Pre_GI: SWBIT SVG BLASTN

Query: NC_010645:3720501 Bordetella avium 197N, complete genome

Lineage: Bordetella avium; Bordetella; Alcaligenaceae; Burkholderiales; Proteobacteria; Bacteria

General Information: This strain is a spontaneous nalidixic acid-resistant derivative of virulent strain 197. This group of organisms is capable of invading the respiratory tract of animals and causing severe diseases. They express a number of virulence factors in order to do this including filamentous hemagglutins for attachment, cytotoxins, and proteins that form a type III secretion system for transport of effector molecules into host cells. This organism infects the respiratory tract of birds, and causes bordetellosis in commercially important animals such as turkeys, resulting in devastating losses every year due to secondary infections.

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Subject: NC_011898:2907017 Clostridium cellulolyticum H10, complete genome

Lineage: Clostridium cellulolyticum; Clostridium; Clostridiaceae; Clostridiales; Firmicutes; Bacteria

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.