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http://purl.uniprot.org/citations/20851903http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20851903http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20851903http://www.w3.org/2000/01/rdf-schema#comment"The peptidoglycan of Selenomonas ruminantium is covalently bound to cadaverine (PG-cadaverine), which likely plays a significant role in maintaining the integrity of the cell surface structure. The outer membrane of this bacterium contains a 45-kDa major protein (Mep45) that is a putative peptidoglycan-associated protein. In this report, we determined the nucleotide sequence of the mep45 gene and investigated the relationship between PG-cadaverine, Mep45, and the cell surface structure. Amino acid sequence analysis showed that Mep45 is comprised of an N-terminal S-layer-homologous (SLH) domain followed by α-helical coiled-coil region and a C-terminal β-strand-rich region. The N-terminal SLH domain was found to be protruding into the periplasmic space and was responsible for binding to peptidoglycan. It was determined that Mep45 binds to the peptidoglycan in a manner dependent on the presence of PG-cadaverine. Electron microscopy revealed that defective PG-cadaverine decreased the structural interactions between peptidoglycan and the outer membrane, consistent with the proposed role for PG-cadaverine. The C-terminal β-strand-rich region of Mep45 was predicted to be a membrane-bound unit of the 14-stranded β-barrel structure. Here we propose that PG-cadaverine possesses functional importance to facilitate the structural linkage between peptidoglycan and the outer membrane via specific interaction with the SLH domain of Mep45."xsd:string
http://purl.uniprot.org/citations/20851903http://purl.org/dc/terms/identifier"doi:10.1128/JB.00417-10"xsd:string
http://purl.uniprot.org/citations/20851903http://purl.org/dc/terms/identifier"doi:10.1128/jb.00417-10"xsd:string
http://purl.uniprot.org/citations/20851903http://purl.uniprot.org/core/author"Kojima S."xsd:string
http://purl.uniprot.org/citations/20851903http://purl.uniprot.org/core/author"Kojima S."xsd:string
http://purl.uniprot.org/citations/20851903http://purl.uniprot.org/core/author"Kamio Y."xsd:string
http://purl.uniprot.org/citations/20851903http://purl.uniprot.org/core/author"Kamio Y."xsd:string
http://purl.uniprot.org/citations/20851903http://purl.uniprot.org/core/author"Takatsuka Y."xsd:string
http://purl.uniprot.org/citations/20851903http://purl.uniprot.org/core/author"Takatsuka Y."xsd:string
http://purl.uniprot.org/citations/20851903http://purl.uniprot.org/core/author"Abe N."xsd:string
http://purl.uniprot.org/citations/20851903http://purl.uniprot.org/core/author"Abe N."xsd:string
http://purl.uniprot.org/citations/20851903http://purl.uniprot.org/core/author"Itoh Y."xsd:string
http://purl.uniprot.org/citations/20851903http://purl.uniprot.org/core/author"Itoh Y."xsd:string
http://purl.uniprot.org/citations/20851903http://purl.uniprot.org/core/author"Kaneko J."xsd:string
http://purl.uniprot.org/citations/20851903http://purl.uniprot.org/core/author"Kaneko J."xsd:string
http://purl.uniprot.org/citations/20851903http://purl.uniprot.org/core/author"Ko K.C."xsd:string
http://purl.uniprot.org/citations/20851903http://purl.uniprot.org/core/author"Ko K.-C."xsd:string
http://purl.uniprot.org/citations/20851903http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20851903http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20851903http://purl.uniprot.org/core/name"J. Bacteriol."xsd:string
http://purl.uniprot.org/citations/20851903http://purl.uniprot.org/core/name"J Bacteriol"xsd:string
http://purl.uniprot.org/citations/20851903http://purl.uniprot.org/core/pages"5953-5961"xsd:string
http://purl.uniprot.org/citations/20851903http://purl.uniprot.org/core/pages"5953-5961"xsd:string