappropriate conditions |
-, 732009 |
| 3.4.21.92 | physiological function |
arginine-phosphate and arginine-phosphorylated proteins bind to subunit ClpC1 N-terminal domain and induce millisecond dynamics. These dynamics are caused by conformational changes and do not result from unfolding or oligomerization of this domain |
754176 |
| 3.4.21.92 | physiological function |
Azotobacter vinelandii carries a duplicated copy of the ATPase component of the ubiquitous ClpXP protease (ClpX2), which is induced under nitrogen fixing conditions. Inactivation of clpX2 results in the accumulation of NifB and NifEN and a defect in diazotrophic growth, especially when iron is in short supply |
718131 |
| 3.4.21.92 | physiological function |
both protein and small-molecule activators of ClpP allosterically control the ClpP barrel conformation. Acyldepsipeptides in addition to opening the axial pore directly stimulate ClpP activity through cooperative binding. ClpP activation thus reaches beyond active site accessibility and also involves conformational control of the catalytic residues. Substoichiometric amounts of acyldepsipeptide potently prevent binding of ClpX to ClpP and, at the same time, partially inhibit ClpP through conformational perturbance. The hydrophobic binding pocket is a major conformational regulatory site with implications for both ClpXP proteolysis and acyldepsipeptide -based anti-bacterial activity |
-, 732563 |
| 3.4.21.92 | physiological function |
Clp chaperones ClpX and ClpC1 require the intact interaction face of subunit ClpP2 to support degradation. Binding results in an asymmetric complex where chaperones only bind to the ClpP2 side of the proteolytic core |
755086 |
| 3.4.21.92 | physiological function |
ClpC1 is involved in Fe homeostasis in leaves |
717092 |
| 3.4.21.92 | physiological function |
ClpC1-catalyzed unfolding of an SsrA-tagged protein is negatively impacted by association with the ClpS adaptor protein. ClpS-dependent inhibition of ClpC1-catalyzed SsrA-dependent protein unfolding does not require the ClpC1 N-terminal domain but instead requires the presence of an interaction surface located in the ClpC1 middle domain |
-, 753915 |
| 3.4.21.92 | physiological function |
ClpP enhances the unfolding activity of ClpX |
717472 |
| 3.4.21.92 | physiological function |
ClpXP positively regulates T3SS through RpoS degradation. In addition to the regulation of T3SS, ClpXP protease, RssB, and RpoS play a role in pectinolytic enzyme production and virulence of Dickeya dadantii |
718140 |
| 3.4.21.92 | physiological function |
ClpXP protease consists of the ClpX hexamer and the ClpP peptidase. Small-molecule acyldepsipeptides such as ADEP-2B compete with the IGF loops of ClpX for ClpP-cleft binding and cause exceptionally rapid dissociation of otherwise stable ClpXP complexes, suggesting that the IGF-loop interactions with ClpP must be highly dynamic |
752357 |
