EC Number   |
General Information |
Reference |
|---|
   3.4.21.92 | physiological function |
a mutant strain lacking the N-terminal domain of ClpX is not viable |
732530 |
| 3.4.21.92 | malfunction |
a point mutation from G to A at nucleotide 2317 of ClpC1 on chromosome V of Arabidopsis is responsible for the irm1 phenotype (typical Fe-deficiency chlorosis) |
717092 |
| 3.4.21.92 | physiological function |
accessory proteins ClpT1 and ClpT2 regulate the assembly of the Clp proteolytic core in vascular plants |
718212 |
| 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 | malfunction |
both FlhD and FlhC regulator proteins accumulate markedly following ClpXP depletion, and their half-lives are significantly longer in the mutant cells |
718089 |
| 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 |
