| http://purl.uniprot.org/enzyme/3.4.21.107 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Enzyme |
| http://purl.uniprot.org/enzyme/3.4.21.107 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/3.4.-.- |
| http://purl.uniprot.org/enzyme/3.4.21.107 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/3.4.21.- |
| http://purl.uniprot.org/enzyme/3.4.21.107 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/3.-.-.- |
| http://purl.uniprot.org/enzyme/3.4.21.107 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/core/Enzyme |
| http://purl.uniprot.org/enzyme/3.4.21.107 | http://www.w3.org/2000/01/rdf-schema#comment | "Natural substrates of the enzyme include colicin A lysis protein, pilin subunits and MalS from E.coli."xsd:string |
| http://purl.uniprot.org/enzyme/3.4.21.107 | http://www.w3.org/2000/01/rdf-schema#comment | "The enzyme has weak peptidase activity with casein and other non-native substrates."xsd:string |
| http://purl.uniprot.org/enzyme/3.4.21.107 | http://www.w3.org/2000/01/rdf-schema#comment | "They then bind these hydrophobic substrates to prevent aggregation or assist in protein refolding."xsd:string |
| http://purl.uniprot.org/enzyme/3.4.21.107 | http://www.w3.org/2000/01/rdf-schema#comment | "Belongs to peptidase family S1B."xsd:string |
| http://purl.uniprot.org/enzyme/3.4.21.107 | http://www.w3.org/2000/01/rdf-schema#comment | "Molecular chaperones and peptidases control the folded state of proteins by recognizing hydrophobic stretches of polypeptide that become exposed by misfolding or unfolding."xsd:string |
| http://purl.uniprot.org/enzyme/3.4.21.107 | http://www.w3.org/2000/01/rdf-schema#comment | "The peptidase acts as a chaperone at low temperatures but switches to a peptidase (heat shock protein) at higher temperatures."xsd:string |
| http://purl.uniprot.org/enzyme/3.4.21.107 | http://www.w3.org/2000/01/rdf-schema#comment | "If attempts at refolding fail, then irreversibly damaged proteins are degraded by peptidases such as this enzyme."xsd:string |
| http://purl.uniprot.org/enzyme/3.4.21.107 | http://www.w3.org/2000/01/rdf-schema#comment | "This serine endopeptidase is essential for the clearance of denatured or aggregated proteins from the inner-membrane and periplasmic space in Escherichia coli."xsd:string |
| http://purl.uniprot.org/enzyme/3.4.21.107 | http://www.w3.org/2004/02/skos/core#prefLabel | "peptidase Do"xsd:string |
| http://purl.uniprot.org/enzyme/3.4.21.107 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/11919638 |
| http://purl.uniprot.org/enzyme/3.4.21.107 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/12270835 |
| http://purl.uniprot.org/enzyme/3.4.21.107 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/2025286 |
| http://purl.uniprot.org/enzyme/3.4.21.107 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/2180903 |
| http://purl.uniprot.org/enzyme/3.4.21.107 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/6347072 |
| http://purl.uniprot.org/enzyme/3.4.21.107 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/9383148 |
| http://purl.uniprot.org/enzyme/3.4.21.107 | http://www.w3.org/2004/02/skos/core#altLabel | "protease Do"xsd:string |
| http://purl.uniprot.org/enzyme/3.4.21.107 | http://www.w3.org/2004/02/skos/core#altLabel | "HrtA heat shock protein"xsd:string |
| http://purl.uniprot.org/enzyme/3.4.21.107 | http://www.w3.org/2004/02/skos/core#altLabel | "high temperature requirement protease A"xsd:string |
| http://purl.uniprot.org/enzyme/3.4.21.107 | http://purl.uniprot.org/core/activity | http://purl.uniprot.org/enzyme/3.4.21.107#SIP7AAEFD73455674B8 |
| http://purl.uniprot.org/enzyme/3.4.21.107 | http://www.w3.org/2004/02/skos/core#broaderTransitive | http://purl.uniprot.org/enzyme/3.4.21.- |