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Also transports Li(+) but not K(+), Ca(2+) or Mg(2+)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17693497"}],"value":"Forms a heterooligomeric complex that consists of seven subunits: MrpA, MrpB, MrpC, MrpD, MrpE, MrpF and MrpG"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Cell membrane","id":"SL-0039"},"topology":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"value":"Mrp-dependent antiport apparently occurs by a secondary, proton motive force-dependent mechanism, but the similarity of several Mrp proteins to membrane-embedded subunits of energy-coupled NADH dehydrogenase complexes raises the possibility that there is a capacity for electron transport that could provide a primary energy coupling option for Mrp 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