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Details on Person UniProt:P23895 emrE
| Class:Id | ReferenceGeneProduct:9931579 |
|---|---|
| _chainChangeLog | chain:1-110 for 9931579 added on Fri Feb 21 2025 |
| _displayName | UniProt:P23895 emrE |
| _timestamp | 2025-02-21 18:36:18 |
| chain | chain:1-110 |
| checksum | 775153FC47D6AE3D |
| comment | FUNCTION 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).ACTIVITY REGULATION Substrate identity influences both the ground-state and transition-state energies for the conformational exchange process, emphasizing the coupling between substrate binding and transport.BIOPHYSICOCHEMICAL PROPERTIES Optimum pH is 8-8.5. Transport activity occurs from pH 7.5 to 9.SUBUNIT 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).INTERACTION 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).DOMAIN 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).MISCELLANEOUS Mutants designed to insert with biased topology are functional regardless of the topology.MISCELLANEOUS Encoded by the cryptic lambdoid prophage DLP12.SIMILARITY Belongs to the drug/metabolite transporter (DMT) superfamily. Small multidrug resistance (SMR) (TC 2.A.7.1) family.CAUTION 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. |
| created | [InstanceEdit:9931555] Stephan, Ralf, 2024-12-12 |
| description | recommendedName: Multidrug transporter EmrE alternativeName: Efflux-multidrug resistance protein EmrE alternativeName: Ethidium resistance protein alternativeName: Methyl viologen resistance protein C |
| geneName | emrE eb mvrC b0543 JW0531 |
| identifier | P23895 |
| isSequenceChanged | FALSE |
| keyword | 3D-structure Antiport Cell inner membrane Cell membrane Membrane Reference proteome Transmembrane Transmembrane helix Transport |
| modified | [InstanceEdit:9939033] Weiser, Joel, 2025-02-21 |
| name | emrE |
| referenceDatabase | [ReferenceDatabase:2] UniProt |
| secondaryIdentifier | EMRE_ECOLI Q2MBN8 |
| sequenceLength | 110 |
| species | [Species:159879] Escherichia coli |
| (referenceEntity) | [EntityWithAccessionedSequence:9931575] EmrE [plasma membrane] [Escherichia coli] |
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No pathways have been reviewed or authored by UniProt:P23895 emrE (9931579)
