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PROSITE documentation PDOC51786 [for PROSITE entry PS51786]

Lon proteolytic domain profile





Description

Lon (also known as endopeptidase La, EC 3.4.21.53) 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.

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 https://prosite.expasy.org/prosite_license.html --------------------------------------------------------------------------------.

Last update:

December 2015 / First entry.

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Technical section

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

LON_PROTEOLYTIC, PS51786; Lon proteolytic domain profile  (MATRIX)


References

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
DOI10.1074/jbc.M312243200

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
DOI10.1074/jbc.M410437200

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
DOI10.1016/j.jmb.2005.06.008

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
DOI10.1038/emboj.2010.226

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
DOI10.1002/pro.376

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
DOI10.1111/febs.12740

E1Titlehttps://www.ebi.ac.uk/merops/cgi-bin/famsum?family=S16



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.

Miscellaneous

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