PROSITE logo
Black ribbon
We are deeply saddened by the passing of Amos Bairoch (1957–2025), the creator of PROSITE. We wish to dedicate our latest paper, published shortly before his death, to him. He will always be a source of inspiration to us.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
Amos Bairoch

PROSITE documentation PDOC00803
ATP-dependent serine proteases, lon family, serine active site


View entry in original PROSITE document format
View entry in raw text format (no links)
PURL: https://purl.expasy.org/prosite/documentation/PDOC00803

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 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.