MDTE_ECO57
ID MDTE_ECO57 Reviewed; 385 AA.
AC Q8X4L0; Q7AA09;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Multidrug resistance protein MdtE;
DE Flags: Precursor;
GN Name=mdtE; OrderedLocusNames=Z4926, ECs4393;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
CC -!- FUNCTION: Part of the tripartite efflux system MdtEF-TolC, which
CC confers resistance to various compounds. {ECO:0000250}.
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 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC -!- SIMILARITY: Belongs to the membrane fusion protein (MFP) (TC 8.A.1)
CC family. {ECO:0000305}.
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DR EMBL; AE005174; AAG58654.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB37816.1; -; Genomic_DNA.
DR PIR; A91178; A91178.
DR PIR; B86024; B86024.
DR RefSeq; NP_312420.1; NC_002695.1.
DR RefSeq; WP_001082000.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; Q8X4L0; -.
DR SMR; Q8X4L0; -.
DR STRING; 155864.EDL933_4764; -.
DR EnsemblBacteria; AAG58654; AAG58654; Z4926.
DR EnsemblBacteria; BAB37816; BAB37816; ECs_4393.
DR GeneID; 915750; -.
DR KEGG; ece:Z4926; -.
DR KEGG; ecs:ECs_4393; -.
DR PATRIC; fig|386585.9.peg.4591; -.
DR eggNOG; COG0845; Bacteria.
DR HOGENOM; CLU_018816_2_1_6; -.
DR OMA; RHFEEGQ; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
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 3: Inferred from homology;
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_0000018709"
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; 41221 MW; 6823EF67D6141102 CRC64;
MNRRRKLLIP LLFCGAMLTA CDDKSAENTA 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 ILDKDDVVKL REIEASKAIG DQWVVTSGLQ AGDRVIVSGL
QRIRPGIKAR AISSSQENAS TESKQ