Query: NC_017501:147933 Neisseria meningitidis 8013, complete genome Lineage: Neisseria meningitidis; Neisseria; Neisseriaceae; Neisseriales; Proteobacteria; Bacteria General Information: The second of two pathogenic Neisseria, this organism causes septicemia and is the leading cause of life-threatening meningitis (inflammation of the meninges, the membrane surrounding the brain and spinal cord) in children. This organism typically residies in the nasopharynx cavity but can invade the respiratory epthelial barrier, cross into the bloodstream and the blood brain barrier, and cause inflammation of the meninges. Pathogenicity factors include the surface proteins (porins and opacity proteins), and the type IV pilus (which is also found in Neisseria gonorrhoeae). This organism, like Neisseria gonorrhoeae, is naturally competent, and protein complexes at the cell surface recognize the uptake signal sequence in extracellular DNA, an 8mer that is found at high frequency in Neisseria chromosomal DNA.
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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.