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Coxiella (bacterium)
''Coxiella'' refers to a genus of Gram-negative bacteria in the family Coxiellaceae. It is named after Herald Rea Cox (1907–1986), an American bacteriologist. It is one of the Gammaproteobacteria. ''Coxiella burnetii'' is the best known member of this genus. It is an intracellular parasite and it survives within the phagolysosomes of its host. It causes Q fever. The majority of ''Coxiella''’s described members are non pathogenic forms which are often found in ticks. Approximately two-thirds of tick species harbour ''Coxiella''-like endosymbionts required for tick survival and reproduction. Genomes of ''Coxiella''-like endosymbionts encode pathways for the biosynthesis of major B vitamins and co-factors that fit closely with the expected nutritional complements required for strict haematophagy. The experimental elimination of ''Coxiella''-like endosymbionts typically results in decreased tick survival, molting, fecundity and egg viability, as well as in physical abnormali ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
LPSN
List of Prokaryotic names with Standing in Nomenclature (LPSN) is an online database that maintains information on the naming and taxonomy of prokaryotes, following the taxonomy requirements and rulings of the International Code of Nomenclature of Prokaryotes. The database was curated from 1997 to June 2013 by Jean P. Euzéby. From July 2013 to January 2020, LPSN was curated by Aidan C. Parte. In February 2020, a new version of LPSN was published as a service of the Leibniz Institute DSMZ, thereby also integrating the Prokaryotic Nomenclature Up-to-date service. References External links List of Prokaryotic names with Standing in Nomenclature [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
GMP Synthase
Guanosine monophosphate synthetase, () also known as GMPS is an enzyme that converts xanthosine monophosphate to guanosine monophosphate. In the de novo synthesis of purine nucleotides, IMP is the branch point metabolite at which point the pathway diverges to the synthesis of either guanine or adenine nucleotides. In the guanine nucleotide pathway, there are 2 enzymes involved in converting IMP to GMP, namely IMP dehydrogenase (IMPD1), which catalyzes the oxidation of IMP to XMP, and GMP synthetase, which catalyzes the amination of XMP to GMP. Enzymology In enzymology, a GMP synthetase (glutamine-hydrolysing) () is an enzyme that catalyzes the chemical reaction :ATP + xanthosine 5'-phosphate + L-glutamine + H2O \rightleftharpoons AMP + diphosphate + GMP + L-glutamate The 4 substrates of this enzyme are ATP, xanthosine 5'-phosphate, L-glutamine, and H2O, whereas its 4 products are AMP, diphosphate, GMP, and L-glutamate. This enzyme belongs to the family of ligases, sp ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Legionellales
The Legionellales are an order of Pseudomonadota. Like all Pseudomonadota, they are Gram-negative.George M. Garrity: ''Bergey's Manual of Systematic Bacteriology''. 2. Auflage. Springer, New York, 2005, Volume 2: ''The Proteobacteria, Part B: The Gammaproteobacteria'' They comprise two families, typified by ''Legionella'' and '' Coxiella'', both of which include notable pathogens. For example, Q fever is caused by ''Coxiella burnetii'' and ''Legionella pneumophila'' causes Legionnaires' disease and Pontiac fever. Members of the order ''Legionellales'' can be molecularly distinguished from other Gammaproteobacteria by the presence of four conserved signature indels Conserved signature inserts and deletions (CSIs) in protein sequences provide an important category of molecular markers for understanding phylogenetic relationships. CSIs, brought about by rare genetic changes, provide useful phylogenetic markers ... (CSIs) in the proteins tRNA-guanine(34) transglycosylase, lipoprotei ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Aquicella
