EC Number   |
Natural Substrates |
|---|
   3.4.25.2 | Arc + H2O |
N-terminal residues of Arc are important for HslUV degradation |
| 3.4.25.2 | DnaA204-protein + H2O |
the degradation of the DnaA204 protein contributes to the temperature sensitivity of the dna204 strain |
| 3.4.25.2 | lambda CI repressor ext1-lambdacIN-RSEYE + H2O |
- |
| 3.4.25.2 | more |
hslV and hslU are coregulated. It is possible that ATPase HslU and protease HslV are involved in an ATP/GTP-dependent protein metabolism |
| 3.4.25.2 | more |
ClpYQ plays a minor role in stress survival and is required for growth at high temperature of 45°C |
| 3.4.25.2 | more |
the GYVG motif of HslU is important in unfolding of natively folded proteins as well as in translocation of unfolded proteins for degradation by HslV in its inner chamber |
| 3.4.25.2 | more |
the HslUV complex is an assembly of heat shock locus gene products U and V. The formation of the complete complex is essential for the proteasome to carry out its biochemical and physiological role in the parasite, namely to degrade specific target proteins in an ATP-dependent chaperone assisted manner |
| 3.4.25.2 | more |
ClpQ and ClpY are two heat shock proteins |
| 3.4.25.2 | more |
in vivo, ClpYQ targets SulA, RcsA, RpoH, and TraJ molecules, identification of the molecular determinants required for the binding of its natural protein substrates by yeast two-hybrid analysis. Domain I of ClpY contains the residues, amino acids 137-150 of loop 1 and 175-209 of loop 2, double loops in domain I of ClpY, that are responsible for recognition of its natural substrates, while domain C is necessary to engage ClpQ, overview |
| 3.4.25.2 | more |
HslU hexamers recognize and unfold native protein substrates and then translocate the polypeptide into the degradation chamber of the HslV peptidase. The degradation appears to consist of discrete steps, which involve the interaction of different terminal sequence signals in the substrate with different receptor sites in the HslUV protease. Mutations in the unstructured N-terminal and C-terminal sequences of two model substrates alter HslUV recognition and degradation kinetics, including changes in Vmax. Blocking either terminus of the substrate interferes with HslUV degradation, with synergistic effects when both termini are obstructed |
