The Mrp system: A giant among monovalent cation/proton antiporters?

Talia H. Swartz, Sayuri Ikewada, Osamu Ishikawa, Masahiro Ito, Terry Ann Krulwich

Research output: Contribution to journalShort surveypeer-review

136 Scopus citations


Mrp systems are a novel and broadly distributed type of monovalent cation/proton antiporter of bacteria and archaea. Monovalent cation/proton antiporters are membrane transport proteins that catalyze efflux of cytoplasmic sodium, potassium or lithium ions in exchange for external hydrogen ions (protons). Other known monovalent cation antiporters are single gene products, whereas Mrp systems have been proposed to function as hetero-oligomers. A mrp operon typically has six or seven genes encoding hydrophobic proteins all of which are required for optimal Mrp-dependent sodium-resistance. There is little sequence similarity of Mrp proteins to other antiporters but three of these proteins have significant sequence similarity to membrane embedded subunits of ion-translocating electron transport complexes. Mrp antiporters have essential roles in the physiology of alkaliphilic and neutralophilic Bacillus species, nitrogen-fixing Sinorhizobium meliloti and in the pathogen Staphylococcus aureus, although these bacteria contain multiple monovalent cation/proton antiporters. The wide distribution of Mrp systems leads to the anticipation of important roles in an even wider variety of pathogens, extremophiles and environmentally important organisms. Here, the distribution, established physiological roles and catalytic activities of Mrp systems are reviewed, hypotheses regarding their complexity are discussed and major open questions about their function are highlighted.

Original languageEnglish
Pages (from-to)345-354
Number of pages10
Issue number5
StatePublished - Oct 2005


  • Alkaliphilic Bacillus
  • Hetero-oligomeric antiporter
  • Monovalent cation/proton antiporter
  • Mrp
  • Na/H Antiporter
  • pH Homeostasis


Dive into the research topics of 'The Mrp system: A giant among monovalent cation/proton antiporters?'. Together they form a unique fingerprint.

Cite this