''Aquicella'' is a genus of Gram-negative rod-shaped cells and filaments in the family '' Coxiellaceae'' from the order '' Legionellales''. The type species of this genus is ''Aquicella lusitana.'' The name ''Aquicella'' is composed of the Latin term ''aqua'' (referring to water) and the Latin term ''cella'' (referring to a chamber, closet, or cabinet, or in biology, a cell). Together, the name ''Aquicella'' translates to a cell from water. Biochemical Characteristics and Molecular Signatures Members of this genus grow in protozoa and can be isolated from hydrothermal areas. All members are strictly aerobic, non-motile, do not produce spores and are oxidase and catalase negative. ''Aquicella'' species can grow in temperatures ranging from 30 °C to 43 °C and require a neutral pH and growth media containing activated charcoal and a-ketoglutarate. Colonies appear whitish with a pink or blue sheen. Analyses of genome sequences from ''Aquicella'' species identified six ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Rickettsiella
''Rickettsiella'' is a genus of the family Coxiellaceae. It should not be confused with ''Rickettsia''. It is currently considered of the Gammaproteobacteria. However, its placement under Coxiellaceae instead of Legionellaceae has been challenged. Molecular Signatures and Taxonomy Members of the genera ''Rickettsiella'' and '' Diplorickettsia'' are observed to form a reliable clade in phylogenetic trees constructed from various datasets of concatenated protein sequences and 16S rRNA sequences, suggesting that they might belong to a single genus. Genomic analyses identified 12 conserved signature indels (CSIs) that are specific for this clade in the proteins inositol monophosphatase, lysyl-tRNA synthetase, elongation factor P-(R)-beta-lysine ligase, tol-Pal system beta propeller repeat protein TolB, FKBP-type peptidyl-prolyl cis-trans isomerase, response regulator transcription factor, 30S ribosomal protein S2, glycine cleavage system aminomethyltransferase GcvT, M3 family meta ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Diplorickettsia Massiliensis
''Diplorickettsia massiliensis'' species is an obligate intracellular, gram negative bacterium isolated from Ixodes ricinus ticks collected in Slovak republic forest geographically from southeastern part of Rovinka in 2006.Mediannikov, O., et al.A novel obligate intracellular gamma-proteobacterium associated with ixodid ticks, Diplorickettsia massiliensis, Gen. Nov., Sp. Nov.''PLOS ONE'', 2010. 5(7): p. e11478. They belong to the gammaproteobacteria class and are non endospore forming, small rods usually grouped in pairs. The bacteria are non-motile, and 16S rRNA, rpoB, parC and ftsY gene sequencing indicate that this bacterium is clearly different from all other recognized species. An initial phylogenetic analysis based on 16S rRNA, clustered ''D. massiliensis'' with ''Rickettsiella grylli''. Because of its low 16S rDNA similarity (94%) with ''R. grylli'', it was classified as a new genus ''Diplorickettsia'' into the family ''Coxiellaceae'' and the order ''Legionellales''. '' ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
NADH-quinone Oxidoreductase
NADH:ubiquinone reductase (non-electrogenic) (, ''NDH-2'', ''ubiquinone reductase'', ''coenzyme Q reductase'', ''dihydronicotinamide adenine dinucleotide-coenzyme Q reductase'', ''DPNH-coenzyme Q reductase'', ''DPNH-ubiquinone reductase'', ''NADH-coenzyme Q oxidoreductase'', ''NADH-coenzyme Q reductase'', ''NADH-CoQ oxidoreductase'', ''NADH-CoQ reductase'') is an enzyme with systematic name ''NADH:ubiquinone oxidoreductase''. This enzyme catalyses the following chemical reaction: :NADH + H+ + a quinone \rightleftharpoons NAD+ + a quinol The 3 substrates of this enzyme are NADH, H+, and a quinone (electron acceptor), whereas its two products are NAD+ and a quinol (reduced acceptor). An important example of this reaction is: : NADH + H+ + ubiquinone \rightleftharpoons NAD+ + ubiquinol This enzyme is a flavoprotein (FAD). It belongs to the family of oxidoreductases, specifically those acting on NADH or NADPH with other acceptors. The systematic name of this enzyme class is ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
ABC Transporter
The ATP-binding cassette transporters (ABC transporters) are a transport system superfamily that is one of the largest and possibly one of the oldest gene families. It is represented in all extant phyla, from prokaryotes to humans. ABC transporters belong to translocases. ABC transporters often consist of multiple subunits, one or two of which are transmembrane proteins and one or two of which are membrane-associated AAA ATPases. The ATPase subunits utilize the energy of adenosine triphosphate (ATP) binding and hydrolysis to provide the energy needed for the translocation of substrates across membranes, either for uptake or for export of the substrate. Most of the uptake systems also have an extracytoplasmic receptor, a solute binding protein. Some homologous ATPases function in non-transport-related processes such as translation of RNA and DNA repair. ABC transporters are considered to be an ABC superfamily based on the similarities of the sequence and organization of thei ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Translation Initiation Factor IF-3
