2.A.36.6.9 Na+/H+ antiporter, NhaP, of 443 aas. Several 3-d structures are known (Wöhlert et al. 2014). The ion is coordinated by three acidic side chains, a water molecule, a
serine and a main-chain carbonyl in an unwound stretch of TMS 5 at the deepest point of a negatively charged
cytoplasmic funnel. A second narrow polar channel may facilitate proton uptake from the cytoplasm. Transport activity is cooperative
at pH 6 but not at pH 5, due to pH-dependent allosteric
coupling of protomers through two histidines at the dimer interface (Wöhlert et al. 2014).
|
Accession Number: | Q9UZ55 |
Protein Name: | Na+/H+ antiporter, putative |
Length: | 443 |
Molecular Weight: | 49188.00 |
Species: | Pyrococcus abyssi (strain GE5 / Orsay) [272844] |
Number of TMSs: | 13 |
Substrate |
sodium(1+), hydron |
---|
1: MIELSLAEAL FLILFTGVIS MLISRRTGIS YVPIFILTGL VIGPLLKLIP RDLAHEIFDF
61: VRVFGLVIIL FTEGHNLSWR LLKKNMPTIV TLDTIGLILT ALIAGFIFKV VFNSSFLLGF
121: LFGAIIGATD PATLIPLFRQ YRVKQDIETV IVTESIFNDP LGIVLTLIAI SMLVPGYGGG
181: IFSTLSEKLG IYAGGVIYFL YNVSVSISLG IFLGILGYKF IKRTGIFDFP EIEAFSLSLA
241: FLGFFIGERL DASGYLVATV TGIVLGNYKL LKPRENIRIL KRLQRAIEKE VHFNDTLAAL
301: ATIFIFVLLG AEMNLEVIWS NLGKGLLVAL GVMILARPLA TLPLLKWWNF REYLFIALEG
361: PRGVVPSALA SLPLSLALKY KSPLLTVHWG EIIMATVVIT VLTSVIVETL WIPILKDKLD
421: VGETIKERIE EKEEEKERRK VRG