Residue aspartate-147 from the third transmembrane region of Na(+)/H(+) antiporter NhaB of Vibrio alginolyticus plays a role in its activity

J Bacteriol. 2001 Oct;183(19):5762-7. doi: 10.1128/JB.183.19.5762-5767.2001.

Abstract

NhaB is a bacterial Na(+)/H(+) antiporter with unique topology. The pH dependence of NhaB from Vibrio alginolyticus differs from that of the Escherichia coli NhaB homolog. Replacement of Asp-147 with Glu made high H(+) concentrations a requirement for the NhaB activity. Replacement of Asp-147 with neutral amino acids inactivated NhaB.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Substitution
  • Aspartic Acid / genetics
  • Aspartic Acid / metabolism*
  • Bacterial Proteins*
  • Culture Media
  • Escherichia coli Proteins*
  • Hydrogen / metabolism
  • Membrane Proteins / chemistry*
  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism*
  • Sodium Chloride / metabolism
  • Sodium-Hydrogen Exchangers / chemistry*
  • Sodium-Hydrogen Exchangers / genetics
  • Sodium-Hydrogen Exchangers / metabolism*
  • Vibrio / genetics
  • Vibrio / growth & development
  • Vibrio / metabolism*

Substances

  • Bacterial Proteins
  • Culture Media
  • Escherichia coli Proteins
  • Membrane Proteins
  • NhaB protein, E coli
  • Sodium-Hydrogen Exchangers
  • Aspartic Acid
  • Sodium Chloride
  • Hydrogen