Parvulin-like peptidyl-prolyl isomerase (original) (raw)
Parvulin-like peptidyl-prolyl isomerase (PrsA), also referred to as putative proteinase maturation protein A (PpmA), functions as a molecular chaperone in Gram-positive bacteria, such as B. subtilis, S. aureus, L. monocytogenes and S. pyogenes. PrsA proteins contain a highly conserved parvulin domain that contains peptidyl-prolyl cis-trans isomerase (PPIase) activity capable of catalyzing the bond N-terminal to proline from cis to trans, or vice versa, which is a rate limiting step in protein folding. PrsA homologs also contain a foldase domain suspected to aid in the folding of proteins but, unlike the parvulin domain, is not highly conserved. PrsA proteins are capable of forming multimers in vivo and in vitro and, when dimerized, form a claw-like structure linked by the NC domains. Most
| Property | Value |
|---|---|
| dbo:abstract | Parvulin-like peptidyl-prolyl isomerase (PrsA), also referred to as putative proteinase maturation protein A (PpmA), functions as a molecular chaperone in Gram-positive bacteria, such as B. subtilis, S. aureus, L. monocytogenes and S. pyogenes. PrsA proteins contain a highly conserved parvulin domain that contains peptidyl-prolyl cis-trans isomerase (PPIase) activity capable of catalyzing the bond N-terminal to proline from cis to trans, or vice versa, which is a rate limiting step in protein folding. PrsA homologs also contain a foldase domain suspected to aid in the folding of proteins but, unlike the parvulin domain, is not highly conserved. PrsA proteins are capable of forming multimers in vivo and in vitro and, when dimerized, form a claw-like structure linked by the NC domains. Most Gram-positive bacteria contain only one PrsA-like protein, but some organisms such as L. monocytogenes, B. anthracis and S. pyogenes contain two PrsAs. (en) |
| dbo:wikiPageID | 70359040 (xsd:integer) |
| dbo:wikiPageLength | 6731 (xsd:nonNegativeInteger) |
| dbo:wikiPageRevisionID | 1109200711 (xsd:integer) |
| dbo:wikiPageWikiLink | dbr:Gram-positive_bacteria dbc:Molecular_chaperones dbr:Chaperone_(protein) |
| dbp:wikiPageUsesTemplate | dbt:Reflist |
| dcterms:subject | dbc:Molecular_chaperones |
| rdfs:comment | Parvulin-like peptidyl-prolyl isomerase (PrsA), also referred to as putative proteinase maturation protein A (PpmA), functions as a molecular chaperone in Gram-positive bacteria, such as B. subtilis, S. aureus, L. monocytogenes and S. pyogenes. PrsA proteins contain a highly conserved parvulin domain that contains peptidyl-prolyl cis-trans isomerase (PPIase) activity capable of catalyzing the bond N-terminal to proline from cis to trans, or vice versa, which is a rate limiting step in protein folding. PrsA homologs also contain a foldase domain suspected to aid in the folding of proteins but, unlike the parvulin domain, is not highly conserved. PrsA proteins are capable of forming multimers in vivo and in vitro and, when dimerized, form a claw-like structure linked by the NC domains. Most (en) |
| rdfs:label | Parvulin-like peptidyl-prolyl isomerase (en) |
| owl:sameAs | wikidata:Parvulin-like peptidyl-prolyl isomerase https://global.dbpedia.org/id/GURST |
| prov:wasDerivedFrom | wikipedia-en:Parvulin-like_peptidyl-prolyl_isomerase?oldid=1109200711&ns=0 |
| foaf:isPrimaryTopicOf | wikipedia-en:Parvulin-like_peptidyl-prolyl_isomerase |
| is dbo:wikiPageRedirects of | dbr:PrsA_(Parvulin-like_peptidyl-prolyl_isomerase) |
| is dbo:wikiPageWikiLink of | dbr:PrsA_(Parvulin-like_peptidyl-prolyl_isomerase) dbr:PRSA |
| is foaf:primaryTopic of | wikipedia-en:Parvulin-like_peptidyl-prolyl_isomerase |