Sporosarcina Thermotolerans
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Sporosarcina Thermotolerans
''Sporosarcina'' is a genus of bacteria. Specification The cells of the species of ''Sporosarcina'' are either rod-shaped or coccoid. ''Sporosarcina'' forms endospores. The majority species of ''Sporosarcina'' is moveable (motile). Metabolism All species of ''Sporosarcina'' are heterotrophic. They do not perform photosynthesis. A few species are obligate aerobic, they need oxygen. Others are facultative aerobic, they can also perform metabolism in the absence of oxygen. Ecology Some species, such as ''S. ureae'' have the enzyme urease and are thus able to break down urea. The species forms the highest population densities in soils that are subject to influence of urine. These include, for example, meadows where cattle are kept. Thus ''S. ureae'' plays an important role in the ecosystem. Molecular Signatures Analyses of genome sequences of ''Sporosarcina'' species identified eight conserved signature indels (CSIs) that are uniquely present in this genus in the protei ...
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Bacteria
Bacteria (; singular: bacterium) are ubiquitous, mostly free-living organisms often consisting of one biological cell. They constitute a large domain of prokaryotic microorganisms. Typically a few micrometres in length, bacteria were among the first life forms to appear on Earth, and are present in most of its habitats. Bacteria inhabit soil, water, acidic hot springs, radioactive waste, and the deep biosphere of Earth's crust. Bacteria are vital in many stages of the nutrient cycle by recycling nutrients such as the fixation of nitrogen from the atmosphere. The nutrient cycle includes the decomposition of dead bodies; bacteria are responsible for the putrefaction stage in this process. In the biological communities surrounding hydrothermal vents and cold seeps, extremophile bacteria provide the nutrients needed to sustain life by converting dissolved compounds, such as hydrogen sulphide and methane, to energy. Bacteria also live in symbiotic and parasitic relationsh ...
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Urease
Ureases (), functionally, belong to the superfamily of amidohydrolases and phosphotriesterases. Ureases are found in numerous bacteria, fungi, algae, plants, and some invertebrates, as well as in soils, as a soil enzyme. They are nickel-containing metalloenzymes of high molecular weight. These enzymes catalyze the hydrolysis of urea into carbon dioxide and ammonia: : (NH2)2CO + H2O CO2 + 2NH3 The hydrolysis of urea occurs in two stages. In the first stage, ammonia and carbamic acid are produced. The carbamate spontaneously and rapidly hydrolyzes to ammonia and carbonic acid. Urease activity increases the pH of its environment as ammonia is produced, which is basic. History Its activity was first identified in 1876 by Frédéric Alphonse Musculus as a soluble ferment. In 1926, James B. Sumner, showed that urease is a protein by examining its crystallized form. Sumner's work was the first demonstration that a protein can function as an enzyme and led eventually to the reco ...
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Sporosarcina Pasteurii
''Sporosarcina pasteurii'' formerly known as ''Bacillus pasteurii'' from older taxonomies, is a gram positive bacterium with the ability to precipitate calcite and solidify sand given a calcium source and urea; through the process of microbiologically induced calcite precipitation (MICP) or biological cementation. ''S. pasteurii'' has been proposed to be used as an ecologically sound biological construction material. Researchers studied the bacteria in conjunction with plastic and hard mineral; forming a material stronger than bone. It is a commonly used for MICP since it is non-pathogenic and is able to produce high amounts of the enzyme urease which hydrolyzes urea to carbonate and ammonia. Physiology ''S. pasteurii'' is a gram positive bacterium that is rod-like shaped in nature. It has the ability to form endospores in the right environmental conditions to enhance its survival, which is a characteristic of its bacillus class. It has dimensions of 0.5 to 1.2 microns in wi ...
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Sporosarcina Newyorkensis
''Sporosarcina newyorkensis'' is a Gram-positive and endospore-forming bacterium from the genus of ''Sporosarcina'' which has been isolated from human blood and raw cow milk Milk is a white liquid food produced by the mammary glands of mammals. It is the primary source of nutrition for young mammals (including breastfed human infants) before they are able to digest solid food. Immune factors and immune-modulating .... References Bacillales Bacteria described in 2012 {{Gammaproteobacteria-stub ...
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Sporosarcina Globispora
''Sporosarcina globispora'', formerly known as ''Bacillus globisporus'', is a Gram-positive, aerobic, round spore-forming bacillus. Strains of this species were originally described in 1967 and were found to be fairly similar to the species ''Bacillus pantothenticus''. The species was later reassigned to the genus '' Sporosarcina'' along with the species ''Bacillus psychrophilus'' and ''Bacillus pasteurii ''Sporosarcina pasteurii'' formerly known as ''Bacillus pasteurii'' from older taxonomies, is a gram positive bacterium with the ability to precipitate calcite and solidify sand given a calcium source and urea; through the process of microbio ...''. References External linksType strain of ''Sporosarcina globispora'' at Bac''Dive'' - the Bacterial Diversity Metadatabase Bacillales {{bacilli-stub ...
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Sporosarcina Contaminans
''Sporosarcina contaminans'' is a Gram-positive and endospore-forming bacterium from the genus of ''Sporosarcina'' which has been isolated from an industrial clean-room floor from Göteborg in Sweden Sweden, formally the Kingdom of Sweden,The United Nations Group of Experts on Geographical Names states that the country's formal name is the Kingdom of SwedenUNGEGN World Geographical Names, Sweden./ref> is a Nordic country located on .... References Bacillales Bacteria described in 2010 {{Gammaproteobacteria-stub ...
