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  • Rule: ActivityStreamsMapasEquivalentb3sb3sifpdbprdf-labelfacetshttp://dbpedia.org/resource/inference/rules/dbpedia#http://dbpedia.org/resource/inference/rules/opencyc#http://dbpedia.org/resource/inference/rules/umbel#http://dbpedia.org/resource/inference/rules/yago#http://dbpedia.org/schema/property_rules#http://www.ontologyportal.org/inference/rules/SUMO#http://www.ontologyportal.org/inference/rules/WordNet#http://www.w3.org/2002/07/owl#ldpoplwebskos-transurn:det:rdf:labelvirtrdf-labelvirtrdf-urlNone
    
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About: Omptin     Goto   Sponge   NotDistinct   Permalink

An Entity of Type : yago:WikicatProteinFamilies, within Data Space : dbpedia.org associated with source document(s)

Type: ThingBiomoleculeBiomoleculeProteinyago:Abstraction100002137yago:Family108078020yago:Group100031264yago:Organization108008335yago:YagoLegalActoryago:YagoLegalActorGeoyago:YagoPermanentlyLocatedEntityproteinyago:SocialGroup107950920yago:Unit108189659yago:WikicatProteinFamilies New Facet based on Instances of this Class

Omptins (EC 3.4.23.49, protease VII, protease A, gene ompT proteins, ompT protease, protein a, Pla, OmpT) are a family of bacterial proteases. They are aspartate proteases, which cleave peptides with the use of a water molecule. Found in the outer membrane of gram-negative enterobacteria such as Shigella flexneri, Yersinia pestis, Escherichia coli, and Salmonella enterica. Omptins consist of a widely conserved beta barrel spanning the membrane with 5 extracellular loops. These loops are responsible for the various substrate specificities. These proteases rely upon binding of lipopolysaccharide for activity.