TCDB is operated by the Saier Lab Bioinformatics Group
TCIDNameDomainKingdom/PhylumProtein(s)
*2.A.33.1.1









NhaA Na+:2H+ antiporter (structure determined and mechanism proposed (Williams, 2000; Hunte et al., 2005; Olkhova et al., 2006; Screpanti et al., 2006; Arkin et al., 2007)). TMS II lines the cation passage, and Asp65 is critical for pH activation of the antiporter (Herz et al., 2010). NhaA is subject to pH-activation of the ion-translocating conformation (Appel et al., 2009; Diab et al., 2011). A periplasm-facing state of the NhaA antiporter suggests the molecular underpinnings of the pH-induced conformational changes (Schushan et al., 2012).  A central unwound part of TMS IV appears to line the cation passage channel (Rimon et al. 2012).  TMSs VI and VII are absent from many homologues, are not required for transport or its regulation and function in assembly and stability (Padan et al. 2015). pH-induced conformational changes have been documented (Kozachkov et al. 2007).

Bacteria
Proteobacteria
NhaA of E. coli
*2.A.33.1.2









NhaA Na+,K+:H+ antiporter (Radchenko et al., 2006)
Bacteria
Proteobacteria
NhaA of Vibrio parahaemolyticus (BAC59491)
*2.A.33.1.3









Na+/H+ antiporter NhaA (Sodium/proton antiporter NhaA)

Bacteria
Proteobacteria
NhaA of Geobacter metallireducens
*2.A.33.1.4









Na+/H+ antiporter NhaA 1 (Sodium/proton antiporter NhaA 1)

Bacteria
Proteobacteria
NhaA1 of Pelobacter propionicus
*2.A.33.1.5









Na+/H+ antiporter (Sodium/proton antiporter), NhaA

Bacteria
Actinobacteria
NhaA of Bifidobacterium longum
*2.A.33.1.6









Na+/H+ antiporter (Sodium/proton antiporter), NhaA

Bacteria
Actinobacteria
NhaA1 of Streptomyces coelicolor / M145)