Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Multidrug export protein EmrB

Gene

emrB

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.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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11439. emrB.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 12CytoplasmicSequence analysisAdd BLAST12
Transmembranei13 – 38HelicalSequence analysisAdd BLAST26
Topological domaini39 – 51ExtracellularSequence analysisAdd BLAST13
Transmembranei52 – 72HelicalSequence analysisAdd BLAST21
Topological domaini73 – 81CytoplasmicSequence analysis9
Transmembranei82 – 100HelicalSequence analysisAdd BLAST19
Topological domaini101 – 109ExtracellularSequence analysis9
Transmembranei110 – 128HelicalSequence analysisAdd BLAST19
Topological domaini129 – 136CytoplasmicSequence analysis8
Transmembranei137 – 159HelicalSequence analysisAdd BLAST23
Topological domaini160 – 164ExtracellularSequence analysis5
Transmembranei165 – 189HelicalSequence analysisAdd BLAST25
Topological domaini190 – 202CytoplasmicSequence analysisAdd BLAST13
Transmembranei203 – 223HelicalSequence analysisAdd BLAST21
Topological domaini224 – 233ExtracellularSequence analysis10
Transmembranei234 – 249HelicalSequence analysisAdd BLAST16
Topological domaini250 – 271CytoplasmicSequence analysisAdd BLAST22
Transmembranei272 – 295HelicalSequence analysisAdd BLAST24
Topological domaini296 – 305ExtracellularSequence analysis10
Transmembranei306 – 329HelicalSequence analysisAdd BLAST24
Topological domaini330 – 335CytoplasmicSequence analysis6
Transmembranei336 – 355HelicalSequence analysisAdd BLAST20
Topological domaini356 – 363ExtracellularSequence analysis8
Transmembranei364 – 387HelicalSequence analysisAdd BLAST24
Topological domaini388 – 407CytoplasmicSequence analysisAdd BLAST20
Transmembranei408 – 428HelicalSequence analysisAdd BLAST21
Topological domaini429 – 481ExtracellularSequence analysisAdd BLAST53
Transmembranei482 – 504HelicalSequence analysisAdd BLAST23
Topological domaini505 – 512CytoplasmicSequence analysis8

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)DescriptionActionsGraphical viewLength
ChainiPRO_00001733221 – 512Multidrug export protein EmrBAdd BLAST512

Proteomic databases

PaxDbiP0AEJ0.
PRIDEiP0AEJ0.

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 interactors.
STRINGi511145.b2686.

Structurei

3D structure databases

ProteinModelPortaliP0AEJ0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi505 – 510Poly-Gly6

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

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

Family and domain databases

CDDicd06174. MFS. 1 hit.
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)DescriptionActionsGraphical viewLength
Sequence conflicti325G → A in AAA23725 (PubMed:1409590).Curated1
Sequence conflicti501P → A in AAA23725 (PubMed:1409590).Curated1

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 interactors.
STRINGi511145.b2686.

Protein family/group databases

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

Proteomic databases

PaxDbiP0AEJ0.
PRIDEiP0AEJ0.

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.
PhylomeDBiP0AEJ0.

Enzyme and pathway databases

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

Miscellaneous databases

PROiP0AEJ0.

Family and domain databases

CDDicd06174. MFS. 1 hit.
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...

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: November 2, 2016
This is version 87 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.