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Gene Review

nhaB  -  sodium:proton antiporter

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK1174, JW1175
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Disease relevance of nhaB

  • Physiological role of nhaB, a specific Na+/H+ antiporter in Escherichia coli [1].
  • Here we identified two additional antiporter genes, designated Vc-nhaB and Vc-nhaD, encoding two putative proteins of 530 and 477 residues, respectively, highly homologous to the respective antiporters of Vibrio species and E. coli [2].
  • It has previously been shown that functional expression of CcrA, a metallo-beta-lactamase from Bacteroides fragilis, in Escherichia coli requires a mutation in either dsbA or dsbB, components of a periplasmic disulfide bond-catalyzing system [3].

High impact information on nhaB


Chemical compound and disease context of nhaB

  • We replaced each of these Asp residues by Asn in plasmid encoded nhaA and expressed these constructs in an E. coli mutant defective in both nhA and nhaB [8].

Biological context of nhaB

  • Later, it was concluded that the defective Na+/H+ antiporter in the mutant was the NhaB system, and the nhaB gene was mapped to 25.6 min on the E. coli chromosome [Thelen, P., Tsuchiya, T., and Goldberg, E.B. (1991) J. Bacteriol. 173, 6553-6557] [9].
  • When nhaB was deleted, the fusion gene was expressed at pH values below 8, while the expression was observed at alkaline pH after chaA was deleted [10].
  • The Na+ sensitivity of the delta nhaA delta nhaB mutant bearing the H226R-NhaA plasmid at alkaline pH provided a very powerful tool to isolate revertants and suppressants of H226R growing on high Na+ at alkaline pH [11].

Anatomical context of nhaB

  • Membranes from cells containing multiple dose of nhaB display enhanced Na+/H+ antiporter activity, as measured by the ability of Na+ to collapse a preformed pH gradient or by direct measurement of 22Na+ fluxes [12].

Other interactions of nhaB

  • CONCLUSION: pH regulates a core set of genes independently of oxygen, including yagU, fimbriae, periplasmic chaperones, and nhaB [13].
  • 0. Mutants with defects in nhaB grow normally on agar media containing 0.5 M NaCl, but nhaA mutants are sensitive to 0.5 M NaCl [14].
  • To examine this hypothesis, we applied the phoA fusion method to the cloned nhaB gene [15].

Analytical, diagnostic and therapeutic context of nhaB


  1. Physiological role of nhaB, a specific Na+/H+ antiporter in Escherichia coli. Pinner, E., Kotler, Y., Padan, E., Schuldiner, S. J. Biol. Chem. (1993) [Pubmed]
  2. Roles of NhaA, NhaB, and NhaD Na+/H+ antiporters in survival of Vibrio cholerae in a saline environment. Herz, K., Vimont, S., Padan, E., Berche, P. J. Bacteriol. (2003) [Pubmed]
  3. Dsb-insensitive expression of CcrA, a metallo-beta-lactamase from Bacteroides fragilis, in Escherichia coli after amino acid substitution at two cysteine residues within CcrA. Elksne, L.E., Rasmussen, B.A. J. Bacteriol. (1996) [Pubmed]
  4. Histidine-226 is part of the pH sensor of NhaA, a Na+/H+ antiporter in Escherichia coli. Gerchman, Y., Olami, Y., Rimon, A., Taglicht, D., Schuldiner, S., Padan, E. Proc. Natl. Acad. Sci. U.S.A. (1993) [Pubmed]
  5. Reconstitution of a protein disulfide catalytic system. Bader, M., Muse, W., Zander, T., Bardwell, J. J. Biol. Chem. (1998) [Pubmed]
  6. Observing folding pathways and kinetics of a single sodium-proton antiporter from Escherichia coli. Kedrov, A., Janovjak, H., Ziegler, C., Kuhlbrandt, W., Muller, D.J. J. Mol. Biol. (2006) [Pubmed]
  7. Physiological consequences of expression of the Na+/H+ antiporter sod2 in Escherichia coli. Dibrov, P., Young, P.G., Fliegel, L. Mol. Cell. Biochem. (1998) [Pubmed]
  8. Essential aspartic acid residues, Asp-133, Asp-163 and Asp-164, in the transmembrane helices of a Na+/H+ antiporter (NhaA) from Escherichia coli. Inoue, H., Noumi, T., Tsuchiya, T., Kanazawa, H. FEBS Lett. (1995) [Pubmed]
  9. The NhaB Na+/H+ antiporter is essential for intracellular pH regulation under alkaline conditions in Escherichia coli. Shimamoto, T., Inaba, K., Thelen, P., Ishikawa, T., Goldberg, E.B., Tsuda, M., Tsuchiya, T. J. Biochem. (1994) [Pubmed]
  10. Expression of sodium/proton antiporter NhaA at various pH values in Escherichia coli. Shijuku, T., Saito, H., Kakegawa, T., Kobayashi, H. Biochim. Biophys. Acta (2001) [Pubmed]
  11. Replacements of histidine 226 of NhaA-Na+/H+ antiporter of Escherichia coli. Cysteine (H226C) or serine (H226S) retain both normal activity and pH sensitivity, aspartate (H226D) shifts the pH profile toward basic pH, and alanine (H226A) inactivates the carrier at all pH values. Rimon, A., Gerchman, Y., Olami, Y., Schuldiner, S., Padan, E. J. Biol. Chem. (1995) [Pubmed]
  12. Cloning, sequencing, and expression of the nhaB gene, encoding a Na+/H+ antiporter in Escherichia coli. Pinner, E., Padan, E., Schuldiner, S. J. Biol. Chem. (1992) [Pubmed]
  13. Oxygen limitation modulates pH regulation of catabolism and hydrogenases, multidrug transporters, and envelope composition in Escherichia coli K-12. Hayes, E.T., Wilks, J.C., Sanfilippo, P., Yohannes, E., Tate, D.P., Jones, B.D., Radmacher, M.D., BonDurant, S.S., Slonczewski, J.L. BMC Microbiol. (2006) [Pubmed]
  14. Characterization and mapping of a major Na+/H+ antiporter gene of Escherichia coli. Thelen, P., Tsuchiya, T., Goldberg, E.B. J. Bacteriol. (1991) [Pubmed]
  15. Topological study of Vibrio alginolyticus NhaB Na+/H+ antiporter using gene fusions in Escherichia coli cells. Enomoto, H., Unemoto, T., Nishibuchi, M., Padan, E., Nakamura, T. Biochim. Biophys. Acta (1998) [Pubmed]
  16. A new Na+/H+ antiporter, NhaD, of Vibrio parahaemolyticus. Nozaki, K., Kuroda, T., Mizushima, T., Tsuchiya, T. Biochim. Biophys. Acta (1998) [Pubmed]
  17. Controlled unfolding and refolding of a single sodium-proton antiporter using atomic force microscopy. Kedrov, A., Ziegler, C., Janovjak, H., Kühlbrandt, W., Müller, D.J. J. Mol. Biol. (2004) [Pubmed]
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