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| 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) |
| Consensus pattern: |
D-G-[PD]-S-A-[GS]-[LIVMCA]-[TA]-[LIVM]
S is the active site residue |
| Sequences known to belong to this class detected by the pattern: |
ALL |
| Other sequence(s) detected in Swiss-Prot: |
NONE. |
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| Matching PDB structures:
2X36 [ALL] |
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 |
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