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Internal bacterial concentration of Mg
2+
, the most abundant divalent cation in living cells, is estimated to be in the single millimolar range. However, many bacteria will thrive in media with only micromolars of Mg
2+
, by using a range of intensely studied and highly efficient import mechanisms, as well as in media with very high magnesium concentration, presumably mediated by currently unknown export mechanisms.
Staphylococcus aureus
has a particularly high Mg
2+
tolerance for a pathogen, growing unimpaired in up to 770 mM Mg
2+
, and we here identify SA0657, a key factor in this tolerance. The predicted domain structure of SA0657 is shared with a large number of proteins in bacteria, archaea and even eukarya, for example CorB from
Salmonella
and the human CNNM protein family. One of the shared domains, a CBS pair potentially involved in Mg
2+
sensing, contains the conserved Glycine326 which we establish to be a key residue for SA0657 function. In light of our findings, we propose the name MpfA, Magnesium Protection Factor A, for SA0657.