This review reviews the properties and regulation of the Salmonella enterica serovar Typhimurium and Escherichia coli transporters that mediate Mg 2+ influx: CorA and the Mgt P-type ATPases. In addition, potential Mg 2+ regulation of transcription and translation, largely via the PhoPQ two component system, is discussed. CorA proteins are a unique class of transporters and are widespread in the Bacteria and Archaea , with rather distant but functional homologs in eukaryotes. The Mgt transporters are highly homologous to other P-type ATPases but are more closely related to the eukaryotic H + and Ca 2+ ATPases than to most prokaryotic ATPases. Hundreds of homologs of CorA are currently known from genomic sequencing. In contrast, only when extracellular and possibly intracellular Mg 2+ levels fall significantly is the expression of mgtA and mgtB induced. Topology studies using blaM and lacZ fusions initially indicated that the Salmonella serovar Typhimurium CorA contained three transmembrane (TM) segments; however, subsequent data obtained using a variety of approaches showed that the CorA superfamily of proteins have only two TMs at the extreme C terminus. PhoP-PhoQ is a two-component system consisting of PhoQ, the sensor/receptor histidine kinase, and PhoP, the response regulator/transcriptional activator. The expression of both mgtA and mgtCB in either E. coli or Salmonella serovar Typhimurium is markedly induced in a PhoPQ-dependent manner by low concentrations of Mg 2+ in the medium. phoP and phoQ form an operon with two promoters in both E. coli and Salmonella serovar Typhimurium.