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 | Periplasmic serine protease DegS |
Enzyme Information
| 3.4.21.107 |
Peptidase Do.
based on mapping to UniProt P0AEE3
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)
| P0AEE3 |
DEGS_ECOLI
Escherichia coli K-12
Serine endoprotease DegS
|
PDB Structure
| PDB | 3LGI |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Allostery is an intrinsic property of the protease domain of DegS: implications for enzyme function and evolution.
J.Biol.Chem.
|
