PROSITE documentation PDOC51786
Lon proteolytic domain profile


Lon (also known as endopeptidase La, EC 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 (see <PDOC51787>) 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 [1,2,3,4,5,6]. The Lon proteolytic domain forms peptidase family S16 of clan SJ [3,E1].

The structure of the Lon proteolytic domain consists of six α helices and ten β strands (see <PDB:1RR9>) [1,2,3,4,5].

The profile we developed covers the entire Lon proteolytic domain.

Last update:

December 2015 / First entry.


Technical section

PROSITE method (with tools and information) covered by this documentation:

LON_PROTEOLYTIC, PS51786; Lon proteolytic domain profile  (MATRIX)


1AuthorsBotos I. Melnikov E.E. Cherry S. Tropea J.E. Khalatova A.G. Rasulova F. Dauter Z. Maurizi M.R. Rotanova T.V. Wlodawer A. Gustchina A.
TitleThe catalytic domain of Escherichia coli Lon protease has a unique fold and a Ser-Lys dyad in the active site.
SourceJ. Biol. Chem. 279:8140-8148(2004).
PubMed ID14665623

2AuthorsIm Y.J. Na Y. Kang G.B. Rho S.-H. Kim M.-K. Lee J.H. Chung C.H. Eom S.H.
TitleThe active site of a lon protease from Methanococcus jannaschii distinctly differs from the canonical catalytic Dyad of Lon proteases.
SourceJ. Biol. Chem. 279:53451-53457(2004).
PubMed ID15456757

3AuthorsBotos I. Melnikov E.E. Cherry S. Kozlov S. Makhovskaya O.V. Tropea J.E. Gustchina A. Rotanova T.V. Wlodawer A.
TitleAtomic-resolution crystal structure of the proteolytic domain of Archaeoglobus fulgidus lon reveals the conformational variability in the active sites of lon proteases.
SourceJ. Mol. Biol. 351:144-157(2005).
PubMed ID16002085

4AuthorsCha S.-S. An Y.J. Lee C.R. Lee H.S. Kim Y.-G. Kim S.J. Kwon K.K. De Donatis G.M. Lee J.-H. Maurizi M.R. Kang S.G.
TitleCrystal structure of Lon protease: molecular architecture of gated entry to a sequestered degradation chamber.
SourceEMBO J. 29:3520-3530(2010).
PubMed ID20834233

5AuthorsGarcia-Nafria J. Ondrovicova G. Blagova E. Levdikov V.M. Bauer J.A. Suzuki C.K. Kutejova E. Wilkinson A.J. Wilson K.S.
TitleStructure of the catalytic domain of the human mitochondrial Lon protease: proposed relation of oligomer formation and activity.
SourceProtein Sci. 19:987-999(2010).
PubMed ID20222013

6AuthorsAmbro L. Pevala V. Ondrovicova G. Bellova J. Kunova N. Kutejova E. Bauer J.
TitleMutations to a glycine loop in the catalytic site of human Lon changes its protease, peptidase and ATPase activities.
SourceFEBS J. 281:1784-1797(2014).
PubMed ID24520911


PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.


View entry in original PROSITE document format
View entry in raw text format (no links)