v5.1.0.3
Glycine data from LIS
Type | Domain |
Description | Lon (also known as endopeptidase La) is a multi-domain ATP- dependent protease found throughout all kingdoms of life. It is involved inprotein quality control and several regulatory processes. All Lon proteases contain an ATPase domain belonging to the AAA+ superfamily of molecularmachines, and a proteolytic domain with a serine-lysine catalytic dyad in which a lysine assists the catalytic serine in proteolytic cleavage. Lonproteases can be divided into two subfamilies: A type (A-Lons), which have a large multi-lobed N-terminal domain together with the ATPaseand protease domains, and B type (B-Lons), which lack an N domain, but have a membrane-anchoring region emerging from the ATPase domain. B-Lons are found inArchaea, in which they are the lone membrane-anchored ATP-dependent protease. The soluble A-Lons are found in all bacteria and in eukaryotic cellorganelles, such as mitochondria and peroxisomes, and are needed for recovery from various stress conditions [, , , , , ]. The Lon proteolytic domain formspeptidase family S16 of clan SJ [ ].The structure of the Lon proteolytic domain consists of six alpha helices and ten beta strands [, , , , ]. |
Short Name | Lon_proteolytic |