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AntiportersEscherichia coli ProteinsPotassium-Hydrogen AntiportersSodium-Hydrogen AntiporterEscherichia coliEscherichia coli InfectionsMolecular Sequence DataBacterial ProteinsZygosaccharomycesGenes, BacterialAmino Acid SequenceEscherichia coli O157Metals, AlkaliHydrogen-Ion ConcentrationCloning, MolecularBase SequenceMutationDNA, BacterialLithiumPlasmidsEscherichia coli K12Cations, MonovalentSodiumSodium ChlorideEscherichiaGenetic Complementation TestSequence Homology, Amino AcidKineticsAlkaliesAdhesins, Escherichia coliGene Expression Regulation, BacterialLithium ChlorideRecombinant ProteinsCation Transport ProteinsSaltsProton PumpsYarrowiaOperonPotassiumBiological TransportCarrier ProteinsHydrogenIon TransportCationsMutagenesis, Site-DirectedSubstrate SpecificityProtonsVacuolesChromosomes, BacterialRNA, BacterialMembrane Transport ProteinsModels, MolecularPhylogenyProtein ConformationCell MembraneBacterial Outer Membrane ProteinsSaccharomyces cerevisiaeColiphagesMembrane ProteinsBacillusProteolipidsGenesProtein Structure, SecondaryRestriction MappingHomeostasisElectron Transport Complex IEnterotoxigenic Escherichia coliBinding SitesChloride ChannelsShiga-Toxigenic Escherichia coliCulture MediaTemperatureAnti-Bacterial AgentsBacterial ToxinsEnteropathogenic Escherichia coliConjugation, GeneticFimbriae, BacterialElectrophoresis, Polyacrylamide GelTranscription, GeneticEnterotoxinsBacterial AdhesionEnterohemorrhagic Escherichia coliArabidopsisRecombinant Fusion ProteinsMolecular WeightDrug Resistance, Microbialbeta-GalactosidaseUropathogenic Escherichia coliChromosome MappingEscherichia coli VaccinesChloramphenicolBacteriophage lambdaDiarrheaModels, BiologicalProtein BindingFecesDNA-Directed RNA PolymerasesTransduction, GeneticSequence Analysis, DNAFimbriae Proteins

NhaA from EscherichiaGenes of Escherichia coliTransporter of Escherichia coliSodium-protonProtonTransportersMG1655Succinate antiporterColi genomeProteinBacteriaBacillusCationInner membraneVibrioProteomeGlutamateHomologousStrainsBiochemistrySpeciesGeneSequenceProteinsSystemModelComplexCrystalTransportFamilyActiveEssential

NhaA from Escherichia3

• Here, we report a crystal form of the prototypical sodium-proton antiporter NhaA from Escherichia coli in which the protein is seen as a dimer. (bvsalud.org)
• Nevertheless, extensive analysis on the model Na + /H + antiporter NhaA from Escherichia coli, has shown that residues on the cytoplasmic surface, termed the pH sensor, shifts the pH at which NhaA becomes active. (elsevierpure.com)
• Nevertheless, extensive analysis on the model Na+/H+ antiporter NhaA from Escherichia coli, has shown that residues on the cytoplasmic surface, termed the pH sensor, shifts the pH at which NhaA becomes active. (elsevierpure.com)

Genes of Escherichia coli1

• Nucleotide sequences of the fumarase (fumC) and aspartase (aspA) genes of Escherichia coli K12. (tcdb.org)

Transporter of Escherichia coli1

• 9] "Topological analysis of DcuA, an anaerobic C4-dicarboxylate transporter of Escherichia coli. (tcdb.org)

