MDTE_ECOLI
ID MDTE_ECOLI Reviewed; 385 AA.
AC P37636; Q2M7H5;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Multidrug resistance protein MdtE;
DE Flags: Precursor;
GN Name=mdtE; Synonyms=yhiU; OrderedLocusNames=b3513, JW3481;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8041620; DOI=10.1093/nar/22.13.2576;
RA Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT "Analysis of the Escherichia coli genome. V. DNA sequence of the region
RT from 76.0 to 81.5 minutes.";
RL Nucleic Acids Res. 22:2576-2586(1994).
RN [2]
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 [3]
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 [4]
RP FUNCTION IN MULTIDRUG RESISTANCE.
RX PubMed=11566977; DOI=10.1128/jb.183.20.5803-5812.2001;
RA Nishino K., Yamaguchi A.;
RT "Analysis of a complete library of putative drug transporter genes in
RT Escherichia coli.";
RL J. Bacteriol. 183:5803-5812(2001).
RN [5]
RP INDUCTION, AND SUBUNIT.
RX PubMed=11914367; DOI=10.1128/jb.184.8.2319-2323.2002;
RA Nishino K., Yamaguchi A.;
RT "EvgA of the two-component signal transduction system modulates production
RT of the yhiUV multidrug transporter in Escherichia coli.";
RL J. Bacteriol. 184:2319-2323(2002).
RN [6]
RP INDUCTION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=12399493; DOI=10.1128/jb.184.22.6225-6234.2002;
RA Masuda N., Church G.M.;
RT "Escherichia coli gene expression responsive to levels of the response
RT regulator EvgA.";
RL J. Bacteriol. 184:6225-6234(2002).
RN [7]
RP INDUCTION.
RX PubMed=14523115; DOI=10.1099/mic.0.26460-0;
RA Eguchi Y., Oshima T., Mori H., Aono R., Yamamoto K., Ishihama A.,
RA Utsumi R.;
RT "Transcriptional regulation of drug efflux genes by EvgAS, a two-component
RT system in Escherichia coli.";
RL Microbiology 149:2819-2828(2003).
RN [8]
RP INDUCTION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=12694615; DOI=10.1046/j.1365-2958.2003.03477.x;
RA Masuda N., Church G.M.;
RT "Regulatory network of acid resistance genes in Escherichia coli.";
RL Mol. Microbiol. 48:699-712(2003).
RN [9]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=BL21-DE3;
RX PubMed=16079137; DOI=10.1074/jbc.m506479200;
RA Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L.,
RA von Heijne G., Daley D.O.;
RT "Protein complexes of the Escherichia coli cell envelope.";
RL J. Biol. Chem. 280:34409-34419(2005).
CC -!- FUNCTION: Part of the tripartite efflux system MdtEF-TolC, which
CC confers resistance to compounds such as rhodamine 6G, erythromycin,
CC doxorubicin, ethidium bromide, TPP, SDS, deoxycholate, crystal violet
CC and benzalkonium. {ECO:0000269|PubMed:11566977}.
CC -!- SUBUNIT: Homotrimer. Part of the tripartite efflux system MdtEF-TolC,
CC which is composed of an inner membrane transporter, MdtF, a membrane
CC fusion protein, MdtE, and an outer membrane component, TolC. The
CC complex forms a large protein conduit and can translocate molecules
CC across both the inner and outer membranes.
CC {ECO:0000269|PubMed:11914367, ECO:0000269|PubMed:16079137}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC -!- INDUCTION: Induced by EvgA, probably via YdeO.
CC {ECO:0000269|PubMed:11914367, ECO:0000269|PubMed:12399493,
CC ECO:0000269|PubMed:12694615, ECO:0000269|PubMed:14523115}.
CC -!- SIMILARITY: Belongs to the membrane fusion protein (MFP) (TC 8.A.1)
CC family. {ECO:0000305}.
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DR EMBL; U00039; AAB18489.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76538.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77781.1; -; Genomic_DNA.
DR PIR; S47733; S47733.
DR RefSeq; NP_417970.1; NC_000913.3.
DR RefSeq; WP_001081984.1; NZ_STEB01000046.1.
DR AlphaFoldDB; P37636; -.
DR SMR; P37636; -.
DR BioGRID; 4262520; 226.
DR BioGRID; 852339; 3.
DR IntAct; P37636; 4.
DR STRING; 511145.b3513; -.
DR TCDB; 8.A.1.6.3; the membrane fusion protein (mfp) family.
DR jPOST; P37636; -.
DR PaxDb; P37636; -.
DR PRIDE; P37636; -.
DR EnsemblBacteria; AAC76538; AAC76538; b3513.
DR EnsemblBacteria; BAE77781; BAE77781; BAE77781.
DR GeneID; 66672602; -.
DR GeneID; 948031; -.
DR KEGG; ecj:JW3481; -.
DR KEGG; eco:b3513; -.
DR PATRIC; fig|1411691.4.peg.3205; -.
DR EchoBASE; EB2151; -.
DR eggNOG; COG0845; Bacteria.
DR HOGENOM; CLU_018816_2_1_6; -.
DR InParanoid; P37636; -.
DR OMA; RHFEEGQ; -.
DR PhylomeDB; P37636; -.
DR BioCyc; EcoCyc:EG12240-MON; -.
DR BioCyc; MetaCyc:EG12240-MON; -.
DR PRO; PR:P37636; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0031226; C:intrinsic component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0015125; F:bile acid transmembrane transporter activity; IMP:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0015721; P:bile acid and bile salt transport; IMP:EcoCyc.
DR GO; GO:0046677; P:response to antibiotic; IMP:EcoCyc.
DR GO; GO:0009636; P:response to toxic substance; IMP:EcoCyc.
DR GO; GO:0042908; P:xenobiotic transport; IMP:EcoCyc.
DR InterPro; IPR043602; CusB_dom_1.
DR InterPro; IPR032317; HlyD_D23.
DR InterPro; IPR006143; RND_pump_MFP.
DR Pfam; PF00529; CusB_dom_1; 1.
DR Pfam; PF16576; HlyD_D23; 1.
DR TIGRFAMs; TIGR01730; RND_mfp; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW Antibiotic resistance; Cell inner membrane; Cell membrane; Lipoprotein;
KW Membrane; Palmitate; Reference proteome; Signal; Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 21..385
FT /note="Multidrug resistance protein MdtE"
FT /id="PRO_0000018708"
FT LIPID 21
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 21
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ SEQUENCE 385 AA; 41191 MW; 2C825B6CDE15C70F CRC64;
MNRRRKLLIP LLFCGAMLTA CDDKSAENAA AMTPEVGVVT LSPGSVNVLS ELPGRTVPYE
VAEIRPQVGG IIIKRNFIEG DKVNQGDSLY QIDPAPLQAE LNSAKGSLAK ALSTASNARI
TFNRQASLLK TNYVSRQDYD TARTQLNEAE ANVTVAKAAV EQATINLQYA NVTSPITGVS
GKSSVTVGAL VTANQADSLV TVQRLDPIYV DLTQSVQDFL RMKEEVASGQ IKQVQGSTPV
QLNLENGKRY SQTGTLKFSD PTVDETTGSV TLRAIFPNPN GDLLPGMYVT ALVDEGSRQN
VLLVPQEGVT HNAQGKATAL ILDKDDVVQL REIEASKAIG DQWVVTSGLQ AGDRVIVSGL
QRIRPGIKAR AISSSQENAS TESKQ
