EMRY_ECOLI
ID EMRY_ECOLI Reviewed; 512 AA.
AC P52600;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Probable multidrug resistance protein EmrY;
GN Name=emrY; OrderedLocusNames=b2367, JW2364;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Utsumi R.;
RT "Analysis and characterization of the upstream region of evgA and evgS.";
RL Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP INDUCTION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=12501312; DOI=10.2323/jgam.43.257;
RA Tanabe H., Yamasak K., Furue M., Yamamoto K., Katoh A., Yamamoto M.,
RA Yoshioka S., Tagami H., Aiba H.A., Utsumi R.;
RT "Growth phase-dependent transcription of emrKY, a homolog of multidrug
RT efflux emrAB genes of Escherichia coli, is induced by tetracycline.";
RL J. Gen. Appl. Microbiol. 43:257-263(1997).
RN [6]
RP SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [7]
RP DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=20128927; DOI=10.1186/1471-2180-10-35;
RA Han X., Dorsey-Oresto A., Malik M., Wang J.Y., Drlica K., Zhao X., Lu T.;
RT "Escherichia coli genes that reduce the lethal effects of stress.";
RL BMC Microbiol. 10:35-35(2010).
CC -!- FUNCTION: Part of the tripartite efflux system EmrYK-TolC, which
CC confers resistance to various drugs. {ECO:0000250}.
CC -!- SUBUNIT: Part of the tripartite efflux system EmrYK-TolC, which is
CC composed of an inner membrane transporter, EmrY, a membrane fusion
CC protein, EmrK, and an outer membrane component, TolC. The complex forms
CC a large protein conduit and can translocate molecules across both the
CC inner and outer membranes (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15919996}.
CC -!- INDUCTION: Growth phase-dependent transcription is induced by
CC tetracycline. Expression may be controlled by both RpoS and the Mar
CC system. {ECO:0000269|PubMed:12501312}.
CC -!- DISRUPTION PHENOTYPE: Mutants are more sensitive to nalidixic acid,
CC mitomycin C and other stresses such as hydrogen peroxide or UV
CC irradiation. {ECO:0000269|PubMed:20128927}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. EmrB family.
CC {ECO:0000305}.
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DR EMBL; D78168; BAA11237.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75426.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16230.1; -; Genomic_DNA.
DR PIR; D65010; D65010.
DR RefSeq; NP_416868.1; NC_000913.3.
DR RefSeq; WP_001018714.1; NZ_SSZK01000006.1.
DR AlphaFoldDB; P52600; -.
DR SMR; P52600; -.
DR BioGRID; 4260556; 101.
DR ComplexPortal; CPX-4273; EmrKY-TolC multidrug efflux transport system.
DR DIP; DIP-9507N; -.
DR IntAct; P52600; 2.
DR STRING; 511145.b2367; -.
DR PaxDb; P52600; -.
DR PRIDE; P52600; -.
DR EnsemblBacteria; AAC75426; AAC75426; b2367.
DR EnsemblBacteria; BAA16230; BAA16230; BAA16230.
DR GeneID; 946835; -.
DR KEGG; ecj:JW2364; -.
DR KEGG; eco:b2367; -.
DR PATRIC; fig|1411691.4.peg.4362; -.
DR EchoBASE; EB3068; -.
DR eggNOG; COG0477; Bacteria.
DR HOGENOM; CLU_000960_28_0_6; -.
DR InParanoid; P52600; -.
DR OMA; WAINSYT; -.
DR PhylomeDB; P52600; -.
DR BioCyc; EcoCyc:EMRY-MON; -.
DR BioCyc; MetaCyc:EMRY-MON; -.
DR PRO; PR:P52600; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:1990281; C:efflux pump complex; IC:ComplexPortal.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0098567; C:periplasmic side of plasma membrane; IC:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015721; P:bile acid and bile salt transport; IMP:EcoCyc.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:EcoCyc.
DR GO; GO:0046677; P:response to antibiotic; IMP:EcoCyc.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR GO; GO:0140330; P:xenobiotic detoxification by transmembrane export across the cell outer membrane; IC:ComplexPortal.
DR GO; GO:1990961; P:xenobiotic detoxification by transmembrane export across the plasma membrane; IDA:EcoCyc.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR004638; EmrB-like.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00711; efflux_EmrB; 1.
DR PROSITE; PS50850; MFS; 1.
PE 2: Evidence at transcript level;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..512
FT /note="Probable multidrug resistance protein EmrY"
FT /id="PRO_0000173325"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 52..53
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 75..84
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 85..105
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 127..141
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 163..172
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 194..204
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 205..225
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 226..234
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 235..255
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 256..273
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 295..307
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 308..328
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 329..338
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 339..359
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 360..364
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 365..385
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 386..486
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 487..507
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 508..512
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 512 AA; 56001 MW; 3A2DC008D3E8D8F5 CRC64;
MAITKSTPAP LTGGTLWCVT IALSLATFMQ MLDSTISNVA IPTISGFLGA STDEGTWVIT
SFGVANAIAI PVTGRLAQRI GELRLFLLSV TFFSLSSLMC SLSTNLDVLI FFRVVQGLMA
GPLIPLSQSL LLRNYPPEKR TFALALWSMT VIIAPICGPI LGGYICDNFS WGWIFLINVP
MGIIVLTLCL TLLKGRETET SPVKMNLPGL TLLVLGVGGL QIMLDKGRDL DWFNSSTIII
LTVVSVISLI SLVIWESTSE NPILDLSLFK SRNFTIGIVS ITCAYLFYSG AIVLMPQLLQ
ETMGYNAIWA GLAYAPIGIM PLLISPLIGR YGNKIDMRLL VTFSFLMYAV CYYWRSVTFM
PTIDFTGIIL PQFFQGFAVA CFFLPLTTIS FSGLPDNKFA NASSMSNFFR TLSGSVGTSL
TMTLWGRRES LHHSQLTATI DQFNPVFNSS SQIMDKYYGS LSGVLNEINN EITQQSLSIS
ANEIFRMAAI AFILLTVLVW FAKPPFTAKG VG
