CATH Classification

Domain Context

CATH Clusters

Functional Family Periplasmic serine protease Do

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.
HtrA2 peptidase.
based on mapping to UniProt P0C0V0
Cleavage of non-polar aliphatic amino-acids at the P1 position, with a preference for Val, Ile and Met. At the P2 and P3 positions, Arg is selected most strongly with a secondary preference for other hydrophilic residues.
-!- Up-regulated in mammalian cells in response to stress induced by both heat shock and tunicamycin treatment. -!- Can induce apoptosis in a caspase-independent manner through its peptidase activity and in a caspase-dependent manner by disrupting the interaction between caspase and the inhibitor of apoptosis (IAP). -!- Belongs to peptidase family S1B.
Serine endopeptidases.
based on mapping to UniProt P0C0V0

UniProtKB Entries (1)

Escherichia coli K-12
Periplasmic serine endoprotease DegP

PDB Structure

External Links
Organism Escherichia
Primary Citation
Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine.
Krojer, T., Garrido-Franco, M., Huber, R., Ehrmann, M., Clausen, T.