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http://purl.uniprot.org/citations/2760036http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/2760036http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/2760036http://www.w3.org/2000/01/rdf-schema#comment"We have determined the complete nucleotide sequence of the gene for the cell envelope-located proteinase of Lactococcus lactis SK11. The gene contains a very AT-rich promoter region followed by the coding sequence of a protein of 1962 amino acids. Comparison of the NH2-terminal amino acid sequence of the mature proteinase and the expected primary translation product of the proteinase gene indicates that the enzyme is probably synthesized as a pre-pro-protein. This is confirmed by expression studies of the proteinase gene in Escherichia coli. The amino acid sequence of the proteinase shows significant homology to a number of serine proteinases of the subtilisin family. Compared with the related proteinase of L. lactis Wg2, the proteinase of L. lactis SK11 contains a 60-amino acids duplication and a total of 44-amino acid substitutions, some of which may account for the different cleavage specificity of both enzymes. Furthermore, a region was identified in the Lactococcus proteinase, which shows homology to the membrane-anchoring domains of a number of proteins from other Gram-positive bacteria."xsd:string
http://purl.uniprot.org/citations/2760036http://purl.org/dc/terms/identifier"doi:10.1016/s0021-9258(18)80036-9"xsd:string
http://purl.uniprot.org/citations/2760036http://purl.org/dc/terms/identifier"doi:10.1016/s0021-9258(18)80036-9"xsd:string
http://purl.uniprot.org/citations/2760036http://purl.uniprot.org/core/author"Siezen R.J."xsd:string
http://purl.uniprot.org/citations/2760036http://purl.uniprot.org/core/author"Siezen R.J."xsd:string
http://purl.uniprot.org/citations/2760036http://purl.uniprot.org/core/author"Vos P."xsd:string
http://purl.uniprot.org/citations/2760036http://purl.uniprot.org/core/author"Vos P."xsd:string
http://purl.uniprot.org/citations/2760036http://purl.uniprot.org/core/author"de Vos W.M."xsd:string
http://purl.uniprot.org/citations/2760036http://purl.uniprot.org/core/author"de Vos W.M."xsd:string
http://purl.uniprot.org/citations/2760036http://purl.uniprot.org/core/author"Simons G."xsd:string
http://purl.uniprot.org/citations/2760036http://purl.uniprot.org/core/author"Simons G."xsd:string
http://purl.uniprot.org/citations/2760036http://purl.uniprot.org/core/date"1989"xsd:gYear
http://purl.uniprot.org/citations/2760036http://purl.uniprot.org/core/date"1989"xsd:gYear
http://purl.uniprot.org/citations/2760036http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/2760036http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/2760036http://purl.uniprot.org/core/pages"13579-13585"xsd:string
http://purl.uniprot.org/citations/2760036http://purl.uniprot.org/core/pages"13579-13585"xsd:string
http://purl.uniprot.org/citations/2760036http://purl.uniprot.org/core/title"Primary structure and organization of the gene for a procaryotic, cell envelope-located serine proteinase."xsd:string
http://purl.uniprot.org/citations/2760036http://purl.uniprot.org/core/title"Primary structure and organization of the gene for a procaryotic, cell envelope-located serine proteinase."xsd:string
http://purl.uniprot.org/citations/2760036http://purl.uniprot.org/core/volume"264"xsd:string
http://purl.uniprot.org/citations/2760036http://purl.uniprot.org/core/volume"264"xsd:string
http://purl.uniprot.org/citations/2760036http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/2760036
http://purl.uniprot.org/citations/2760036http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/2760036