| Predicate | Object |
|---|---|
| rdf:type | |
| rdfs:comment |
Belongs to peptidase family S1B.,
If attempts at refolding fail, then irreversibly damaged proteins are degraded by peptidases such as this enzyme.,
Molecular chaperones and peptidases control the folded state of proteins by recognizing hydrophobic stretches of polypeptide that become exposed by misfolding or unfolding.,
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.,
They then bind these hydrophobic substrates to prevent aggregation or assist in protein refolding.,
This serine endopeptidase is essential for the clearance of denatured or aggregated proteins from the inner-membrane and periplasmic space in Escherichia coli.
|
| rdfs:subClassOf | |
| skos:broaderTransitive | |
| uniprot:name |
High temperature requirement protease A,
HrtA heat shock protein,
Peptidase Do,
Protease Do
|
| uniprot:activity |
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.
|