NhaE Family
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NhaE Family
The NhaE familyTC# 2.A.111 belongs to the Ion Transporter (IT) Superfamily, which has an end. A representative list of proteins belonging to the NhaE family can be found in thTransporter Classification Database The NhaH family consists of proteins from Gram-negative bacteria (e.g., ''Leptospira'', '' Azotobacter'', '' Neisseria'', '' Ralstonia'', ''Chlorobium'' and ''Rhizobial'' species). The proteins are of about 480 aas with 12-14 putative TMSs. An open reading frame (ORF) from the genome of '' Neisseria meningitidis'' displaying similarity with the NhaE type of Na+/H+ antiporters was expressed in ''E. coli'' and characterized for sodium transport ability. The ''N. meningitidis'' antiporter (NmNhaE) was able to complement an ''E. coli'' strain devoid of Na+/H+ antiporters (KNabc) with respect to the ability to grow in the presence of high concentrations of NaCl or LiCl. Ion transport assays in everted vesicles prepared from the KNabc strain expressing NmNhaE from a plasmid confi ...
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Ion Transporter
In biology, a transporter is a transmembrane protein that moves ions (or other small molecules) across a biological membrane to accomplish many different biological functions including, cellular communication, maintaining homeostasis, energy production, etc. There are different types of transporters including, pumps, uniporters, antiporters, and symporters. Active transporters or ion pumps are transporters that convert energy from various sources—including adenosine triphosphate (ATP), sunlight, and other redox reactions—to potential energy by pumping an ion up its concentration gradient. This potential energy could then be used by secondary transporters, including ion carriers and ion channels, to drive vital cellular processes, such as ATP synthesis. This page is focused mainly on ion transporters acting as pumps, but transporters can also function to move molecules through facilitated diffusion. Facilitated diffusion does not require ATP and allows molecules, that are unable ...
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Transmembrane Proteins
A transmembrane protein (TP) is a type of integral membrane protein that spans the entirety of the cell membrane. Many transmembrane proteins function as gateways to permit the transport of specific substances across the membrane. They frequently undergo significant conformational changes to move a substance through the membrane. They are usually highly hydrophobic and aggregate and precipitate in water. They require detergents or nonpolar solvents for extraction, although some of them (beta-barrels) can be also extracted using denaturing agents. The peptide sequence that spans the membrane, or the transmembrane segment, is largely hydrophobic and can be visualized using the hydropathy plot. Depending on the number of transmembrane segments, transmembrane proteins can be classified as single-span (or bitopic) or multi-span (polytopic). Some other integral membrane proteins are called monotopic, meaning that they are also permanently attached to the membrane, but do not pass t ...
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Protein Families
A protein family is a group of evolutionarily related proteins. In many cases, a protein family has a corresponding gene family, in which each gene encodes a corresponding protein with a 1:1 relationship. The term "protein family" should not be confused with family as it is used in taxonomy. Proteins in a family descend from a common ancestor and typically have similar three-dimensional structures, functions, and significant sequence similarity. The most important of these is sequence similarity (usually amino-acid sequence), since it is the strictest indicator of homology and therefore the clearest indicator of common ancestry. A fairly well developed framework exists for evaluating the significance of similarity between a group of sequences using sequence alignment methods. Proteins that do not share a common ancestor are very unlikely to show statistically significant sequence similarity, making sequence alignment a powerful tool for identifying the members of protein familie ...
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Membrane Proteins
Membrane proteins are common proteins that are part of, or interact with, biological membranes. Membrane proteins fall into several broad categories depending on their location. Integral membrane proteins are a permanent part of a cell membrane and can either penetrate the membrane (transmembrane) or associate with one or the other side of a membrane ( integral monotopic). Peripheral membrane proteins are transiently associated with the cell membrane. Membrane proteins are common, and medically important—about a third of all human proteins are membrane proteins, and these are targets for more than half of all drugs. Nonetheless, compared to other classes of proteins, determining membrane protein structures remains a challenge in large part due to the difficulty in establishing experimental conditions that can preserve the correct conformation of the protein in isolation from its native environment. Function Membrane proteins perform a variety of functions vital to the surv ...
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Integral Membrane Proteins
An integral, or intrinsic, membrane protein (IMP) is a type of membrane protein that is permanently attached to the biological membrane. All ''transmembrane proteins'' are IMPs, but not all IMPs are transmembrane proteins. IMPs comprise a significant fraction of the proteins encoded in an organism's genome. Proteins that cross the membrane are surrounded by annular lipids, which are defined as lipids that are in direct contact with a membrane protein. Such proteins can only be separated from the membranes by using detergents, nonpolar solvents, or sometimes denaturing agents. Structure Three-dimensional structures of ~160 different integral membrane proteins have been determined at atomic resolution by X-ray crystallography or nuclear magnetic resonance spectroscopy. They are challenging subjects for study owing to the difficulties associated with extraction and crystallization. In addition, structures of many water-soluble protein domains of IMPs are available in the Prote ...
