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http://purl.uniprot.org/citations/25231992http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/25231992http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/25231992http://www.w3.org/2000/01/rdf-schema#comment"Francisella tularensis is the etiological agent of tularemia, or rabbit fever. Although F. tularensis is a recognized biothreat agent with broad and expanding geographical range, its mechanism of infection and environmental persistence remain poorly understood. Previously, we identified seven F. tularensis proteins that induce a rapid encystment phenotype (REP) in the free-living amoeba, Acanthamoeba castellanii. Encystment is essential to the pathogen's long term intracellular survival in the amoeba. Here, we characterize the cellular and molecular function of REP34, a REP protein with a mass of 34 kDa. A REP34 knock-out strain of F. tularensis has a reduced ability to both induce encystment in A. castellanii and invade human macrophages. We determined the crystal structure of REP34 to 2.05-Å resolution and demonstrate robust carboxypeptidase B-like activity for the enzyme. REP34 is a zinc-containing monomeric protein with close structural homology to the metallocarboxypeptidase family of peptidases. REP34 possesses a novel topology and substrate binding pocket that deviates from the canonical funnelin structure of carboxypeptidases, putatively resulting in a catalytic role for a conserved tyrosine and distinct S1' recognition site. Taken together, these results identify REP34 as an active carboxypeptidase, implicate the enzyme as a potential key F. tularensis effector protein, and may help elucidate a mechanistic understanding of F. tularensis infection of phagocytic cells."xsd:string
http://purl.uniprot.org/citations/25231992http://purl.org/dc/terms/identifier"doi:10.1074/jbc.M114.599381"xsd:string
http://purl.uniprot.org/citations/25231992http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m114.599381"xsd:string
http://purl.uniprot.org/citations/25231992http://purl.uniprot.org/core/author"Segelke B.W."xsd:string
http://purl.uniprot.org/citations/25231992http://purl.uniprot.org/core/author"Segelke B.W."xsd:string
http://purl.uniprot.org/citations/25231992http://purl.uniprot.org/core/author"Monack D.M."xsd:string
http://purl.uniprot.org/citations/25231992http://purl.uniprot.org/core/author"Monack D.M."xsd:string
http://purl.uniprot.org/citations/25231992http://purl.uniprot.org/core/author"Frank M."xsd:string
http://purl.uniprot.org/citations/25231992http://purl.uniprot.org/core/author"Frank M."xsd:string
http://purl.uniprot.org/citations/25231992http://purl.uniprot.org/core/author"Hunter M.S."xsd:string
http://purl.uniprot.org/citations/25231992http://purl.uniprot.org/core/author"Hunter M.S."xsd:string
http://purl.uniprot.org/citations/25231992http://purl.uniprot.org/core/author"Belhocine K."xsd:string
http://purl.uniprot.org/citations/25231992http://purl.uniprot.org/core/author"Belhocine K."xsd:string
http://purl.uniprot.org/citations/25231992http://purl.uniprot.org/core/author"Feld G.K."xsd:string
http://purl.uniprot.org/citations/25231992http://purl.uniprot.org/core/author"Feld G.K."xsd:string
http://purl.uniprot.org/citations/25231992http://purl.uniprot.org/core/author"Corzett M.H."xsd:string
http://purl.uniprot.org/citations/25231992http://purl.uniprot.org/core/author"Corzett M.H."xsd:string
http://purl.uniprot.org/citations/25231992http://purl.uniprot.org/core/author"Rasley A."xsd:string
http://purl.uniprot.org/citations/25231992http://purl.uniprot.org/core/author"Rasley A."xsd:string
http://purl.uniprot.org/citations/25231992http://purl.uniprot.org/core/author"El-Etr S."xsd:string
http://purl.uniprot.org/citations/25231992http://purl.uniprot.org/core/author"El-Etr S."xsd:string
http://purl.uniprot.org/citations/25231992http://purl.uniprot.org/core/date"2014"xsd:gYear
http://purl.uniprot.org/citations/25231992http://purl.uniprot.org/core/date"2014"xsd:gYear