ID   MDTB_ECOHS              Reviewed;        1040 AA.
AC   A8A1U7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 74.
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=EcHS_A2217;
OS   Escherichia coli O9:H4 (strain HS).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=331112;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HS;
RX   PubMed=18676672; DOI=10.1128/jb.00619-08;
RA   Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA   Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA   Henderson I.R., Sperandio V., Ravel J.;
RT   "The pangenome structure of Escherichia coli: comparative genomic analysis
RT   of E. coli commensal and pathogenic isolates.";
RL   J. Bacteriol. 190:6881-6893(2008).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000802; ABV06501.1; -; Genomic_DNA.
DR   RefSeq; WP_001197829.1; NC_009800.1.
DR   AlphaFoldDB; A8A1U7; -.
DR   SMR; A8A1U7; -.
DR   KEGG; ecx:EcHS_A2217; -.
DR   HOGENOM; CLU_002755_1_2_6; -.
DR   OMA; FIIPCFY; -.
DR   Proteomes; UP000001123; 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_1000068503"
FT   TRANSMEM        16..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01423"
FT   TRANSMEM        347..367
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01423"
FT   TRANSMEM        369..389
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01423"
FT   TRANSMEM        396..416
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01423"
FT   TRANSMEM        440..460
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01423"
FT   TRANSMEM        472..492
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01423"
FT   TRANSMEM        537..557
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01423"
FT   TRANSMEM        863..883
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01423"
FT   TRANSMEM        888..908
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01423"
FT   TRANSMEM        911..931
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01423"
FT   TRANSMEM        968..988
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01423"
FT   TRANSMEM        998..1018
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01423"
SQ   SEQUENCE   1040 AA;  112090 MW;  06C2D5A0492894F7 CRC64;
     MQVLPPSSTG GPSRLFIMRP VATTLLMVAI LLAGIIGYRA LPVSALPEVD YPTIQVVTLY
     PGASPDVMTS AVTAPLERQF GQMSGLKQMS SQSSGGASVI TLQFQLTLPL DVAEQEVQAA
     INAATNLLPS DLPNPPVYSK VNPADPPIMT LAVTSIAMPM 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
     AGVGALLALL IAGSELDVIA IIGIILLIGI VKKNAIMMID FALAAEREQG MSPREAIYQA
     CLLRFRPILM TTLAALLGAL PLMLSTGVGA ELRRPLGIGM VGGLIVSQVL TLFTTPVIYL
     LFDRLALWTK SRFARHEEEA