ID   MDTB_ECOL6              Reviewed;        1040 AA.
AC   Q8FG04;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Multidrug resistance protein MdtB {ECO:0000255|HAMAP-Rule:MF_01423};
DE   AltName: Full=Multidrug transporter MdtB {ECO:0000255|HAMAP-Rule:MF_01423};
GN   Name=mdtB {ECO:0000255|HAMAP-Rule:MF_01423}; OrderedLocusNames=c2601;
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: The MdtABC tripartite complex confers resistance against
CC       novobiocin and deoxycholate. {ECO:0000255|HAMAP-Rule:MF_01423}.
CC   -!- SUBUNIT: Part of a tripartite efflux system composed of MdtA, MdtB and
CC       MdtC. MdtB forms a heteromultimer with MdtC. {ECO:0000255|HAMAP-
CC       Rule:MF_01423}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01423}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01423}.
CC   -!- INDUCTION: The mdtABC operon is transcriptionally activated by BaeR.
CC   -!- SIMILARITY: Belongs to the resistance-nodulation-cell division (RND)
CC       (TC 2.A.6) family. MdtB subfamily. {ECO:0000255|HAMAP-Rule:MF_01423}.
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DR   EMBL; AE014075; AAN81057.1; -; Genomic_DNA.
DR   RefSeq; WP_001197878.1; NC_004431.1.
DR   AlphaFoldDB; Q8FG04; -.
DR   SMR; Q8FG04; -.
DR   STRING; 199310.c2601; -.
DR   EnsemblBacteria; AAN81057; AAN81057; c2601.
DR   KEGG; ecc:c2601; -.
DR   eggNOG; COG0841; Bacteria.
DR   HOGENOM; CLU_002755_1_2_6; -.
DR   OMA; FIIPCFY; -.
DR   BioCyc; ECOL199310:C2601-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:0022857; F:transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.2090.10; -; 2.
DR   HAMAP; MF_01423; MdtB; 1.
DR   InterPro; IPR027463; AcrB_DN_DC_subdom.
DR   InterPro; IPR001036; Acrflvin-R.
DR   InterPro; IPR022831; Multidrug-R_MdtB.
DR   PANTHER; PTHR32063; PTHR32063; 1.
DR   Pfam; PF00873; ACR_tran; 1.
DR   PRINTS; PR00702; ACRIFLAVINRP.
DR   SUPFAM; SSF82714; SSF82714; 2.
PE   2: Evidence at transcript level;
KW   Cell inner membrane; Cell membrane; Membrane; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..1040
FT                   /note="Multidrug resistance protein MdtB"
FT                   /id="PRO_0000161822"
FT   TRANSMEM        15..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01423"
FT   TRANSMEM        345..362
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01423"
FT   TRANSMEM        367..389
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01423"
FT   TRANSMEM        396..418
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01423"
FT   TRANSMEM        438..460
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01423"
FT   TRANSMEM        472..494
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01423"
FT   TRANSMEM        535..557
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01423"
FT   TRANSMEM        867..889
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01423"
FT   TRANSMEM        909..931
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01423"
FT   TRANSMEM        968..990
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01423"
FT   TRANSMEM        1000..1022
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01423"
SQ   SEQUENCE   1040 AA;  112096 MW;  181B3D6D9DCAC6F0 CRC64;
     MQVLPPSSTG GPSRLFIMRP VATTLLMVAI LLAGIIGYRA LPVSALPEVD YPTIQVVTLY
     PGASPDVMTS AVTAPLERQF GQMSGLKQMS SQSSGGASVI TLQFQLTLPL DVAEQEVQAA
     INAATNLLPS DLPNPPVYSK VNPADPPIMT LAVTSTAMPM TQVEDMVETR VAQKISQISG
     VGLVTLSGGQ RPAVRVKLNA QAIAALGLTS ETVRTAITGA NVNSAKGSLD GPSRAVTLSA
     NDQMQSAEEY RQLIIAYQNG APIRLGDVAT VEQGAENSWL GAWANKEQAI VMNVQRQPGA
     NIISTADSIR QMLPQLTESL PKSVKVTVLS DRTTNIRASV DDTQFELMMA IALVVMIIYL
     FLRNIPATII PGVAVPLSLI GTFAVMVFLD FSINNLTLMA LTIATGFVVD DAIVVIENIS
     RYIEKGEKPL AAALKGAGEI GFTIISLTFS LIAVLIPLLF MGDIVGRLFR EFAITLAVAI
     LISAVVSLTL TPMMCARMLS QESLRKQNRF SRASEKMFDR IIAAYGRGLA KVLNHPWLTL
     SVALSTLLLS VLLWVFIPKG FFPVQDNGII QGTLQAPQSS SFANMAQRQR QVADVILQDP
     AVQSLTSFVG VDGTNPSLNS ARLQINLKPL DERDDRVQKV IARLQTAVDK VPGVDLFLQP
     TQDLTIDTQV SRTQYQFTLQ ATSLDALSTW VPQLMEKLQQ LPQLSDVSSD WQDKGLVAYV
     NVDRDSASRL GISMADVDNA LYNAFGQRLI STIYTQANQY RVVLEHNTEN TPGLAALDTI
     RLTSSDGGVV PLSSIAKIEQ RFAPLSINHL DQFPVTTISF NVPDNYSLGD AVQAIMDTEK
     TLNLPVDITT QFQGSTLAFQ SALGSTVWLI VAAVVAMYIV LGILYESFIH PITILSTLPT
     AGVGALLALM IAGSELDVIA IIGIILLIGI VKKNAIMMID FALAAEREQG MSPREAIYQA
     CLLRFRPILM TTLAALLGAL PLMLSTGVGA ELRRPLGIGM VGGLIVSQVL TLFTTPVIYL
     LFDRLALWTK SRFARHEEEA