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MDTE_ECOL6
ID   MDTE_ECOL6              Reviewed;         385 AA.
AC   Q8CVL1;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Multidrug resistance protein MdtE;
DE   Flags: Precursor;
GN   Name=mdtE; OrderedLocusNames=c4324;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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; AE014075; AAN82760.1; -; Genomic_DNA.
DR   RefSeq; WP_001081978.1; NC_004431.1.
DR   AlphaFoldDB; Q8CVL1; -.
DR   SMR; Q8CVL1; -.
DR   STRING; 199310.c4324; -.
DR   EnsemblBacteria; AAN82760; AAN82760; c4324.
DR   KEGG; ecc:c4324; -.
DR   eggNOG; COG0845; Bacteria.
DR   HOGENOM; CLU_018816_2_1_6; -.
DR   OMA; RHFEEGQ; -.
DR   BioCyc; ECOL199310:C4324-MON; -.
DR   Proteomes; UP000001410; 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; 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_0000018710"
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;  41161 MW;  3DC65B6CCF51CB8B 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 GQTGTLKFSD PTVDETTGSV TLRAIFPNPN GDLLPGMYVT ALVDEGSRQN
     VLLVPQEGVT HNAQGKATAL ILDKDDVVQL REIEASKAIG DQWVVTSGLQ AGDRVIVSGL
     QRIRPGIKAR AISSSQENAS TESKQ
 
 
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