Sodium-proton7

• Alternative proton-binding site and long-distance coupling in Escherichia coli sodium-proton antiporter NhaA. (computchem.org)
• Mechanism of pH-dependent activation of the sodium-proton antiporter NhaA. (computchem.org)
• Escherichia coli NhaA is a prototype sodium-proton antiporter, which has been extensively characterized by X-ray crystallography, biochemical and biophysical experiments. (computchem.org)
• Sodium-proton antiporters rapidly exchange protons and sodium ions across the membrane to regulate intracellular pH, cell volume, and sodium concentration. (bvsalud.org)
• With MemStar, we have been able to obtain new structural information for several transporters, including the sodium/proton antiporter NapA. (bvsalud.org)
• Sodium/proton (Na(+)/H(+)) antiporters, located at the plasma membrane in every cell, are vital for cell homeostasis. (bvsalud.org)
• The SMF is generated by primary sodium pumps (e.g. sodium/potassium ATPases, sodium translocating respiratory chain complexes) or via the action of sodium/proton antiporters. (embl.de)

Proton3

• To pave the way, we demonstrated that CpHMD can directly reveal the atomic details of the pH-dependent conformational transitions of a proton channel, an antiporter, and a multi-drug efflux pump. (computchem.org)
• Department of Pharmacology and Systems Therapeutics, Mount Sinai School of Medicine, New York, NY, USA Multiple resistance and pH adaptation (Mrp) antiporters are widely distributed in various prokaryotes and have been reported to function as a hetero-oligomeric monovalent cation/proton antiporter, which exchanges a cytoplasmic monovalent cation (Na+, Li+, and/or K+) with extracellular H+. (mirnamimic.com)
• Here, we report that the Mrp antiporter click here from the thermophilic gram-negative bacterium, Thermomicrobium roseum, does not catalyze monovalent cation/proton antiport like the Mrp antiporters studied to date, but catalyzes Ca2+/H+ antiport in Escherichia coli membrane vesicles. (mirnamimic.com)

Transporters1

• 2] "Escherichia coli possesses two homologous anaerobic C4-dicarboxylate membrane transporters (DcuA and DcuB) distinct from the aerobic dicarboxylate transport system (Dct). (tcdb.org)

MG16552

• 5] "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. (tcdb.org)
• MG1655, Escherichia coli MG1655, Escherichia coli str. (string-db.org)

Succinate antiporter1

• Escherichia coli catabolizes L-tartrate under anaerobic conditions to oxaloacetate by the use of L-tartrate/succinate antiporter TtdT and L-tartrate dehydratase TtdAB. (ewha.ac.kr)

Coli genome2

• 3] "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes. (tcdb.org)
• 3, 137-155 (1996) REFERENCE 9 AUTHORS Fujita,N., Mori,H., Yura,T. and Ishihama,A. TITLE Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region JOURNAL Nucleic Acids Res. (nig.ac.jp)

Protein2

• A secondary structure model of PutP from Escherichia coli suggests the protein contains 13 TMs with the N terminus located on the periplasmic side of the membrane and the C terminus facing the cytoplasm. (embl.de)
• ACCESSION AP009048-129 PROTEIN_ID BAB96710.2 SOURCE Escherichia coli str. (nig.ac.jp)

Bacteria1

• Glucose is the essential carbon source for growing and cultivating heterotrophic bacteria, such as Escherichia coli , for laboratory and production purposes. (encyclopedia.pub)

Bacillus1

• 261 essential genes from Bacillus subtilis , codon optimized for Escherichia coli in MoClo-compatible high-copy ampicillin resistance backbones. (freegenes.org)

Cation1

• Steuber, J. The Na+ -translocating NADH:quinone oxidoreductase (NDH I) from Klebsiella pneumoniae and Escherichia coli: implications for the mechanism of redox-driven cation translocation by complex I. (uzh.ch)

Inner membrane1

• 10] "Global topology analysis of the Escherichia coli inner membrane proteome. (tcdb.org)

Vibrio1

• NorM is a member of the multidrug and toxic compound extrusion (MATE) family and functions as a Na + /multidrug antiporter in Vibrio parahaemolyticus, although the underlying mechanism of the Na + /multidrug antiport is unknown. (elsevierpure.com)

Proteome1

• The current study elucidates and compares the changes in the membrane proteome of Escherichia coli in response to a range of alcohols. (biomedcentral.com)

Glutamate2

• Collaborative regulation of Escherichia coli glutamate-dependent acid resistance by two AraC-like regulators, GadX and GadW (YhiW). (drugbank.com)
• One very efficient E. coli acid resistance system encompasses two isoforms of glutamate decarboxylase (gadA and gadB) and a putative glutamate:gamma-amino butyric acid (GABA) antiporter (gadC). (drugbank.com)

