{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P23895","secondaryAccessions":["Q2MBN8"],"uniProtkbId":"EMRE_ECOLI","entryAudit":{"firstPublicDate":"1991-11-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1991-11-01","entryVersion":187,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Escherichia coli (strain K12)","taxonId":83333,"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"Multidrug transporter EmrE"}},"alternativeNames":[{"fullName":{"value":"Efflux-multidrug resistance protein EmrE"}},{"fullName":{"value":"Ethidium resistance protein"}},{"fullName":{"value":"Methyl viologen resistance protein C"}}]},"genes":[{"geneName":{"value":"emrE"},"synonyms":[{"value":"eb"},{"value":"mvrC"}],"orderedLocusNames":[{"value":"b0543"},{"value":"JW0531"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10681497"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11574548"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15371426"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18024586"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18295794"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22942246"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23042996"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24448799"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29114048"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30287687"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7896833"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9050242"}],"value":"Multidrug efflux protein that confers resistance to a wide range of toxic compounds, including ethidium, methyl viologen, acriflavine, tetraphenylphosphonium (TPP(+)), benzalkonium, propidium, dequalinium and the aminoglycoside antibiotics streptomycin and tobramycin (PubMed:10681497, PubMed:11574548, PubMed:15371426, PubMed:18024586, PubMed:18295794, PubMed:23042996, PubMed:24448799, PubMed:7896833, PubMed:9050242). Can also transport the osmoprotectants betaine and choline (PubMed:22942246). The drug efflux is coupled to an influx of protons (PubMed:15371426, PubMed:29114048, PubMed:7896833). Can couple antiport of a drug to either one or two protons, performing both electrogenic and electroneutral transport of a single substrate (PubMed:29114048). Simultaneously binds and cotransports proton and drug (PubMed:29114048, PubMed:30287687)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24448799"}],"value":"Substrate identity influences both the ground-state and transition-state energies for the conformational exchange process, emphasizing the coupling between substrate binding and transport"}],"commentType":"ACTIVITY REGULATION"},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"maximumVelocities":[{"velocity":1572.0,"unit":"nmol/min/mg","enzyme":"enzyme with methyl viologen as substrate","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7896833"}]}],"michaelisConstants":[{"constant":247.0,"unit":"uM","substrate":"methyl viologen","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7896833"}]}]},"phDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10681497"}],"value":"Optimum pH is 8-8.5. Transport activity occurs from pH 7.5 to 9."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14633977"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14755055"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15111102"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15882076"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17003034"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17005200"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18024586"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20551331"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22178925"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23920359"}],"value":"Homodimer (PubMed:14633977, PubMed:14755055, PubMed:15111102, PubMed:15882076, PubMed:17003034, PubMed:18024586, PubMed:20551331, PubMed:22178925, PubMed:23920359). Forms an antiparallel dimeric structure (PubMed:17005200, PubMed:18024586, PubMed:20551331, PubMed:22178925, PubMed:23920359). Also forms dimers of homodimers (PubMed:14755055)"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"P23895","intActId":"EBI-8789431"},"interactantTwo":{"uniProtKBAccession":"P23895","geneName":"emrE","intActId":"EBI-8789431"},"numberOfExperiments":2,"organismDiffer":false}]},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17005200"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18024586"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20508091"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20551331"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22178925"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23920359"}],"value":"Forms antiparallel homodimers (PubMed:17005200, PubMed:18024586, PubMed:20508091, PubMed:20551331, PubMed:22178925, PubMed:23920359). The topology could be controlled by a single positively charged residue placed in different locations throughout the protein, including the very C terminus (PubMed:20508091)"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15044024"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9688273"}],"value":"Cell inner