InterPro domain: IPR030400

This entry represents the sedolisin domain.

Sedolisins (serine-carboxyl peptidases) are proteolytic enzymes whose foldressembles that of subtilisin; however they are considerably larger, with themature catalytic domains containing approximately 375 amino acids. Thedefining 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 acidresidue in the oxyanion hole. Sedolisins are acid-acting endopeptidases ortripeptidyl peptidases. They are widely distributed among archea, bacteria,fungi, slime mold, amoeba and animal kingdom including amphibians, fish andmammals. Sedolisins form peptidase family S53 of the subtilisin-like (SB) clan[ 1 , 2 , 3 ].

The three dimensional fold of sedolisin is based on a 7-stranded, all-parallelbeta-sheet. The sheet is flanked on both sides by several helices [ 4 ].

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.

1. Structural and enzymatic properties of the sedolisin family of serine-carboxyl peptidases. Acta Biochim. Pol. 50, 81-102
2. Evolution of prokaryotic subtilases: genome-wide analysis reveals novel subfamilies with different catalytic residues. Proteins 67, 681-94
3. New families of carboxyl peptidases: serine-carboxyl peptidases and glutamic peptidases. J. Biochem. 151, 13-25