Query: NC_006142:140853 Rickettsia typhi str. Wilmington, complete genome Lineage: Rickettsia typhi; Rickettsia; Rickettsiaceae; Rickettsiales; Proteobacteria; Bacteria General Information: This genus, like other Rickettsial organisms such as Neorickettsia and Anaplasma, is composed of obligate intracellular pathogens. The latter is composed of two organisms, Rickettsia prowazekii and Rickettsia typhi. The bacteria are transmitted via an insect, usually a tick, to a host organism, in this case humans, where they target endothelial cells and sometimes macrophages. They attach via an adhesin, rickettsial outer membrane protein A, and are internalized where they persist as cytoplasmically free organisms. Transovarial transmission (from mother to offspring) occurs in the invertebrate host. Rickettsia typhi causes murine typhus and is an obligate intracellular pathogen that infects both the flea vector and hosts such as human, rat, and mouse. In the flea vector, the bacterium penetrates the gut epithelial barrier and is found in the feces which become infective.
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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.