Peptidase S16, Lon proteolytic domain (IPR008269)

Short name: Lon_proteolytic

Overlapping homologous superfamilies

Domain relationships



Lon (also known as endopeptidase La) is a multi-domain ATP- dependent protease found throughout all kingdoms of life. It is involved in protein quality control and several regulatory processes. All Lon proteases contain an ATPase domain belonging to the AAA+ superfamily of molecular machines, and a proteolytic domain with a serine-lysine catalytic dyad in which a lysine assists the catalytic serine in proteolytic cleavage. Lon proteases can be divided into two subfamilies: A type (A-Lons), which have a large multi-lobed N-terminal domain together with the ATPase and 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 in Archaea, in which they are the lone membrane-anchored ATP-dependent protease. The soluble A-Lons are found in all bacteria and in eukaryotic cell organelles, such as mitochondria and peroxisomes, and are needed for recovery from various stress conditions [PMID: 14665623, PMID: 15456757, PMID: 16002085, PMID: 20834233, PMID: 20222013, PMID: 24520911]. The Lon proteolytic domain forms peptidase family S16 of clan SJ [PMID: 16002085].

The structure of the Lon proteolytic domain consists of six alpha helices and ten beta strands [PMID: 14665623, PMID: 15456757, PMID: 16002085, PMID: 20834233, PMID: 20222013].

GO terms

Biological Process

GO:0006508 proteolysis

Molecular Function

GO:0004176 ATP-dependent peptidase activity
GO:0004252 serine-type endopeptidase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE profiles