PROSITE documentation PDOC51786 [for PROSITE entry PS51786]Lon proteolytic domain profile
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.
Last update:December 2015 / First entry.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Botos 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. |
| Title | The catalytic domain of Escherichia coli Lon protease has a unique fold and a Ser-Lys dyad in the active site. | |
| Source | J. Biol. Chem. 279:8140-8148(2004). | |
| PubMed ID | 14665623 | |
| DOI | 10.1074/jbc.M312243200 |
| 2 | Authors | Im Y.J. Na Y. Kang G.B. Rho S.-H. Kim M.-K. Lee J.H. Chung C.H. Eom S.H. |
| Title | The active site of a lon protease from Methanococcus jannaschii distinctly differs from the canonical catalytic Dyad of Lon proteases. | |
| Source | J. Biol. Chem. 279:53451-53457(2004). | |
| PubMed ID | 15456757 | |
| DOI | 10.1074/jbc.M410437200 |
| 3 | Authors | Botos I. Melnikov E.E. Cherry S. Kozlov S. Makhovskaya O.V. Tropea J.E. Gustchina A. Rotanova T.V. Wlodawer A. |
| Title | Atomic-resolution crystal structure of the proteolytic domain of Archaeoglobus fulgidus lon reveals the conformational variability in the active sites of lon proteases. | |
| Source | J. Mol. Biol. 351:144-157(2005). | |
| PubMed ID | 16002085 | |
| DOI | 10.1016/j.jmb.2005.06.008 |
| 4 | Authors | Cha 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. |
| Title | Crystal structure of Lon protease: molecular architecture of gated entry to a sequestered degradation chamber. | |
| Source | EMBO J. 29:3520-3530(2010). | |
| PubMed ID | 20834233 | |
| DOI | 10.1038/emboj.2010.226 |
| 5 | Authors | Garcia-Nafria J. Ondrovicova G. Blagova E. Levdikov V.M. Bauer J.A. Suzuki C.K. Kutejova E. Wilkinson A.J. Wilson K.S. |
| Title | Structure of the catalytic domain of the human mitochondrial Lon protease: proposed relation of oligomer formation and activity. | |
| Source | Protein Sci. 19:987-999(2010). | |
| PubMed ID | 20222013 | |
| DOI | 10.1002/pro.376 |
| 6 | Authors | Ambro L. Pevala V. Ondrovicova G. Bellova J. Kunova N. Kutejova E. Bauer J. |
| Title | Mutations to a glycine loop in the catalytic site of human Lon changes its protease, peptidase and ATPase activities. | |
| Source | FEBS J. 281:1784-1797(2014). | |
| PubMed ID | 24520911 | |
| DOI | 10.1111/febs.12740 |
| E1 | Title | https://www.ebi.ac.uk/merops/cgi-bin/famsum?family=S16 |
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