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Protein

Multidrug export protein EmrA

Gene

emrA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Part of the tripartite efflux system EmrAB-TolC, which confers resistance to antibiotics such as CCCP, FCCP, 2,4-dinitrophenol and nalidixic acid. EmrA is a drug-binding protein that provides a physical link between EmrB and TolC.2 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Antibiotic resistance, Transport

Enzyme and pathway databases

BioCyciEcoCyc:EG11354-MONOMER.
ECOL316407:JW2660-MONOMER.

Protein family/group databases

TCDBi8.A.1.1.1. the membrane fusion protein (mfp) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Multidrug export protein EmrA
Gene namesi
Name:emrA
Ordered Locus Names:b2685, JW2660
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11354. emrA.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2424CytoplasmicSequence analysisAdd
BLAST
Transmembranei25 – 4521HelicalSequence analysisAdd
BLAST
Topological domaini46 – 390345PeriplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • intrinsic component of periplasmic side of plasma membrane Source: EcoCyc
  • intrinsic component of plasma membrane Source: EcoliWiki
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 390390Multidrug export protein EmrAPRO_0000201869Add
BLAST

Proteomic databases

PaxDbiP27303.
PRIDEiP27303.

Interactioni

Subunit structurei

Homodimer and homotrimer. Part of the tripartite efflux system EmrAB-TolC, which is composed of an inner membrane transporter, EmrB, a periplasmic membrane fusion protein, EmrA, and an outer membrane component, TolC. The complex forms a large protein conduit and can translocate molecules across both the inner and outer membranes. Interacts with EmrB. EmrAB complex forms a dimer in vitro.3 Publications

Protein-protein interaction databases

BioGridi4262946. 195 interactions.
DIPiDIP-9502N.
IntActiP27303. 2 interactions.
STRINGi511145.b2685.

Structurei

3D structure databases

ProteinModelPortaliP27303.
SMRiP27303. Positions 52-348.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili120 – 18061Sequence analysisAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105CW7. Bacteria.
COG1566. LUCA.
HOGENOMiHOG000112072.
InParanoidiP27303.
KOiK03543.
OMAiRQLMINS.
OrthoDBiEOG6C014B.
PhylomeDBiP27303.

Family and domain databases

InterProiIPR005694. Emr.
IPR032317. HlyD_D23.
IPR006143. RND_pump_MFP.
[Graphical view]
PfamiPF00529. HlyD. 1 hit.
PF16576. HlyD_D23. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00998. 8a0101. 1 hit.

Sequencei

Sequence statusi: Complete.

P27303-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSANAETQTP QQPVKKSGKR KRLLLLLTLL FIIIAVAIGI YWFLVLRHFE
60 70 80 90 100
ETDDAYVAGN QIQIMSQVSG SVTKVWADNT DFVKEGDVLV TLDPTDARQA
110 120 130 140 150
FEKAKTALAS SVRQTHQLMI NSKQLQANIE VQKIALAKAQ SDYNRRVPLG
160 170 180 190 200
NANLIGREEL QHARDAVTSA QAQLDVAIQQ YNANQAMILG TKLEDQPAVQ
210 220 230 240 250
QAATEVRNAW LALERTRIIS PMTGYVSRRA VQPGAQISPT TPLMAVVPAT
260 270 280 290 300
NMWVDANFKE TQIANMRIGQ PVTITTDIYG DDVKYTGKVV GLDMGTGSAF
310 320 330 340 350
SLLPAQNATG NWIKVVQRLP VRIELDQKQL EQYPLRIGLS TLVSVNTTNR
360 370 380 390
DGQVLANKVR STPVAVSTAR EISLAPVNKL IDDIVKANAG
Length:390
Mass (Da):42,736
Last modified:November 1, 1997 - v2
Checksum:i0FB9AE8C20A270F9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti62 – 621I → M in AAA23724 (PubMed:1409590).Curated
Sequence conflicti138 – 1381K → Q in AAA23724 (PubMed:1409590).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M86657 Genomic DNA. Translation: AAA23724.1.
U00096 Genomic DNA. Translation: AAC75732.1.
AP009048 Genomic DNA. Translation: BAA16547.1.
PIRiF65048.
RefSeqiNP_417170.1. NC_000913.3.
WP_001326681.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75732; AAC75732; b2685.
BAA16547; BAA16547; BAA16547.
GeneIDi947166.
KEGGiecj:JW2660.
eco:b2685.
PATRICi32120764. VBIEscCol129921_2779.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M86657 Genomic DNA. Translation: AAA23724.1.
U00096 Genomic DNA. Translation: AAC75732.1.
AP009048 Genomic DNA. Translation: BAA16547.1.
PIRiF65048.
RefSeqiNP_417170.1. NC_000913.3.
WP_001326681.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP27303.
SMRiP27303. Positions 52-348.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262946. 195 interactions.
DIPiDIP-9502N.
IntActiP27303. 2 interactions.
STRINGi511145.b2685.

Protein family/group databases

TCDBi8.A.1.1.1. the membrane fusion protein (mfp) family.

Proteomic databases

PaxDbiP27303.
PRIDEiP27303.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75732; AAC75732; b2685.
BAA16547; BAA16547; BAA16547.
GeneIDi947166.
KEGGiecj:JW2660.
eco:b2685.
PATRICi32120764. VBIEscCol129921_2779.

Organism-specific databases

EchoBASEiEB1329.
EcoGeneiEG11354. emrA.

Phylogenomic databases

eggNOGiENOG4105CW7. Bacteria.
COG1566. LUCA.
HOGENOMiHOG000112072.
InParanoidiP27303.
KOiK03543.
OMAiRQLMINS.
OrthoDBiEOG6C014B.
PhylomeDBiP27303.

Enzyme and pathway databases

BioCyciEcoCyc:EG11354-MONOMER.
ECOL316407:JW2660-MONOMER.

Miscellaneous databases

PROiP27303.

Family and domain databases

InterProiIPR005694. Emr.
IPR032317. HlyD_D23.
IPR006143. RND_pump_MFP.
[Graphical view]
PfamiPF00529. HlyD. 1 hit.
PF16576. HlyD_D23. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00998. 8a0101. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Emr, an Escherichia coli locus for multidrug resistance."
    Lomovskaya O., Lewis K.
    Proc. Natl. Acad. Sci. U.S.A. 89:8938-8942(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION.
  2. "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
    Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T.
    , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
    DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Multidrug resistance pumps in bacteria: variations on a theme."
    Lewis K.
    Trends Biochem. Sci. 19:119-123(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  6. "Identification of oligomerization and drug-binding domains of the membrane fusion protein EmrA."
    Borges-Walmsley M.I., Beauchamp J., Kelly S.M., Jumel K., Candlish D., Harding S.E., Price N.C., Walmsley A.R.
    J. Biol. Chem. 278:12903-12912(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
  7. "The multidrug resistance efflux complex, EmrAB from Escherichia coli forms a dimer in vitro."
    Tanabe M., Szakonyi G., Brown K.A., Henderson P.J., Nield J., Byrne B.
    Biochem. Biophys. Res. Commun. 380:338-342(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EMRB.
  8. Cited for: INTERACTION WITH TOLC.

Entry informationi

Entry nameiEMRA_ECOLI
AccessioniPrimary (citable) accession number: P27303
Secondary accession number(s): P77356
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: November 1, 1997
Last modified: January 20, 2016
This is version 129 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.