EmrAB-TolC multidrug efflux transport complex
An Escherichia coli MFS-family cell-envelope efflux pump complex composed of EmrA, EmrB, and TolC subunits that exports hydrophobic xenobiotics across the inner and outer membranes. [ComplexPortal:CPX-4268]
Synonyms: EmrAB-TolC multidrug efflux transport system
Components
| Component | Type | Part of / acts on | Grounding | Genes | Stoichiometry | Essential | Role |
|---|---|---|---|---|---|---|---|
| Multidrug export protein EmrA | Protein | part of | Reviewed label only (reviewed name; no accession asserted) | emrA | 6 copies in the E. coli K-12 Complex Portal CPX-4268 entry | ESSENTIAL | Periplasmic membrane-fusion adaptor subunit that links EmrB to the TolC outer-membrane channel in the EmrAB-TolC conduit.
|
| Multidrug export protein EmrB | Protein | part of | InterPro:IPR004638 | emrB | 1 copy in the E. coli K-12 Complex Portal CPX-4268 entry | ESSENTIAL | Inner-membrane MFS transporter subunit that forms the EmrAB core and exports hydrophobic xenobiotics through the EmrA/TolC conduit.
|
| Outer membrane channel protein TolC | Protein | part of | InterPro:IPR058622 | tolC | 3 copies in the E. coli K-12 Complex Portal CPX-4268 entry | ESSENTIAL | Trimeric outer-membrane channel constituent that completes the EmrAB-TolC cell-envelope efflux conduit.
|
Organism-specific protein examples
Named proteins in which each component's role was established, with the organism the evidence comes from. The component above is the taxon-agnostic family; these are the specific entries behind it.
Multidrug export protein EmrA
| Accession | Protein | Gene | Organism | Entry |
|---|---|---|---|---|
UniProtKB:P27303 | Multidrug export protein EmrA | emrA | Escherichia coli K-12 (NCBITaxon:83333) | REVIEWED |
Role and evidence (1 reference)
| ||||
Multidrug export protein EmrB
| Accession | Protein | Gene | Organism | Entry |
|---|---|---|---|---|
UniProtKB:P0AEJ0 | Multidrug export protein EmrB | emrB | Escherichia coli K-12 (NCBITaxon:83333) | REVIEWED |
Role and evidence (1 reference)
| ||||
Outer membrane channel protein TolC
| Accession | Protein | Gene | Organism | Entry |
|---|---|---|---|---|
UniProtKB:P02930 | Outer membrane protein TolC | tolC | Escherichia coli K-12 (NCBITaxon:83333) | REVIEWED |
Role and evidence (1 reference)
| ||||
Source composition assertions
EmrAB-TolC multidrug efflux transport system (ComplexPortal:CPX-4268)
Escherichia coli (strain K12) (NCBITaxon:83333) · Heterodecamer · ECO:0005547 · retrieved 2026-10-02
| Participant | Source type | Source name | Stoichiometry |
|---|---|---|---|
UniProtKB:P27303 — Multidrug export protein EmrA | protein | emrA | 6 |
UniProtKB:P0AEJ0 — Multidrug export protein EmrB | protein | emrB | 1 |
UniProtKB:P02930 — Outer membrane protein TolC | protein | tolC | 3 |
Curator-scoped import: E. coli K-12 EmrAB-TolC source composition for this record. Source evidence: inferred by curator. The accession was resolved through the Complex Portal accession endpoint; no equivalence xref was inferred.
Canonical examples
NCBITaxon:83333Escherichia coli K-12 — Source strain for Complex Portal CPX-4268, which curates the heterodecameric EmrAB-TolC pump with six EmrA, one EmrB, and three TolC subunits. [ComplexPortal:CPX-4268]
Functions
- xenobiotic transmembrane transporter activity
GO:0042910— The EmrAB-TolC complex exports hydrophobic xenobiotics across the E. coli inner and outer membranes through the coupled EmrB transporter, EmrA adaptor, and TolC channel.GO:0042910GO:0042910 is the molecular-function term for xenobiotic transmembrane transporter activity.ComplexPortal:CPX-4268Complex Portal cross-references GO:0042910 for the E. coli K-12 EmrAB-TolC multidrug efflux transport system.PMID:33065135Yousefian et al. 2021 structurally characterized the EmrAB-TolC efflux complex from E. coli.
