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2.A.37.2.7
Na+/H+ antiporter of 386 aas and 13 predicted TMSs, NapA. The 3-d structure is known (PDB# 4BWZ; 4BZ2; 4BZ3).  In the NapA structure, the core and dimerization domains are in different positions to those seen in the E. coli NhaA, and a negatively charged cavity is open to the outside. The extracellular cavity allows access to a strictly conserved aspartate residue thought to coordinate ion binding directly. To alternate access to this ion-binding site, however, requires a surprisingly large rotation of the core domain, some 20° against the dimerization interface (Lee et al. 2013). A  transmembrane lysine residue is essential for electrogenic transport in this and related Na+/H+ antiporters(Uzdavinys et al. 2017).

Accession Number:Q5SIA2
Protein Name:Na(+)/H(+) antiporter
Length:386
Molecular Weight:40286.00
Species:Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) [300852]
Number of TMSs:13
Substrate Na+, H+

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MHGAEHLLEI FYLLLAAQVM AFIFKRLNQP VVIGEVLAGV LVGPALLGLV HEGEILEFLA 
61:	ELGAVFLLFM VGLETRLKDI LAVGKEAFLV AVLGVALPFL GGYLYGLEIG FETLPALFLG 
121:	TALVATSVGI TARVLQELGV LSRPYSRIIL GAAVIDDVLG LIVLAVVNGV AETGQVEVGA 
181:	ITRLIVLSVV FVGLAVFLST LIARLPLERL PVGSPLGFAL ALGVGMAALA ASIGLAPIVG 
241:	AFLGGMLLSE VREKYRLEEP IFAIESFLAP IFFAMVGVRL ELSALASPVV LVAGTVVTVI 
301:	AILGKVLGGF LGALTQGVRS ALTVGVGMAP RGEVGLIVAA LGLKAGAVNE EEYAIVLFMV 
361:	VFTTLFAPFA LKPLIAWTER ERAAKE