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Protein

Probable multidrug resistance protein EmrY

Gene

emrY

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

Functioni

Part of the tripartite efflux system EmrYK-TolC, which confers resistance to various drugs.By similarity

GO - Biological processi

  • cellular response to DNA damage stimulus Source: EcoCyc
  • response to antibiotic Source: EcoCyc
  • transmembrane transport Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Transport

Enzyme and pathway databases

BioCyciEcoCyc:EMRY-MONOMER.
ECOL316407:JW2364-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable multidrug resistance protein EmrY
Gene namesi
Name:emrY
Ordered Locus Names:b2367, JW2364
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13283. emrY.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 88CytoplasmicSequence analysis
Transmembranei9 – 2921HelicalSequence analysisAdd
BLAST
Topological domaini30 – 301PeriplasmicSequence analysis
Transmembranei31 – 5121HelicalSequence analysisAdd
BLAST
Topological domaini52 – 532CytoplasmicSequence analysis
Transmembranei54 – 7421HelicalSequence analysisAdd
BLAST
Topological domaini75 – 8410PeriplasmicSequence analysis
Transmembranei85 – 10521HelicalSequence analysisAdd
BLAST
Transmembranei106 – 12621HelicalSequence analysisAdd
BLAST
Topological domaini127 – 14115PeriplasmicSequence analysisAdd
BLAST
Transmembranei142 – 16221HelicalSequence analysisAdd
BLAST
Topological domaini163 – 17210CytoplasmicSequence analysis
Transmembranei173 – 19321HelicalSequence analysisAdd
BLAST
Topological domaini194 – 20411PeriplasmicSequence analysisAdd
BLAST
Transmembranei205 – 22521HelicalSequence analysisAdd
BLAST
Topological domaini226 – 2349CytoplasmicSequence analysis
Transmembranei235 – 25521HelicalSequence analysisAdd
BLAST
Topological domaini256 – 27318PeriplasmicSequence analysisAdd
BLAST
Transmembranei274 – 29421HelicalSequence analysisAdd
BLAST
Topological domaini295 – 30713CytoplasmicSequence analysisAdd
BLAST
Transmembranei308 – 32821HelicalSequence analysisAdd
BLAST
Topological domaini329 – 33810PeriplasmicSequence analysis
Transmembranei339 – 35921HelicalSequence analysisAdd
BLAST
Topological domaini360 – 3645CytoplasmicSequence analysis
Transmembranei365 – 38521HelicalSequence analysisAdd
BLAST
Topological domaini386 – 486101PeriplasmicSequence analysisAdd
BLAST
Transmembranei487 – 50721HelicalSequence analysisAdd
BLAST
Topological domaini508 – 5125CytoplasmicSequence 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

Pathology & Biotechi

Disruption phenotypei

Mutants are more sensitive to nalidixic acid, mitomycin C and other stresses such as hydrogen peroxide or UV irradiation.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 512512Probable multidrug resistance protein EmrYPRO_0000173325Add
BLAST

Proteomic databases

PaxDbiP52600.
PRIDEiP52600.

Expressioni

Inductioni

Growth phase-dependent transcription is induced by tetracycline. Expression may be controlled by both RpoS and the Mar system.1 Publication

Interactioni

Subunit structurei

Part of the tripartite efflux system EmrYK-TolC, which is composed of an inner membrane transporter, EmrY, a membrane fusion protein, EmrK, and an outer membrane component, TolC. The complex forms a large protein conduit and can translocate molecules across both the inner and outer membranes (By similarity).By similarity

Protein-protein interaction databases

BioGridi4260556. 101 interactions.
DIPiDIP-9507N.
IntActiP52600. 2 interactions.
MINTiMINT-1286081.
STRINGi511145.b2367.

Structurei

3D structure databases

ProteinModelPortaliP52600.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105C0R. Bacteria.
ENOG410XNN3. LUCA.
HOGENOMiHOG000112190.
InParanoidiP52600.
KOiK07786.
OMAiSSHEGEN.
OrthoDBiEOG6ZH2DN.
PhylomeDBiP52600.

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.