Physical properties
- SUBUNIT_COUNT: 10 (E. coli K-12 6xEmrA:1xEmrB:3xTolC heterodecamer in ComplexPortal:CPX-4268) [
ComplexPortal:CPX-4268]
Mechanism graphs
EmrAB-TolC exports hydrophobic xenobiotics across the cell envelope (FUNCTION)
EmrB, EmrA, and TolC form an envelope-spanning MFS-type efflux pump that exports hydrophobic xenobiotics from E. coli.
| Subject | Predicate | Object | Evidence |
|---|---|---|---|
| Multidrug export protein EmrB | couples to | Multidrug export protein EmrA |
|
| Multidrug export protein EmrA | couples to | Outer membrane channel protein TolC |
|
| EmrAB-TolC multidrug efflux transport complex | enables | xenobiotic transmembrane transporter activity |
|
| xenobiotic transmembrane transporter activity | transports | hydrophobic xenobiotic substrate |
|
| xenobiotic detoxification by transmembrane export across the cell outer membrane | targets | cell exterior |
|
Discussions
- CURATION_TODO (OPEN): Resolve an exact source-neutral EmrA protein family before replacing the reviewed-label-only component row. ComplexPortal:CPX-4268 and the reviewed E. coli K-12 UniProt record exactly identify EmrA, but no InterPro, Pfam, NCBIfam, or GO accession was verified as an exact source-neutral family for this named pump constituent; EmrB and TolC are grounded to InterPro:IPR004638 and InterPro:IPR058622.
Evidence
ComplexPortal:CPX-4268Complex Portal entry for the E. coli K-12 EmrAB-TolC multidrug efflux transport system.GO:1990281Gene Ontology cellular-component parent term for efflux pump complexes.GO:0042910Gene Ontology molecular-function term for xenobiotic transmembrane transporter activity.GO:0140330Gene Ontology biological-process term for xenobiotic detoxification by transmembrane export across the cell outer membrane.InterPro:IPR004638InterPro family entry for Drug resistance transporter EmrB-like.InterPro:IPR058622InterPro family entry for Outer membrane channel protein TolC.UniProtKB:P27303Reviewed E. coli K-12 EmrA UniProtKB entry.UniProtKB:P0AEJ0Reviewed E. coli K-12 EmrB UniProtKB entry.UniProtKB:P02930Reviewed E. coli K-12 TolC UniProtKB entry.PDB:8ZALRCSB Protein Data Bank entry for the EmrAB-TolC MFS-type tripartite multidrug efflux pump EA electron-microscopy model.PMID:33065135PubMed identifier for Yousefian et al. 2021, Structural characterization of the EmrAB-TolC efflux complex from E. coli.DOI:10.1016/j.bbamem.2020.183488DOI for Yousefian et al. 2021, Structural characterization of the EmrAB-TolC efflux complex from E. coli.PMID:12482849PubMed identifier for Borges-Walmsley et al. 2003, Identification of oligomerization and drug-binding domains of the membrane fusion protein EmrA.DOI:10.1074/jbc.M209457200DOI for Borges-Walmsley et al. 2003, Identification of oligomerization and drug-binding domains of the membrane fusion protein EmrA.PMID:41839863PubMed identifier for Zhong et al. 2026, A model for drug transport across two membranes of Gram-negative bacteria by an MFS tripartite assembly.DOI:10.1038/s41467-026-70500-5DOI for Zhong et al. 2026, A model for drug transport across two membranes of Gram-negative bacteria by an MFS tripartite assembly.
Curation history
2026-10-02T10:09:54Zcodex · CREATED_RECORD — Scaffolded by scripts/new_record.py2026-10-02T10:11:12Zcodex · EXPANDED_RECORD — Added CPX-4268/GO efflux-pump parentage, EmrA, EmrB, and TolC component rows with E. coli K-12 reviewed UniProt examples, exact InterPro groundings for EmrB and TolC, PDB/PubMed evidence, a compact xenobiotic export graph, the exact Complex Portal heterodecamer source composition, and an EmrA component-family grounding TODO.
Source: data/structures/other/emrab_tolc_multidrug_efflux_transport_complex.yaml