Matches in DBpedia 2015-10 for { ?s ?p "Na+/H+ antiporter 1 family contains a number of bacterial sodium-proton antiporter (SPAP) 1 proteins. These are integral membrane proteins that catalyse the exchange of H+ for Na+ in a manner that is highly dependent on the pH.In particular, the Escherichia coli NhaA Na+:H+ Antiporter (NhaA) protein probably functions in the regulation of the internal pH when the external pH is alkaline. It also uses the H+ gradient to expel Na+ from the cell. Its activity is highly pH dependent.A model of the Last Universal Common Ancestor (LUCA) of all life on Earth suggests a SPAP was crucial for extracting energy from the natural proton gradients across the surface of underwater hydrothermal vents. A SPAP could have increased by 60% the free energy obtainable from proton gradients through a hypothesized leaky proto-membrane of LUCA; and a SPAP would have increasingly assisted proton pump efficiency in the less permeable membranes of LUCA's descendants, Archaea and Bacteria."@en }
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- proton_antiporter_1 abstract "Na+/H+ antiporter 1 family contains a number of bacterial sodium-proton antiporter (SPAP) 1 proteins. These are integral membrane proteins that catalyse the exchange of H+ for Na+ in a manner that is highly dependent on the pH.In particular, the Escherichia coli NhaA Na+:H+ Antiporter (NhaA) protein probably functions in the regulation of the internal pH when the external pH is alkaline. It also uses the H+ gradient to expel Na+ from the cell. Its activity is highly pH dependent.A model of the Last Universal Common Ancestor (LUCA) of all life on Earth suggests a SPAP was crucial for extracting energy from the natural proton gradients across the surface of underwater hydrothermal vents. A SPAP could have increased by 60% the free energy obtainable from proton gradients through a hypothesized leaky proto-membrane of LUCA; and a SPAP would have increasingly assisted proton pump efficiency in the less permeable membranes of LUCA's descendants, Archaea and Bacteria.".