Home  |  Contact
PROSITE documentation PDOC00803

ATP-dependent serine proteases, lon family, serine active site





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.

Technical section

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

LON_SER, PS01046; ATP-dependent serine proteases, lon family, serine active site  (PATTERN)


References

1AuthorsThomas C.D. Modha J. Razzaq T.M. Cullis P.M. Rivett A.J.
TitleControlled high-level expression of the lon gene of Escherichia coli allows overproduction of Lon protease.
SourceGene 136:237-242(1993).
PubMed ID8294008

2AuthorsTojo N. Inouye S. Komano T.
TitleThe lonD gene is homologous to the lon gene encoding an ATP-dependent protease and is essential for the development of Myxococcus xanthus.
SourceJ. Bacteriol. 175:4545-4549(1993).
PubMed ID8331083

3Authorsvan Dyck L. Pearce D.A. Sherman F.
SourceJ. Biol. Chem. 269:238-242(1994).

4AuthorsWang N. Gottesman S. Willingham M.C. Gottesman M.M. Maurizi M.R.
TitleA human mitochondrial ATP-dependent protease that is highly homologous to bacterial Lon protease.
SourceProc. Natl. Acad. Sci. U.S.A. 90:11247-11251(1993).
PubMed ID8248235

5AuthorsFischer H. Glockshuber R.
TitleATP hydrolysis is not stoichiometrically linked with proteolysis in the ATP-dependent protease La from Escherichia coli.
SourceJ. Biol. Chem. 268:22502-22507(1993).
PubMed ID8226758

6AuthorsRawlings N.D. Barrett A.J.
TitleFamilies of serine peptidases.
SourceMethods Enzymol. 244:19-61(1994).
PubMed ID7845208

E1Titlehttps://www.uniprot.org/docs/peptidas



PROSITE is copyright. It is produced by the SIB Swiss Institute Bioinformatics. There are no restrictions on its use by non-profit institutions as long as its content is in no way modified. Usage by and for commercial entities requires a license agreement. For information about the licensing scheme send an email to
Prosite License or see: prosite_license.html.

Miscellaneous

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