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Antiporter
An antiporter (also called exchanger or counter-transporter) is a cotransporter and integral membrane protein involved in secondary active transport of two or more different molecules or ions across a phospholipid membrane such as the plasma membrane in opposite directions, one into the cell and one out of the cell. Na+/H+ antiporters have been reviewed. In secondary active transport, one species of solute moves along its electrochemical gradient, allowing a different species to move against its own electrochemical gradient. This movement is in contrast to primary active transport, in which all solutes are moved against their concentration gradients, fueled by ATP. Transport may involve one or more of each type of solute. For example, the Na+/Ca2+ exchanger, found in the plasma membrane of many cells, moves three sodium ions in one direction, and one calcium ion in the other. Role in Homeostatic Mechanisms Na+/H+ Antiporters Antiporters, such as Na+/H+ antiporter protei ...
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Neisseria Meningitidis
''Neisseria meningitidis'', often referred to as meningococcus, is a Gram-negative bacterium that can cause meningitis and other forms of meningococcal disease such as meningococcemia, a life-threatening sepsis. The bacterium is referred to as a coccus because it is round, and more specifically a diplococcus because of its tendency to form pairs. About 10% of adults are carriers of the bacteria in their nasopharynx. As an exclusively human pathogen, it is the main cause of bacterial meningitis in children and young adults, causing developmental impairment and death in about 10% of cases. It causes the only form of bacterial meningitis known to occur epidemically, mainly in Africa and Asia. It occurs worldwide in both epidemic and endemic form. ''N. meningitidis'' is spread through saliva and respiratory secretions during coughing, sneezing, kissing, chewing on toys and through sharing a source of fresh water. It has also been reported to be transmitted through oral sex and cause ...
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Leptospira
''Leptospira'' ( grc, leptos, italics=yes, 'fine, thin' and la, spira, links=no, 'coil') is a genus of spirochaete bacteria, including a small number of pathogenic and saprophytic species. ''Leptospira'' was first observed in 1907 in kidney tissue slices of a leptospirosis victim who was described as having died of "yellow fever". Taxonomy ''Leptospira'', together with the genera ''Leptonema'' and ''Turneria'', is a member of the family Leptospiraceae. The genus ''Leptospira'' is divided into 20 species based on DNA hybridization studies. Pathogenic ''Leptospira'' :''Leptospira alstonii'' Smythe et al. 2013 ''Leptospira alstoni''" Haake et al. 1993:''Leptospira interrogans'' (Stimson 1907) Wenyon 1926 emend. Faine and Stallman 1982 ["''Spirochaeta interrogans''" Stimson 1907; "''Spirochaeta nodosa''" Hubener & Reiter 1916; "''Spirochaeta icterohaemorrhagiae''" Inada et al. 1916; "''Spirochaeta icterogenes''" Uhlenhuth & Fromme 1916; "''Leptospira icteroides''" Noguchi 1919 ...
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Open Reading Frame
In molecular biology, open reading frames (ORFs) are defined as spans of DNA sequence between the start and stop codons. Usually, this is considered within a studied region of a prokaryotic DNA sequence, where only one of the six possible reading frames will be "open" (the "reading", however, refers to the RNA produced by transcription of the DNA and its subsequent interaction with the ribosome in translation). Such an ORF may contain a start codon (usually AUG in terms of RNA) and by definition cannot extend beyond a stop codon (usually UAA, UAG or UGA in RNA). That start codon (not necessarily the first) indicates where translation may start. The transcription termination site is located after the ORF, beyond the translation stop codon. If transcription were to cease before the stop codon, an incomplete protein would be made during translation. In eukaryotic genes with multiple exons, introns are removed and exons are then joined together after transcription to yield the final ...
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Rhizobia
Rhizobia are diazotrophic bacteria that fix nitrogen after becoming established inside the root nodules of legumes (Fabaceae). To express genes for nitrogen fixation, rhizobia require a plant host; they cannot independently fix nitrogen. In general, they are gram negative, motile, non-sporulating rods. Rhizobia are a "group of soil bacteria that infect the roots of legumes to form root nodules". Rhizobia are found in the soil and after infection, produce nodules in the legume where they fix nitrogen gas (N2) from the atmosphere turning it into a more readily useful form of nitrogen. From here, the nitrogen is exported from the nodules and used for growth in the legume. Once the legume dies, the nodule breaks down and releases the rhizobia back into the soil where they can live individually or reinfect a new legume host. History The first known species of rhizobia, '' Rhizobium leguminosarum'', was identified in 1889, and all further species were initially placed in the ''Rhiz ...
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