In molecular biology, translation initiation factor IF-3 (gene infC) is one of the three factors required for the initiation of protein biosynthesis in bacteria. IF-3 is thought to function as a fidelity factor during the assembly of the ternary initiation complex which consists of the 30S ribosomal subunit, the initiator tRNA and the messenger RNA. IF-3 is a basic protein that binds to the 30S ribosomal subunit. The chloroplast homolog enhances the poly( A, U, G)-dependent binding of the initiator tRNA to its ribosomal 30s subunits. IF1–IF3 may also perform ribosome recycling. IF3 is not universally found in all bacterial species. However, in '' E. coli'', it is required for the 30S subunit to bind to the initiation site in mRNA. In addition, it has several other jobs including the stabilization of free 30S subunits, enables 30S subunits to bind to mRNA and checks for accuracy against the first aminoacyl-tRNA. It also allows for rapid codon-anticodon pairing for the initiat ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Ribonucleoside-diphosphate Reductase
Ribonucleotide reductase (RNR), also known as ribonucleoside diphosphate reductase (rNDP), is an enzyme that catalyzes the formation of deoxyribonucleotides from ribonucleotides. It catalyzes this formation by removing the 2'-hydroxyl group of the ribose ring of nucleoside diphosphates. This reduction produces deoxyribonucleotides. Deoxyribonucleotides in turn are used in the synthesis of DNA. The reaction catalyzed by RNR is strictly conserved in all living organisms. Furthermore, RNR plays a critical role in regulating the total rate of DNA synthesis so that DNA to cell mass is maintained at a constant ratio during cell division and DNA repair. A somewhat unusual feature of the RNR enzyme is that it catalyzes a reaction that proceeds via a free radical mechanism of action. The substrates for RNR are ADP, GDP, CDP and UDP. dTDP (deoxythymidine diphosphate) is synthesized by another enzyme (thymidylate kinase) from dTMP (deoxythymidine monophosphate). Structure Ribonucleotide ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Methionyl Aminopeptidase
Methionyl aminopeptidase (, ''methionine aminopeptidase'', ''peptidase M'', ''L-methionine aminopeptidase'', ''MAP'') is an enzyme. This enzyme catalyses the following chemical reaction : Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides This membrane-bound enzymatic activity is present in both prokaryotes and eukaryote Eukaryotes () are organisms whose cells have a nucleus. All animals, plants, fungi, and many unicellular organisms, are Eukaryotes. They belong to the group of organisms Eukaryota or Eukarya, which is one of the three domains of life. Bact ...s. Proteins possessing this activity include METAP1 and METAP2. References External links * {{Portal bar, Biology, border=no EC 3.4.11 ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protein
Proteins are large biomolecules and macromolecules that comprise one or more long chains of amino acid residues. Proteins perform a vast array of functions within organisms, including catalysing metabolic reactions, DNA replication, responding to stimuli, providing structure to cells and organisms, and transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the nucleotide sequence of their genes, and which usually results in protein folding into a specific 3D structure that determines its activity. A linear chain of amino acid residues is called a polypeptide. A protein contains at least one long polypeptide. Short polypeptides, containing less than 20–30 residues, are rarely considered to be proteins and are commonly called peptides. The individual amino acid residues are bonded together by peptide bonds and adjacent amino acid residues. The sequence of amino acid resid ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