Homologous2

• The typical bacterial scenario seemed to be a two-component sHsps system of two homologous sHsps, such as the Escherichia coli sHsps IbpA and IbpB. (cipsm.de)
• 1] "Construction and properties of Escherichia coli mutants defective in two genes encoding homologous membrane proteins with putative roles in anaerobic C4-dicarboxylic acid transport. (tcdb.org)

Strains1

• Bioinformatics comparisons of RNA-binding proteins of pathogenic and non-pathogenic Escherichia coli strains reveal novel virulence factors. (ncbs.res.in)

Biochemistry1

• To answer these questions, we will combine biochemistry with site-directed and selection-driven mutagenesis of UhpT, a model transporter in Escherichia coli, We plan four kinds of experiments. (grantome.com)

Species3

• species= Escherichia coli str. (lbl.gov)
• In this regard, Escherichia coli is of special interest, since it is genetically tractable and the most well-understood bacterial species that is widely considered for commercial biofuel production [ 6 , 7 ]. (biomedcentral.com)
• 2020. Distinct Evolutionary Origins of Intron Retention Splicing Events in Antiporter Transcripts Relate to Sequence Specific Distinctions in Species. . (ncbs.res.in)

Gene2

• 8] "Nucleotide sequence of the FNR-regulated fumarase gene (fumB) of Escherichia coli K-12. (tcdb.org)
• The codon table used was the FreqB table from " Design Parameters to Control Synthetic Gene Expression in Escherichia coli ", which was used because it was shown to express proteins well and was recommended to us by JCVI. (freegenes.org)

Sequence1

• 4] "The complete genome sequence of Escherichia coli K-12. (tcdb.org)

Proteins2

• Here, we present a simple overexpression condition for high-throughput screening of membrane proteins in Escherichia coli. (bvsalud.org)
• Escherichia coli is the best-known model for the biotechnological production of many biotechnological products, including housekeeping and heterologous primary and secondary metabolites and recombinant proteins, and is an efficient biofactory model to produce biofuels to nanomaterials. (encyclopedia.pub)

System1

• Here we demonstrate that NarK is a nitrate/nitrite antiporter, using an in vitro reconstituted system. (nurekilab.net)

Model1

• The structure and function of the cadaverine-lysine antiporter, CadB (2.A.3.2.2), and the putrescine-ornithine antiporter, PotE (2.A.3.2.1), in E. coli have been evaluated using model structures based on the crystal structure of AdiC (2.A.3.2.5), an agmatine-arginine antiporter. (tcdb.org)

Complex1

• Steuber, J. The C-terminally truncated NuoL subunit (ND5 homologue) of the Na+ -dependent complex I from Escherichia coli transports Na+. (uzh.ch)

Crystal1

• Furthermore, we present the high-resolution crystal structures of NarK from Escherichia coli in the nitrate-bound occluded, nitrate-bound inward-open and apo inward-open states. (nurekilab.net)

Transport2

• Carreón-Rodríguez OE, Gosset G, Escalante A, Bolívar F. Dynamics of Glucose Transport in Escherichia coli . (encyclopedia.pub)
• Dynamics of Glucose Transport in Escherichia coli " Encyclopedia , https://encyclopedia.pub/entry/46077 (accessed November 28, 2023). (encyclopedia.pub)

Family2

• The Basic Amino Acid Antiporter (ArcD) family (TC# 2.A.118) is a constituent of the IT superfamily. (wikipedia.org)
• Portal: Biology As of this edit, this article uses content from "2.A.118 The Basic Amino Acid Antiporter (ArcD) Family", which is licensed in a way that permits reuse under the Creative Commons Attribution-ShareAlike 3.0 Unported License, but not under the GFDL. (wikipedia.org)

Active1

• Tn5085 is functionally active in Escherichia coli. (dadospdf.com)

Essential1

• All the essential genes have been recorded for expression in Escherichia coli and have been made MoClo compatible. (freegenes.org)