Query: NC_010634:2376245 Yersinia pseudotuberculosis PB1/+, complete genome Lineage: Yersinia pseudotuberculosis; Yersinia; Enterobacteriaceae; Enterobacteriales; Proteobacteria; Bacteria General Information: Environmental bacterium that causes gastrointestinal disease. Specific virulence factors are encoded within pathogenicity islands (PAIs) that are required for the invasive phenotype associated with Yersinia infections. One key virulence plasmid contained by the three human-specific pathogens is pCD1/pYv, which encodes a type III secretion system for the delivery of virulence proteins that contribute to internalization into the host cell. This organism was first isolated in 1883 by Malassez and Vignal and is termed pseudotuberculosis since it causes lesions in the lung that are similar to those observed during tuberculosis infection. It is ubiquitous in the environment and is a food and waterborne pathogen that affects animals as well as humans by causing gastroenteritis like Yersinia enterocolitica.
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General Information: A non-ruminal mesophilic cellulolytic bacterium originally isolated from decayed grass compost. This genus comprises about 150 metabolically diverse species of anaerobes that are ubiquitous in virtually all anoxic habitats where organic compounds are present, including soils, aquatic sediments and the intestinal tracts of animals and humans. This shape is attributed to the presence of endospores that develop under conditions unfavorable for vegetative growth and distend single cells terminally or sub-terminally. Spores germinate under conditions favorable for vegetative growth, such as anaerobiosis and presence of organic substrates. It is believed that present day Mollicutes (Eubacteria) have evolved regressively (i.e., by genome reduction) from gram-positive clostridia-like ancestors with a low GC content in DNA. Clostridium cellulolyticum is a mesophilic cellulolytic bacterium. Cellulose-degradation by C. cellulolyticum has been extensively studied. The cellulolytic enzymes of this organism are bound to a protein scaffold in an extracellular multienzyme complex called a cellulosome.