Proteasome endopeptidase complex
Definition:
EC Tree > 3 Hydrolases > 3.4 Acting on peptide bonds (peptidases) > 3.4.25 Threonine endopeptidases > 3.4.25.1 proteasome endopeptidase complex
HslU-HslV peptidase is an ATP-dependent bacterial proteasome-like complex in peptidase family T1, found in bacteria and eukaryotes. The HslU subunit is an ATP-dependent unfoldase; ATP binding and hydrolysis by HslU are essential to unfold protein substrates that are subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of substrates and unfolds them before threading into HslV. It cleaves peptide bonds with broad specificity in an ATP-dependent manner. In bacteria it performs protein quality control. It features an HslV threonine-protease chamber capped by HslU AAA+ unfoldase rings.
HslU-HslV peptidase is an ATP-dependent bacterial proteasome-like complex in peptidase family T1, found in bacteria and eukaryotes. The HslU subunit is an ATP-dependent unfoldase; ATP binding and hydrolysis by HslU are essential to unfold protein substrates that are subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of substrates and unfolds them before threading into HslV. It cleaves peptide bonds with broad specificity in an ATP-dependent manner. In bacteria it performs protein quality control. It features an HslV threonine-protease chamber capped by HslU AAA+ unfoldase rings.
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