Protein Variants | Comment | Organism |
---|---|---|
R86G | ATP inhibits the degradation of unfolded proteins by HslV. This inhibitory effect of ATP is markedly diminished by substitution of the Arg86 residue located in the apical pore of HslV with Gly | Escherichia coli |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
ATP | inhibits the degradation of unfolded proteins by HslV | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
unfolded lactalbumin + H2O | HslV alone can efficiently degrade certain unfolded proteins, such as unfolded lactalbumin and lysozyme prepared by complete reduction of disulfide bonds, but not their native forms. HslV alone cleaves a lactalbumin fragment sandwiched by two thioredoxin molecules, indicating that it can hydrolyze the internal peptide bonds of lactalbumin. Uncomplexed HslV is inactive under normal conditions, but can degrade unfolded proteins when the ATP level is low, as it is during carbon starvation | Escherichia coli | ? | - |
? | |
unfolded lysozyme + H2O | HslV alone can efficiently degrade certain unfolded proteins, such as unfolded lactalbumin and lysozyme prepared by complete reduction of disulfide bonds, but not their native forms. HslV alone cleaved a lactalbumin fragment sandwiched by two thioredoxin molecules, indicating that it can hydrolyze the internal peptide bonds of lactalbumin. Uncomplexed HslV is inactive under normal conditions, but can degrade unfolded proteins when the ATP level is low, as it is during carbon starvation | Escherichia coli | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
hslVU | ATP-dependent protease consisting of two heat shock proteins, the HslU ATPase and HslV peptidase | Escherichia coli |