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CATH Superfamily 2.40.10.10

Trypsin-like serine proteases

The name of this superfamily has been modified since the most recent official CATH+ release (v4_2_0). At the point of the last release, this superfamily was named:

"
Trypsin-like serine proteases
".

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 14679: Serine protease Do-like HtrB

There are 1 EC terms in this cluster

Please note: EC annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

Note: The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.

EC Term Annotations Evidence
Peptidase Do. [EC: 3.4.21.107]
Acts on substrates that are at least partially unfolded. The cleavage site P1 residue is normally between a pair of hydrophobic residues, such as Val-|-Val.
  • This serine endopeptidase is essential for the clearance of denatured or aggregated proteins from the inner-membrane and periplasmic space in Escherichia coli.
  • Natural substrates of the enzyme include colicin A lysis protein, pilin subunits and MalS from E.coli.
  • The enzyme has weak peptidase activity with casein and other non- native substrates.
  • The peptidase acts as a chaperone at low temperatures but switches to a peptidase (heat shock protein) at higher temperatures.
  • Molecular chaperones and peptidases control the folded state of proteins by recognizing hydrophobic stretches of polypeptide that become exposed by misfolding or unfolding.
  • They then bind these hydrophobic substrates to prevent aggregation or assist in protein refolding.
  • If attempts at refolding fail, then irreversibly damaged proteins are degraded by peptidases such as this enzyme.
  • Belongs to peptidase family S1B.
 10 A0A0K6K2Y7 A0A0K6M6H4 A0A0M0KTB9 A0A164TQN9 A0A1B2AZE0 A0A1G4LET9 G4ERE0 G4P0K0 L8ATW0 Q9R9I1