{PDOC00803}
{PS01046; LON_SER}
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* ATP-dependent serine proteases, lon family, serine active site *
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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.

-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.

-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.

[ 1] Thomas C.D., Modha J., Razzaq T.M., Cullis P.M., Rivett A.J.
     "Controlled high-level expression of the lon gene of Escherichia coli
     allows overproduction of Lon protease."
     Gene 136:237-242(1993).
     PubMed=8294008
[ 2] Tojo N., Inouye S., Komano T.
     "The lonD gene is homologous to the lon gene encoding an ATP-dependent
     protease and is essential for the development of Myxococcus xanthus."
     J. Bacteriol. 175:4545-4549(1993).
     PubMed=8331083
[ 3] van Dyck L., Pearce D.A., Sherman F.
     J. Biol. Chem. 269:238-242(1994).
[ 4] Wang N., Gottesman S., Willingham M.C., Gottesman M.M., Maurizi M.R.
     "A human mitochondrial ATP-dependent protease that is highly
     homologous to bacterial Lon protease."
     Proc. Natl. Acad. Sci. U.S.A. 90:11247-11251(1993).
     PubMed=8248235
[ 5] Fischer H., Glockshuber R.
     "ATP hydrolysis is not stoichiometrically linked with proteolysis in
     the ATP-dependent protease La from Escherichia coli."
     J. Biol. Chem. 268:22502-22507(1993).
     PubMed=8226758
[ 6] Rawlings N.D., Barrett A.J.
     "Families of serine peptidases."
     Methods Enzymol. 244:19-61(1994).
     PubMed=7845208
[E1] https://www.uniprot.org/docs/peptidas

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