P52600-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAITKSTPAP LTGGTLWCVT IALSLATFMQ MLDSTISNVA IPTISGFLGA
60 70 80 90 100
STDEGTWVIT SFGVANAIAI PVTGRLAQRI GELRLFLLSV TFFSLSSLMC
110 120 130 140 150
SLSTNLDVLI FFRVVQGLMA GPLIPLSQSL LLRNYPPEKR TFALALWSMT
160 170 180 190 200
VIIAPICGPI LGGYICDNFS WGWIFLINVP MGIIVLTLCL TLLKGRETET
210 220 230 240 250
SPVKMNLPGL TLLVLGVGGL QIMLDKGRDL DWFNSSTIII LTVVSVISLI
260 270 280 290 300
SLVIWESTSE NPILDLSLFK SRNFTIGIVS ITCAYLFYSG AIVLMPQLLQ
310 320 330 340 350
ETMGYNAIWA GLAYAPIGIM PLLISPLIGR YGNKIDMRLL VTFSFLMYAV
360 370 380 390 400
CYYWRSVTFM PTIDFTGIIL PQFFQGFAVA CFFLPLTTIS FSGLPDNKFA
410 420 430 440 450
NASSMSNFFR TLSGSVGTSL TMTLWGRRES LHHSQLTATI DQFNPVFNSS
460 470 480 490 500
SQIMDKYYGS LSGVLNEINN EITQQSLSIS ANEIFRMAAI AFILLTVLVW
510
FAKPPFTAKG VG
Length:512
Mass (Da):56,001
Last modified:October 1, 1996 - v1
Checksum:i3A2DC008D3E8D8F5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D78168 Genomic DNA. Translation: BAA11237.1.
U00096 Genomic DNA. Translation: AAC75426.1.
AP009048 Genomic DNA. Translation: BAA16230.1.
PIRiD65010.
RefSeqiNP_416868.1. NC_000913.3.
WP_001018714.1. NZ_CP014272.1.

Genome annotation databases

EnsemblBacteriaiAAC75426; AAC75426; b2367.
BAA16230; BAA16230; BAA16230.
GeneIDi946835.
KEGGiecj:JW2364.
eco:b2367.
PATRICi32120113. VBIEscCol129921_2465.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D78168 Genomic DNA. Translation: BAA11237.1.
U00096 Genomic DNA. Translation: AAC75426.1.
AP009048 Genomic DNA. Translation: BAA16230.1.
PIRiD65010.
RefSeqiNP_416868.1. NC_000913.3.
WP_001018714.1. NZ_CP014272.1.

3D structure databases

ProteinModelPortaliP52600.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260556. 101 interactions.
DIPiDIP-9507N.
IntActiP52600. 2 interactions.
MINTiMINT-1286081.
STRINGi511145.b2367.

Proteomic databases

PaxDbiP52600.
PRIDEiP52600.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75426; AAC75426; b2367.
BAA16230; BAA16230; BAA16230.
GeneIDi946835.
KEGGiecj:JW2364.
eco:b2367.
PATRICi32120113. VBIEscCol129921_2465.

Organism-specific databases

EchoBASEiEB3068.
EcoGeneiEG13283. emrY.

Phylogenomic databases

eggNOGiENOG4105C0R. Bacteria.
ENOG410XNN3. LUCA.
HOGENOMiHOG000112190.
InParanoidiP52600.
KOiK07786.
OMAiSSHEGEN.
OrthoDBiEOG6ZH2DN.
PhylomeDBiP52600.

Enzyme and pathway databases

BioCyciEcoCyc:EMRY-MONOMER.
ECOL316407:JW2364-MONOMER.

Miscellaneous databases

PROiP52600.

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. "Analysis and characterization of the upstream region of evgA and evgS."
    Utsumi R.
    Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  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. "Growth phase-dependent transcription of emrKY, a homolog of multidrug efflux emrAB genes of Escherichia coli, is induced by tetracycline."
    Tanabe H., Yamasak K., Furue M., Yamamoto K., Katoh A., Yamamoto M., Yoshioka S., Tagami H., Aiba H.A., Utsumi R.
    J. Gen. Appl. Microbiol. 43:257-263(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
  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: SUBCELLULAR LOCATION.
    Strain: K12 / MG1655 / ATCC 47076.
  7. "Escherichia coli genes that reduce the lethal effects of stress."
    Han X., Dorsey-Oresto A., Malik M., Wang J.Y., Drlica K., Zhao X., Lu T.
    BMC Microbiol. 10:35-35(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
    Strain: K12.

Entry informationi

Entry nameiEMRY_ECOLI
AccessioniPrimary (citable) accession number: P52600
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 11, 2016
This is version 123 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.