MDTF_ECOLI
ID MDTF_ECOLI Reviewed; 1037 AA.
AC P37637; Q2M7H6;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Multidrug resistance protein MdtF;
GN Name=mdtF; Synonyms=yhiV; OrderedLocusNames=b3514, JW3482;
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).
RN [10]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(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
CC {ECO:0000269|PubMed:16079137}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16079137}.
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 resistance-nodulation-cell division (RND)
CC (TC 2.A.6) family. {ECO:0000305}.
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DR EMBL; U00039; AAB18490.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76539.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77780.1; -; Genomic_DNA.
DR PIR; S47734; S47734.
DR RefSeq; NP_417971.1; NC_000913.3.
DR RefSeq; WP_000024872.1; NZ_SSZK01000042.1.
DR AlphaFoldDB; P37637; -.
DR SMR; P37637; -.
DR BioGRID; 4262521; 292.
DR IntAct; P37637; 1.
DR STRING; 511145.b3514; -.
DR TCDB; 2.A.6.2.13; the resistance-nodulation-cell division (rnd) superfamily.
DR jPOST; P37637; -.
DR PaxDb; P37637; -.
DR PRIDE; P37637; -.
DR EnsemblBacteria; AAC76539; AAC76539; b3514.
DR EnsemblBacteria; BAE77780; BAE77780; BAE77780.
DR GeneID; 948030; -.
DR KEGG; ecj:JW3482; -.
DR KEGG; eco:b3514; -.
DR PATRIC; fig|1411691.4.peg.3204; -.
DR EchoBASE; EB2152; -.
DR eggNOG; COG0841; Bacteria.
DR HOGENOM; CLU_002755_0_2_6; -.
DR InParanoid; P37637; -.
DR OMA; ITRHNMY; -.
DR PhylomeDB; P37637; -.
DR BioCyc; EcoCyc:YHIV-MON; -.
DR BioCyc; MetaCyc:YHIV-MON; -.
DR PRO; PR:P37637; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0015125; F:bile acid transmembrane transporter activity; IMP:EcoCyc.
DR GO; GO:0015562; F:efflux transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; IMP:EcoliWiki.
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:0006855; P:xenobiotic transmembrane transport; IMP:EcoliWiki.
DR GO; GO:0042908; P:xenobiotic transport; IMP:EcoCyc.
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 1: Evidence at protein level;
KW Antibiotic resistance; Cell inner membrane; Cell membrane; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1037
FT /note="Multidrug resistance protein MdtF"
FT /id="PRO_0000161841"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 10..28
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 29..339
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 340..359
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 360..365
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 366..385
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 386..391
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 392..413
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 414..441
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 442..460
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 461..473
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 474..496
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 497..536
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 537..555
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 556..870
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 871..890
FT /note="Helical; Name=8"
FT /evidence="ECO:0000250"
FT TOPO_DOM 891..896
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 897..916
FT /note="Helical; Name=9"
FT /evidence="ECO:0000250"
FT TOPO_DOM 917..922
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 923..944
FT /note="Helical; Name=10"
FT /evidence="ECO:0000250"
FT TOPO_DOM 945..972
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 973..991
FT /note="Helical; Name=11"
FT /evidence="ECO:0000250"
FT TOPO_DOM 992..1004
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 1005..1027
FT /note="Helical; Name=12"
FT /evidence="ECO:0000250"
FT TOPO_DOM 1028..1037
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1037 AA; 111517 MW; 3B67502160F51724 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 IKLAAGANAL
DTSRAVKEEL NRLSAYFPAS LKTVYPYDTT PFIEISIQEV 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
KDNVQSVFTV GGFGFSGQGQ NNGLAFISLK PWSERVGEEN SVTAIIQRAM IALSSINKAV
VFPFNLPAVA ELGTASGFDM ELLDNGNLGH EKLTQARNEL LSLAAQSPNQ VTGVRPNGLE
DTPMFKVNVN AAKAEAMGVA LSDINQTIST AFGSSYVNDF LNQGRVKKVY VQAGTPFRML
PDNINQWYVR NASGTMAPLS AYSSTEWTYG SPRLERYNGI PSMEILGEAA AGKSTGDAMK
FMADLVAKLP AGVGYSWTGL SYQEALSSNQ APALYAISLV VVFLALAALY ESWSIPFSVM
LVVPLGVVGA LLATDLRGLS NDVYFQVGLL TTIGLSAKNA ILIVEFAVEM MQKEGKTPIE
AIIEAARMRL RPILMTSLAF ILGVLPLVIS HGAGSGAQNA VGTGVMGGMF AATVLAIYFV
PVFFVVVEHL FARFKKA
