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