{PDOC51786}
{PS51786; LON_PROTEOLYTIC}
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* Lon proteolytic domain profile *
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Lon (also  known  as  endopeptidase  La,  EC 3.4.21.53) is a multi-domain ATP-
dependent protease  found  throughout  all kingdoms of life. It is involved in
protein quality  control  and  several regulatory processes. All Lon proteases
contain an  ATPase  domain  belonging  to  the  AAA+  superfamily of molecular
machines, and  a  proteolytic  domain  with  a serine-lysine catalytic dyad in
which a  lysine  assists  the  catalytic  serine  in proteolytic cleavage. Lon
proteases can  be  divided into two subfamilies: A type (A-Lons), which have a
large multi-lobed N-terminal domain (see <PDOC51787>) together with the ATPase
and protease  domains, and B type (B-Lons), which lack an N domain, but have a
membrane-anchoring region emerging from the ATPase domain. B-Lons are found in
Archaea, in  which they are the lone membrane-anchored ATP-dependent protease.
The soluble   A-Lons  are  found  in  all  bacteria  and  in  eukaryotic  cell
organelles, such  as mitochondria and peroxisomes, and are needed for recovery
from various stress conditions [1,2,3,4,5,6]. The Lon proteolytic domain forms
peptidase family S16 of clan SJ [3,E1].

The structure  of the Lon proteolytic domain consists of six alpha helices and
ten beta strands (see <PDB:1RR9>) [1,2,3,4,5].

The profile we developed covers the entire Lon proteolytic domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: December 2015 / First entry.

[ 1] Botos I., Melnikov E.E., Cherry S., Tropea J.E., Khalatova A.G.,
     Rasulova F., Dauter Z., Maurizi M.R., Rotanova T.V., Wlodawer A.,
     Gustchina A.
     "The catalytic domain of Escherichia coli Lon protease has a unique
     fold and a Ser-Lys dyad in the active site."
     J. Biol. Chem. 279:8140-8148(2004).
     PubMed=14665623; DOI=10.1074/jbc.M312243200
[ 2] Im Y.J., Na Y., Kang G.B., Rho S.-H., Kim M.-K., Lee J.H., Chung C.H.,
     Eom S.H.
     "The active site of a lon protease from Methanococcus jannaschii
     distinctly differs from the canonical catalytic Dyad of Lon
     proteases."
     J. Biol. Chem. 279:53451-53457(2004).
     PubMed=15456757; DOI=10.1074/jbc.M410437200
[ 3] Botos I., Melnikov E.E., Cherry S., Kozlov S., Makhovskaya O.V.,
     Tropea J.E., Gustchina A., Rotanova T.V., Wlodawer A.
     "Atomic-resolution crystal structure of the proteolytic domain of
     Archaeoglobus fulgidus lon reveals the conformational variability in
     the active sites of lon proteases."
     J. Mol. Biol. 351:144-157(2005).
     PubMed=16002085; DOI=10.1016/j.jmb.2005.06.008
[ 4] Cha S.-S., An Y.J., Lee C.R., Lee H.S., Kim Y.-G., Kim S.J., Kwon K.K.,
     De Donatis G.M., Lee J.-H., Maurizi M.R., Kang S.G.
     "Crystal structure of Lon protease: molecular architecture of gated
     entry to a sequestered degradation chamber."
     EMBO J. 29:3520-3530(2010).
     PubMed=20834233; DOI=10.1038/emboj.2010.226
[ 5] Garcia-Nafria J., Ondrovicova G., Blagova E., Levdikov V.M.,
     Bauer J.A., Suzuki C.K., Kutejova E., Wilkinson A.J., Wilson K.S.
     "Structure of the catalytic domain of the human mitochondrial Lon
     protease: proposed relation of oligomer formation and activity."
     Protein Sci. 19:987-999(2010).
     PubMed=20222013; DOI=10.1002/pro.376
[ 6] Ambro L., Pevala V., Ondrovicova G., Bellova J., Kunova N.,
     Kutejova E., Bauer J.
     "Mutations to a glycine loop in the catalytic site of human Lon
     changes its protease, peptidase and ATPase activities."
     FEBS J. 281:1784-1797(2014).
     PubMed=24520911; DOI=10.1111/febs.12740
[E1] https://www.ebi.ac.uk/merops/cgi-bin/famsum?family=S16

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