CATH Domain 3mh4A02

CATH Classification

Level	CATH Code	Description
	2	Mainly Beta
	2.40	Beta Barrel
	2.40.10	Thrombin, subunit H
	2.40.10.10	Trypsin-like serine proteases

Domain Context

CATH Clusters

Superfamily	Trypsin-like serine proteases
Functional Family

Enzyme Information

3.4.21.107

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)

P0C0V0

DEGP_ECOLI

Escherichia coli K-12

Periplasmic serine endoprotease DegP

PDB Structure

PDB	3MH4
External Links	PDBSum Proteopedia
Method	X-RAY DIFFRACTION
Organism
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. Nat.Struct.Mol.Biol.