PROSITE documentation PDOC00803ATP-dependent serine proteases, lon family, serine active site
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Description
The following proteins belongs to a family of proteases which are dependent on the hydrolysis of ATP for their activity and which have a serine in their active site:
- Bacterial ATP-dependent proteases [1,2]. The prototype of those bacterial enzymes is the Escherichia coli La protease (EC 3.4.21.53) (gene lon). La is capable of hydrolyzing large proteins; it degrades short-lived regulatory (such as rcsA and sulA) and abnormal proteins. It is a cytoplasmic protein of 87 Kd that associates as an homotetramer. Its proteolytic activity is stimulated by single-stranded DNA.
- Eukaryotic mitochondrial matrix proteases [3,4]. The prototype of these enzymes is the yeast PIM1 protease. It is a mitochondrial matrix protein of 120 Kd that associated as an homohexamer. It catalyzes the initial step of mitochondrial protein degradation.
- Haemophilus influenzae lon-B (HI1324), a protein which does not contain the ATP-binding domain, but possess a slightly divergent form of the catalytic domain.
The region around the serine residue involved in the catalytic mechanism [5] is perfectly conserved and can be used as a signature pattern.
Note:Proteins belonging to this family also contain a copy of the ATP/GTP- binding motif 'A' (P-loop) (see <PDOC00017>).
Note:These proteins belong to family S16 in the classification of peptidases [6,E1].
Last update:November 1995 / First entry.
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References
| 1 | Authors | Thomas C.D. Modha J. Razzaq T.M. Cullis P.M. Rivett A.J. |
| Title | Controlled high-level expression of the lon gene of Escherichia coli allows overproduction of Lon protease. | |
| Source | Gene 136:237-242(1993). | |
| PubMed ID | 8294008 |
| 2 | Authors | Tojo N. Inouye S. Komano T. |
| Title | The lonD gene is homologous to the lon gene encoding an ATP-dependent protease and is essential for the development of Myxococcus xanthus. | |
| Source | J. Bacteriol. 175:4545-4549(1993). | |
| PubMed ID | 8331083 |
| 3 | Authors | van Dyck L. Pearce D.A. Sherman F. |
| Source | J. Biol. Chem. 269:238-242(1994). |
| 4 | Authors | Wang N. Gottesman S. Willingham M.C. Gottesman M.M. Maurizi M.R. |
| Title | A human mitochondrial ATP-dependent protease that is highly homologous to bacterial Lon protease. | |
| Source | Proc. Natl. Acad. Sci. U.S.A. 90:11247-11251(1993). | |
| PubMed ID | 8248235 |
| 5 | Authors | Fischer H. Glockshuber R. |
| Title | ATP hydrolysis is not stoichiometrically linked with proteolysis in the ATP-dependent protease La from Escherichia coli. | |
| Source | J. Biol. Chem. 268:22502-22507(1993). | |
| PubMed ID | 8226758 |
| 6 | Authors | Rawlings N.D. Barrett A.J. |
| Title | Families of serine peptidases. | |
| Source | Methods Enzymol. 244:19-61(1994). | |
| PubMed ID | 7845208 |
| E1 | Title | https://www.uniprot.org/docs/peptidas |
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