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Sporosarcina Aquimarina
''Sporosarcina aquimarina'' is a rod-shaped bacterium of the genus ''Sporosarcina''. Characteristics Cells of ''Sporosarcina aquimarina'' are 0.9–1.2 μm x 2.0–3.5 μm. It is motile by means of a single polar flagellum. The bacterium forms endospores (like all species of the genus). Metabolism ''Sporosarcina aquimarina'' is heterotrophic, as it does not perform photosynthesis. It is facultative anaerobe. If oxygen is present the metabolism is due to cellular respiration, but it can also grow anaerobic if oxygen is absent. The species is halophilic. 13% NaCl are still tolerated. ''Sporosarcina aquimarina'' is one of the bacteria that can make use of urea with the enzyme urease. Others bacteria of the same genus which possess the enzyme urease are for example '' S. ureaea'' und '' S. pasteurii''. Etymology The genus name derives from the Greek word ''spora'' ("spore") and the Latin word ''sarcina'' ("package", "bundle") and refers to the fact that it forms endospores an ...
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Sporosarcina Luteola
''Sporosarcina luteola'' is a Gram-variable, spore-forming and motile bacterium from the genus of ''Sporosarcina'' which has been isolated from equipment used for soy sauce production in Japan Japan ( ja, 日本, or , and formally , ''Nihonkoku'') is an island country in East Asia. It is situated in the northwest Pacific Ocean, and is bordered on the west by the Sea of Japan, while extending from the Sea of Okhotsk in the north .... References Bacillales Bacteria described in 2009 {{Gammaproteobacteria-stub ...
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Cytochrome B
Cytochrome b within both molecular and cell biology, is a protein found in the mitochondria of eukaryotic cells. It functions as part of the electron transport chain and is the main subunit of transmembrane cytochrome bc1 and b6f complexes. Function In the mitochondrion of eukaryotes and in aerobic prokaryotes, cytochrome b is a component of respiratory chain complex III () — also known as the bc1 complex or ubiquinol-cytochrome c reductase. In plant chloroplasts and cyanobacteria, there is an analogous protein, cytochrome b6, a component of the plastoquinone-plastocyanin reductase (), also known as the b6f complex. These complexes are involved in electron transport, the pumping of protons to create a proton-motive force ( PMF). This proton gradient is used for the generation of ATP. These complexes play a vital role in cells. Structure Cytochrome b/b6 is an integral membrane protein of approximately 400 amino acid residues that probably has 8 transmembrane segments. ...
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DEAD Box
Death is the irreversible cessation of all biological functions that sustain an organism. For organisms with a brain, death can also be defined as the irreversible cessation of functioning of the whole brain, including brainstem, and brain death is sometimes used as a legal definition of death. The remains of a former organism normally begin to decompose shortly after death. Death is an inevitable process that eventually occurs in almost all organisms. Death is generally applied to whole organisms; the similar process seen in individual components of an organism, such as cells or tissues, is necrosis. Something that is not considered an organism, such as a virus, can be physically destroyed but is not said to die. As of the early 21st century, over 150,000 humans die each day, with ageing being by far the most common cause of death. Many cultures and religions have the idea of an afterlife, and also may hold the idea of judgement of good and bad deeds in one's life (heaven, ...
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Thymidylate Synthase
Thymidylate synthase (TS) () is an enzyme that catalyzes the conversion of deoxyuridine monophosphate (dUMP) to deoxythymidine monophosphate (dTMP). Thymidine is one of the nucleotides in DNA. With inhibition of TS, an imbalance of deoxynucleotides and increased levels of dUMP arise. Both cause DNA damage. Function The following reaction is catalyzed by thymidylate synthase: : 5,10-methylenetetrahydrofolate + dUMP \rightleftharpoons dihydrofolate + dTMP By means of reductive methylation, deoxyuridine monophosphate (dUMP) and N5,N10-methylene tetrahydrofolate are together used to form dTMP, yielding dihydrofolate as a secondary product. This provides the sole de novo pathway for production of dTMP and is the only enzyme in folate metabolism in which the 5,10-methylenetetrahydrofolate is oxidised during one-carbon transfer. The enzyme is essential for regulating the balanced supply of the 4 DNA precursors in normal DNA replication: defects in the enzyme activity affectin ...
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Aspartate—tRNA Ligase
In enzymology, an aspartate—tRNA ligase () is an enzyme that catalyzes the chemical reaction :ATP + L-aspartate + tRNAAsp \rightleftharpoons AMP + diphosphate + L-aspartyl-tRNAAsp The 3 substrates of this enzyme are ATP, L-aspartate, and tRNA(Asp), whereas its 3 products are AMP, diphosphate, and L-aspartyl-tRNA(Asp). This enzyme belongs to the family of ligases, to be specific those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds. The systematic name of this enzyme class is L-aspartate:tRNAAsp ligase (AMP-forming). Other names in common use include aspartyl-tRNA synthetase, aspartyl ribonucleic synthetase, aspartyl-transfer RNA synthetase, aspartic acid translase, aspartyl-transfer ribonucleic acid synthetase, and aspartyl ribonucleate synthetase. This enzyme participates in alanine and aspartate metabolism and aminoacyl-trna biosynthesis. Structural studies As of late 2007, 10 structures have been solved for this class of enzymes, with PDB acce ...
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