Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. The complex has been shown to be involved in the specific degradation of heat shock induced transcription factors such as RpoH and SulA. In addition, small hydrophobic peptides are also hydrolyzed by HslV. HslV has weak protease activity even in the absence of HslU, but this activity is induced more than 100-fold in the presence of HslU. HslU recognizes protein substrates and unfolds these before guiding them to HslV for hydrolysis. HslV is not believed to degrade folded proteins. ATP-dependent cleavage of peptide bonds with broad specificity. Allosterically activated by HslU binding. Arc is a repressor protein, Arc-MYL-st11 is a hyperstable variant of Arc. Optimum temperature is 55 degrees Celsius. A double ring-shaped homohexamer of HslV is capped on each side by a ring-shaped HslU homohexamer. The assembly of the HslU/HslV complex is dependent on binding of ATP. By heat shock. Belongs to the peptidase T1B family. HslV subfamily. PubMed:9013898 sequence is supposed to originate from rat but, based on sequence similarity, it seems that this is a case of bacterial contamination from E.coli.