{PDOC51695}
{PS51695; SEDOLISIN}
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* Sedolisin domain profile *
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Sedolisins (serine-carboxyl  peptidases)  are  proteolytic  enzymes whose fold
ressembles that  of subtilisin; however they are considerably larger, with the
mature catalytic   domains  containing  approximately  375  amino  acids.  The
defining features  of  these enzymes are a unique catalytic triad, Ser-Glu-Asp
(SED in  single-letter  notation), as well as the presence of an aspartic acid
residue in  the  oxyanion  hole.  Sedolisins are acid-acting endopeptidases or
tripeptidyl peptidases.  They  are  widely distributed among archea, bacteria,
fungi, slime  mold,  amoeba  and animal kingdom including amphibians, fish and
mammals. Sedolisins form peptidase family S53 of the subtilisin-like (SB) clan
[1,2,3,E1].

The three dimensional fold of sedolisin is based on a 7-stranded, all-parallel
beta-sheet. The  sheet  is  flanked  on  both  sides  by  several helices (see
<PDB:1GA6>) [1].

Some proteins known to contain a sedolisin domain are listed below:

 - Pseudomonas sedolisin.
 - Xanthomonas sp. Xanthomonalisin.
 - Bacterial kumamolisin.
 - Aspergillus oryzae aorsin.
 - Fungal   sedolisin-B,   a  secreted  tripeptidyl-peptidase  which  degrades
   proteins at acidic pHs and is involved in virulence.
 - Mammalian  lysosomal  tripeptidyl-peptidase  1 (TPP-1) or CLN2, involved in
   hydrolysis of  hydrophobic proteins. A hereditary deficiency of human TPP-1
   results in  infantile  neuronal  ceroid  lipofuscinosis (Batten disease), a
   rare but fatal neurodegenerative disorder.

The profile we developed covers the entire sedolisin domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: November 2013 / First entry.

[ 1] Wlodawer A., Li M., Gustchina A., Oyama H., Dunn B.M., Oda K.
     "Structural and enzymatic properties of the sedolisin family of
     serine-carboxyl peptidases."
     Acta Biochim. Pol. 50:81-102(2003).
     PubMed=12673349
[ 2] Siezen R.J., Renckens B., Boekhorst J.
     "Evolution of prokaryotic subtilases: genome-wide analysis reveals
     novel subfamilies with different catalytic residues."
     Proteins 67:681-694(2007).
     PubMed=17348030; DOI=10.1002/prot.21290
[ 3] Oda K.
     "New families of carboxyl peptidases: serine-carboxyl peptidases and
     glutamic peptidases."
     J. Biochem. 151:13-25(2012).
     PubMed=22016395; DOI=10.1093/jb/mvr129
[E1] https://www.ebi.ac.uk/merops/cgi-bin/famsum?family=S53

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