CATH Classification

Domain Context

CATH Clusters

Functional Family Periplasmic serine endoprotease DegP-like

Enzyme Information
Peptidase Do.
based on mapping to UniProt P0C0V0
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.

UniProtKB Entries (1)

Escherichia coli K-12
Periplasmic serine endoprotease DegP

PDB Structure

External Links
Primary Citation
HtrA proteases have a conserved activation mechanism that can be triggered by distinct molecular cues
Krojer, T., Sawa, J., Huber, R., Clausen, T.