MDFA_ECO57
ID MDFA_ECO57 Reviewed; 410 AA.
AC P0AEZ0; P71226; P75807; Q46966;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Multidrug transporter MdfA;
DE AltName: Full=Chloramphenicol resistance pump Cmr;
GN Name=mdfA; Synonyms=cmr; OrderedLocusNames=Z1069, ECs0922;
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: Efflux pump driven by the proton motive force. Confers
CC resistance to a broad spectrum of chemically unrelated drugs (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. MdfA family.
CC {ECO:0000305}.
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DR EMBL; AE005174; AAG55218.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB34345.1; -; Genomic_DNA.
DR PIR; B90744; B90744.
DR PIR; F85594; F85594.
DR RefSeq; NP_308949.1; NC_002695.1.
DR RefSeq; WP_001180089.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0AEZ0; -.
DR SMR; P0AEZ0; -.
DR STRING; 155864.EDL933_0969; -.
DR EnsemblBacteria; AAG55218; AAG55218; Z1069.
DR EnsemblBacteria; BAB34345; BAB34345; ECs_0922.
DR GeneID; 917662; -.
DR KEGG; ece:Z1069; -.
DR KEGG; ecs:ECs_0922; -.
DR PATRIC; fig|386585.9.peg.1039; -.
DR eggNOG; COG2814; Bacteria.
DR HOGENOM; CLU_001265_47_2_6; -.
DR OMA; AVLYRMT; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR005829; Sugar_transporter_CS.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance; Cell inner membrane; Cell membrane; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..410
FT /note="Multidrug transporter MdfA"
FT /id="PRO_0000173332"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..52
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 74..82
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 83..103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 104..109
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 131..144
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 166
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 188..226
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 248..255
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 256..276
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 277..287
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 288..308
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 309..314
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 315..335
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 336..346
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 347..367
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 368..378
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 379..399
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 400..410
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 410 AA; 44321 MW; D4466EE680095773 CRC64;
MQNKLASGAR LGRQALLFPL CLVLYEFSTY IGNDMIQPGM LAVVEQYQAG IDWVPTSMTA
YLAGGMFLQW LLGPLSDRIG RRPVMLAGVV WFIVTCLAIL LAQNIEQFTL LRFLQGISLC
FIGAVGYAAI QESFEEAVCI KITALMANVA LIAPLLGPLV GAAWIHVLPW EGMFVLFAAL
AAISFFGLQR AMPETATRIG EKLSLKELGR DYKLVLKNGR FVAGALALGF VSLPLLAWIA
QSPIIIITGE QLSSYEYGLL QVPIFGALIA GNLLLARLTS RRTVRSLIIM GGWPIMIGLL
VAAAATVISS HAYLWMTAGL SIYAFGIGLA NAGLVRLTLF ASDMSKGTVS AAMGMLQMLI
FTVGIEISKH AWLNGGNGLF NLFNLVNGIL WLSLMVIFLK DKQMGNSHEG
