Residue aspartate-147 from the third transmembrane region of Na(+)/H(+) antiporter NhaB of Vibrio alginolyticus plays a role in its activity.
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.
Nakamura
T
T
Laboratory of Molecular Cell Biology, Faculty of Pharmaceutical Sciences, Chiba University, Inage-ku, Chiba 263-8522, Japan. tnakha@p.chiba-u.ac.jp
Fujisaki
Y
Y
Enomoto
H
H
Nakayama
Y
Y
Takabe
T
T
Yamaguchi
N
N
Uozumi
N
N
D019943:Amino Acid Substitution; D001224:Aspartic Acid / Q000235:genetics / Q000378:metabolism*; D001426:Bacterial Proteins; D003470:Culture Media; D029968:Escherichia coli Proteins; D006859:Hydrogen / Q000378:metabolism; D008565:Membrane Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D012965:Sodium Chloride / Q000378:metabolism; D017923:Sodium-Hydrogen Exchangers / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D014733:Vibrio / Q000235:genetics / Q000254:growth & development / Q000378:metabolism*
D001426:Bacterial Proteins; D003470:Culture Media; D029968:Escherichia coli Proteins; D008565:Membrane Proteins; C491047:NhaB protein, E coli; D017923:Sodium-Hydrogen Exchangers; D001224:Aspartic Acid; D012965:Sodium Chloride; D006859:Hydrogen