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Protein

Multidrug export protein EmrB

Gene

emrB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 3 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.2 Publications

GO - Biological processi

  • response to antibiotic Source: UniProtKB-KW
  • response to toxic substance Source: EcoCyc
  • transmembrane transport Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Antibiotic resistance, Transport

Enzyme and pathway databases

BioCyciEcoCyc:EMRB-MONOMER.
ECOL316407:JW2661-MONOMER.

Protein family/group databases

TCDBi2.A.1.3.2. the major facilitator superfamily (mfs).

Names & Taxonomyi

Protein namesi
Recommended name:
Multidrug export protein EmrB
Gene namesi
Name:emrB
Ordered Locus Names:b2686, JW2661
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11439. emrB.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1212CytoplasmicSequence analysisAdd
BLAST
Transmembranei13 – 3826HelicalSequence analysisAdd
BLAST
Topological domaini39 – 5113ExtracellularSequence analysisAdd
BLAST
Transmembranei52 – 7221HelicalSequence analysisAdd
BLAST
Topological domaini73 – 819CytoplasmicSequence analysis
Transmembranei82 – 10019HelicalSequence analysisAdd
BLAST
Topological domaini101 – 1099ExtracellularSequence analysis
Transmembranei110 – 12819HelicalSequence analysisAdd
BLAST
Topological domaini129 – 1368CytoplasmicSequence analysis
Transmembranei137 – 15923HelicalSequence analysisAdd
BLAST
Topological domaini160 – 1645ExtracellularSequence analysis
Transmembranei165 – 18925HelicalSequence analysisAdd
BLAST
Topological domaini190 – 20213CytoplasmicSequence analysisAdd
BLAST
Transmembranei203 – 22321HelicalSequence analysisAdd
BLAST
Topological domaini224 – 23310ExtracellularSequence analysis
Transmembranei234 – 24916HelicalSequence analysisAdd
BLAST
Topological domaini250 – 27122CytoplasmicSequence analysisAdd
BLAST
Transmembranei272 – 29524HelicalSequence analysisAdd
BLAST
Topological domaini296 – 30510ExtracellularSequence analysis
Transmembranei306 – 32924HelicalSequence analysisAdd
BLAST
Topological domaini330 – 3356CytoplasmicSequence analysis
Transmembranei336 – 35520HelicalSequence analysisAdd
BLAST
Topological domaini356 – 3638ExtracellularSequence analysis
Transmembranei364 – 38724HelicalSequence analysisAdd
BLAST
Topological domaini388 – 40720CytoplasmicSequence analysisAdd
BLAST
Transmembranei408 – 42821HelicalSequence analysisAdd
BLAST
Topological domaini429 – 48153ExtracellularSequence analysisAdd
BLAST
Transmembranei482 – 50423HelicalSequence analysisAdd
BLAST
Topological domaini505 – 5128CytoplasmicSequence analysis

GO - Cellular componenti

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

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 512512Multidrug export protein EmrBPRO_0000173322Add
BLAST

Proteomic databases

PaxDbiP0AEJ0.

Interactioni

Subunit structurei

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 EmrA. EmrAB complex forms a dimer in vitro.2 Publications

Protein-protein interaction databases

BioGridi4263179. 213 interactions.
STRINGi511145.b2686.

Structurei

3D structure databases

ProteinModelPortaliP0AEJ0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi505 – 5106Poly-Gly

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105C0R. Bacteria.
ENOG410XNN3. LUCA.
HOGENOMiHOG000112190.
InParanoidiP0AEJ0.
KOiK03446.
OMAiVSNSLNM.
OrthoDBiEOG6ZH2DN.
PhylomeDBiP0AEJ0.