membrane","id":"SL-0037"},"topology":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15044024"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17005200"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9688273"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18295794"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20551331"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22178925"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24448799"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30287687"}],"value":"Binds different substrates in the same active site (PubMed:18295794, PubMed:22178925). Binding of the substrate induces conformational changes of EmrE (PubMed:18295794, PubMed:20551331, PubMed:22178925). The asymmetric antiparallel homodimer exchanges between inward- and outward-facing states that are identical except that they have opposite orientation in the membrane (PubMed:22178925, PubMed:24448799). The conserved C-terminal tail is strongly coupled to EmrE's drug-binding domain and participates in secondary gating of EmrE-mediated proton/drug transport, occluding the binding pocket of fully protonated EmrE in the absence of drug to prevent dissipative proton transport (PubMed:30287687)"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20308069"}],"value":"Mutants designed to insert with biased topology are functional regardless of the topology"}],"commentType":"MISCELLANEOUS"},{"texts":[{"value":"Encoded by the cryptic lambdoid prophage DLP12"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the drug/metabolite transporter (DMT) superfamily. Small multidrug resistance (SMR) (TC 2.A.7.1) family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"15044024"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"17003034"}],"value":"The membrane insertion topology of the two monomers was controversial and some studies originally suggested a parallel arrangement of the two monomers in the EmrE dimer. The antiparallel dimeric structure is now the generally accepted functional topology"}],"commentType":"CAUTION"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":110,"modifier":"EXACT"}},"description":"Multidrug transporter EmrE","featureId":"PRO_0000108074"},{"type":"Transmembrane","location":{"start":{"value":4,"modifier":"EXACT"},"end":{"value":21,"modifier":"EXACT"}},"description":"Helical; Name=1","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"17005200"}]},{"type":"Transmembrane","location":{"start":{"value":34,"modifier":"EXACT"},"end":{"value":52,"modifier":"EXACT"}},"description":"Helical; Name=2","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"17005200"}]},{"type":"Transmembrane","location":{"start":{"value":58,"modifier":"EXACT"},"end":{"value":80,"modifier":"EXACT"}},"description":"Helical; Name=3","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"17005200"}]},{"type":"Transmembrane","location":{"start":{"value":87,"modifier":"EXACT"},"end":{"value":104,"modifier":"EXACT"}},"description":"Helical; Name=4","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"17005200"}]},{"type":"Site","location":{"start":{"value":4,"modifier":"EXACT"},"end":{"value":4,"modifier":"EXACT"}},"description":"Required for proper coupling between the substrate transport and the proton gradient"},{"type":"Site","location":{"start":{"value":14,"modifier":"EXACT"},"end":{"value":14,"modifier":"EXACT"}},"description":"Essential for translocation and for substrate and proton binding","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"12590142"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"29114048"}]},{"type":"Site","location":{"start":{"value":40,"modifier":"EXACT"},"end":{"value":40,"modifier":"EXACT"}},"description":"Involved in substrate binding"},{"type":"Site","location":{"start":{"value":60,"modifier":"EXACT"},"end":{"value":60,"modifier":"EXACT"}},"description":"Involved in substrate binding"},{"type":"Site","location":{"start":{"value":63,"modifier":"EXACT"},"end":{"value":63,"modifier":"EXACT"}},"description":"Involved in substrate binding"},{"type":"Site","location":{"start":{"value":110,"modifier":"EXACT"},"end":{"value":110,"modifier":"EXACT"}},"description":"Important for activity","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"30287687"}]},{"type":"Mutagenesis","location":{"start":{"value":4,"modifier":"EXACT"},"end":{"value":4,"modifier":"EXACT"}},"description":"Still binds substrate. No transport activity in the presence of a proton gradient, but still transports substrate in the absence of a proton gradient. 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Resistance to toxicants is abolished.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12590142"}],"alternativeSequence":{"originalSequence":"L","alternativeSequences":["C"]}},{"type":"Mutagenesis","location":{"start":{"value":10,"modifier":"EXACT"},"end":{"value":10,"modifier":"EXACT"}},"description":"Still binds substrate, with lower affinity. Resistance to toxicants is abolished.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12590142"}],"alternativeSequence":{"originalSequence":"A","alternativeSequences":["C"]}},{"type":"Mutagenesis","location":{"start":{"value":11,"modifier":"EXACT"},"end":{"value":11,"modifier":"EXACT"}},"description":"Still binds substrate, with lower affinity. 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