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Changing 14 residues in the active site of NPr can change its function to that of HPr and P-type ATPase analysis in archaea, spirochetes and across all known domains of life

Abstract

NPr, a bacterial protein functioning in the regulation of nitrogen metabolism, was engineered to take on the function of its evolutionary homolog HPr, a bacterial protein involved in the uptake up of sugars through the PTS. This was achieved by replacing 14 amino acyl residues in NPr with the corresponding residues from HPr. These residues are all present at the active interface between HPr with the Mannitol Enzyme IIA and NPr with the nitrogen regulating IIA. This modified NPr gene was able to complement HPr negative mutants for growth on all PTS sugars. For sugars exclusive to the Mannose Enzyme II complex Family, the modified NPr protein out performed the wild type HPr. P-type ATPases, ion transporting pumps, are ubiquitous in nearly all organisms. This paper presents the bioinformatic analysis of these proteins in two organismal groups, the archaea and spirochetes. These studies involved phylogenetic, size, topological, conserved motif, familial and functional analyses. They also present the conclusions involving the analysis of P- type ATPases from organisms encompassing the three domains of life, bacteria, archaea and eukarya. Integration of protein sequence information provided evolutionary, distributional and functional insight into characterized as well as previously unidentified families of P-type ATPases

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