Family and domain databases

InterProiIPR004638. Drug-R_transpt_efflux_EmrB.
IPR011701. MFS.
IPR020846. MFS_dom.
[Graphical view]
PfamiPF07690. MFS_1. 1 hit.
[Graphical view]
SUPFAMiSSF103473. SSF103473. 3 hits.
TIGRFAMsiTIGR00711. efflux_EmrB. 1 hit.
PROSITEiPS50850. MFS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0AEJ0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQQQKPLEGA QLVIMTIALS LATFMQVLDS TIANVAIPTI AGNLGSSLSQ
60 70 80 90 100
GTWVITSFGV ANAISIPLTG WLAKRVGEVK LFLWSTIAFA IASWACGVSS
110 120 130 140 150
SLNMLIFFRV IQGIVAGPLI PLSQSLLLNN YPPAKRSIAL ALWSMTVIVA
160 170 180 190 200
PICGPILGGY ISDNYHWGWI FFINVPIGVA VVLMTLQTLR GRETRTERRR
210 220 230 240 250
IDAVGLALLV IGIGSLQIML DRGKELDWFS SQEIIILTVV AVVAICFLIV
260 270 280 290 300
WELTDDNPIV DLSLFKSRNF TIGCLCISLA YMLYFGAIVL LPQLLQEVYG
310 320 330 340 350
YTATWAGLAS APVGIIPVIL SPIIGRFAHK LDMRRLVTFS FIMYAVCFYW
360 370 380 390 400
RAYTFEPGMD FGASAWPQFI QGFAVACFFM PLTTITLSGL PPERLAAASS
410 420 430 440 450
LSNFTRTLAG SIGTSITTTM WTNRESMHHA QLTESVNPFN PNAQAMYSQL
460 470 480 490 500
EGLGMTQQQA SGWIAQQITN QGLIISANEI FWMSAGIFLV LLGLVWFAKP
510
PFGAGGGGGG AH
Length:512
Mass (Da):55,624
Last modified:December 20, 2005 - v1
Checksum:i070334E68B303EFF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti325 – 3251G → A in AAA23725 (PubMed:1409590).Curated
Sequence conflicti501 – 5011P → A in AAA23725 (PubMed:1409590).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M86657 Genomic DNA. Translation: AAA23725.1.
U00096 Genomic DNA. Translation: AAC75733.1.
AP009048 Genomic DNA. Translation: BAA16548.1.
PIRiG65048.
RefSeqiNP_417171.1. NC_000913.3.
WP_001295176.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75733; AAC75733; b2686.
BAA16548; BAA16548; BAA16548.
GeneIDi947167.
KEGGiecj:JW2661.
eco:b2686.
PATRICi32120766. VBIEscCol129921_2780.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M86657 Genomic DNA. Translation: AAA23725.1.
U00096 Genomic DNA. Translation: AAC75733.1.
AP009048 Genomic DNA. Translation: BAA16548.1.
PIRiG65048.
RefSeqiNP_417171.1. NC_000913.3.
WP_001295176.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP0AEJ0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263179. 213 interactions.
STRINGi511145.b2686.

Protein family/group databases

TCDBi2.A.1.3.2. the major facilitator superfamily (mfs).

Proteomic databases

PaxDbiP0AEJ0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75733; AAC75733; b2686.
BAA16548; BAA16548; BAA16548.
GeneIDi947167.
KEGGiecj:JW2661.
eco:b2686.
PATRICi32120766. VBIEscCol129921_2780.

Organism-specific databases

EchoBASEiEB1409.
EcoGeneiEG11439. emrB.

Phylogenomic databases

eggNOGiENOG4105C0R. Bacteria.
ENOG410XNN3. LUCA.
HOGENOMiHOG000112190.
InParanoidiP0AEJ0.
KOiK03446.
OMAiVSNSLNM.
OrthoDBiEOG6ZH2DN.
PhylomeDBiP0AEJ0.

Enzyme and pathway databases

BioCyciEcoCyc:EMRB-MONOMER.
ECOL316407:JW2661-MONOMER.

Miscellaneous databases

PROiP0AEJ0.

Family and domain databases

InterProiIPR004638. Drug-R_transpt_efflux_EmrB.
IPR011701. MFS.
IPR020846. MFS_dom.
[Graphical view]
PfamiPF07690. MFS_1. 1 hit.
[Graphical view]
SUPFAMiSSF103473. SSF103473. 3 hits.
TIGRFAMsiTIGR00711. efflux_EmrB. 1 hit.
PROSITEiPS50850. MFS. 1 hit.
[Graphical view]
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.
  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. "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.
  6. "Global topology analysis of the Escherichia coli inner membrane proteome."
    Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.
    Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY [LARGE SCALE ANALYSIS], SUBCELLULAR LOCATION.
    Strain: K12 / MG1655 / ATCC 47076.
  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 EMRA.

Entry informationi

Entry nameiEMRB_ECOLI
AccessioniPrimary (citable) accession number: P0AEJ0
Secondary accession number(s): P27304, P77725
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: February 17, 2016
This is version 84 of the entry and version 1 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.