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MDTF_ECOL6
ID   MDTF_ECOL6              Reviewed;        1037 AA.
AC   Q8FCI8;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Multidrug resistance protein MdtF;
GN   Name=mdtF; OrderedLocusNames=c4325;
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:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the resistance-nodulation-cell division (RND)
CC       (TC 2.A.6) family. {ECO:0000305}.
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DR   EMBL; AE014075; AAN82761.1; -; Genomic_DNA.
DR   RefSeq; WP_000024904.1; NC_004431.1.
DR   AlphaFoldDB; Q8FCI8; -.
DR   SMR; Q8FCI8; -.
DR   STRING; 199310.c4325; -.
DR   EnsemblBacteria; AAN82761; AAN82761; c4325.
DR   KEGG; ecc:c4325; -.
DR   eggNOG; COG0841; Bacteria.
DR   HOGENOM; CLU_002755_0_1_6; -.
DR   OMA; ITRHNMY; -.
DR   BioCyc; ECOL199310:C4325-MON; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015562; F:efflux transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   GO; GO:0042908; P:xenobiotic transport; IEA:InterPro.
DR   Gene3D; 3.30.2090.10; -; 2.
DR   InterPro; IPR027463; AcrB_DN_DC_subdom.
DR   InterPro; IPR001036; Acrflvin-R.
DR   InterPro; IPR004764; HAE1.
DR   PANTHER; PTHR32063; PTHR32063; 1.
DR   Pfam; PF00873; ACR_tran; 1.
DR   PRINTS; PR00702; ACRIFLAVINRP.
DR   SUPFAM; SSF82714; SSF82714; 2.
DR   TIGRFAMs; TIGR00915; 2A0602; 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance; Cell inner membrane; Cell membrane; Membrane;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..1037
FT                   /note="Multidrug resistance protein MdtF"
FT                   /id="PRO_0000161842"
FT   TOPO_DOM        1..9
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        10..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        31..338
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        339..359
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        360..369
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        370..390
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        391..392
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        393..413
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        414..440
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        441..461
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        462..471
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        472..492
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        493..534
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        535..555
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        556..870
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        871..891
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        892
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        893..913
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        914..927
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        928..948
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        949..972
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        973..993
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        994..1006
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1007..1027
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1028..1037
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1037 AA;  111543 MW;  FB10E00B2011BCCA CRC64;
     MANYFIDRPV FAWVLAIIMM LAGGLAIMNL PVAQYPQIAP PTITVSATYP GADAQTVEDS
     VTQVIEQNMN GLDGLMYMSS TSDAAGNASI TLTFETGTSP DIAQVQVQNK LQLAMPSLPE
     AVQQQGISVD KSSSNILMVA AFISDNGSLN QYDIADYVAS NIKDPLSRTA GVGSVQLFGS
     EYAMRIWLDP QKLNKYNLVP SDVISQIKVQ NNQISGGQLG GMPQAADQQL NASIIVQTRL
     QTPEEFGKIL LKVQQDGSQV LLRDVARVEL GAEDYSTVAR YNGKPAAGIA IKLATGANAL
     DTSRAVKEEL NRLSAYFPAS LKTVYPYDTT PFIKISIQEV FKTLVEAIIL VFLVMYLFLQ
     NFRATIIPTI AVPVVILGTF AILSAVGFTI NTLTMFGMVL AIGLLVDDAI VVVENVERVI
     AEDKLPPKEA THKSMGQIQR ALVGIAVVLS AVFMPMAFMS GATGEIYRQF SITLISSMLL
     SVFVAMSLTP ALCATILKAA PEGGHKPNAL FARFNTLFEK STQHYTDSTR SLLRCTGRYM
     VVYLLICAGM AVLFLRTPTS FLPEEDQGVF MTTAQLPSGA TMVNTTKVLQ QVTDYYLTKE
     KNNVQSVFTV GGFGFSGQGQ NNGLAFISLK PWSERVGEEN SVTAIIQRAM IALSSINKAV
     VFPFNLPAVA ELGTASGFDM ELLDNGNLGH EKLTQARNEL LSLAAQSPNQ VIGVRPNGLE
     DTPMFKVNVN AAKAEAMGVA LSDINQTIST AFGSSYVNDF LNQGRVKKVY VQAGTPFRML
     PDNINQWYVR NASGTMAPLS AYSSTEWTYG SPRLERYNGI PSMEILGEAA AGKSTGDAMK
     FMADLVAKLP AGVGYSWTGL SYQEALSSNQ APALYAISLV VVFLALAALY ESWSIPFSVM
     LVVPLGVVGA LLATDLRGLS NDVYFQVGLL TTIGLSAKNA ILIVEFAVEM MQKEGKTPVE
     AIIEAARMRL RPILMTSLAF ILGVLPLVIS HGAGSGAQNA VGTGVMGGMF AATVLAIYFV
     PVFFVVVEHL FARFKKA
 
 
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