Query: NC_010163:63209 Acholeplasma laidlawii PG-8A chromosome, complete genome Lineage: Acholeplasma laidlawii; Acholeplasma; Acholeplasmataceae; Acholeplasmatales; Tenericutes; Bacteria General Information: Acholeplasma species are widely distributed in the nature and can be detected and isolated from different plant, avian, and mammalian sources. Acholeplasma laidlawii is found in soil, compost, wastewaters, cell cultures as well as in human tissues and in many animal species (birds, bovine, goat, equine, ovine, porcine, feline, rodent, primates). Acholeplasma laidlawii is capable of synthesizing glucose using a pyrophosphate-dependent 6-phosphofructokinase which has also been detected in other acholeplasmas (a good example of flexible metabolism). Additionally, Acholeplasma laidlawii and phytoplasmas are the only mollicutes known to use the universal genetic code, in which UGA is a stop codon.
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General Information: This strain (also known as HG66) is virulent in a mouse model and has been extensively studied. It was originally isolated by H. Werner in the 1950s in Bonn, Germany, from an unknown human infection. Associated with severe and chronic periodontal disease. 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.