Query: NC_007958:4541110 Rhodopseudomonas palustris BisB5, complete genome Lineage: Rhodopseudomonas palustris; Rhodopseudomonas; Bradyrhizobiaceae; Rhizobiales; Proteobacteria; Bacteria General Information: Four different strains were isolated from 2 sites, one pristine and one polluted. Environmental bacterium with potential use in bioremediation. This organism has a diverse metabolism and is capable of growth using light, inorganic, or organic compounds as energy sources and carbon dioxide or organic compounds as carbon sources. Commonly found in soil and water environments this bacterium is also capable of degrading a wide range of toxic organic compounds, and may be of use in bioremediation of polluted sites. The bacterium undergoes differentiation to produce a stalked nonmotile cell and a motile flagellated cell. In the presence of light, this bacterium produces a number of intracellular membranous vesicles to house the photosynthetic reaction centers.
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General Information: This organism is associated with severe and chronic periodontal (tissues surrounding and supporting the tooth) diseases. Progression of the disease is caused by colonization by this organism in an anaerobic environment in host tissues and severe progression results in loss of the tissues supporting the tooth and eventually loss of the tooth itself. The black pigmentation characteristic of this bacterium comes from iron acquisition that does not use the typical siderophore system of other bacteria but accumulates hemin. Peptides appear to be the predominant carbon and energy source of this organism, perhaps in keeping with its ability to destroy host tissue. Oxygen tolerance systems play a part in establishment of the organism in the oral cavity, including a superoxide dismutase. Pathogenic factors include extracellular adhesins that mediate interactions with other bacteria as well as the extracellular matrix, and a host of degradative enzymes that are responsible for tissue degradation and spread of the organism including the gingipains, which are trypsin-like cysteine proteases.