ID   MDTB_ECO8A              Reviewed;        1040 AA.
AC   B7M458;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   25-MAY-2022, entry version 70.
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=ECIAI1_2151;
OS   Escherichia coli O8 (strain IAI1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585034;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IAI1;
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
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; CU928160; CAQ98997.1; -; Genomic_DNA.
DR   RefSeq; WP_001197905.1; NC_011741.1.
DR   AlphaFoldDB; B7M458; -.
DR   SMR; B7M458; -.
DR   GeneID; 66674025; -.
DR   KEGG; ecr:ECIAI1_2151; -.
DR   HOGENOM; CLU_002755_1_2_6; -.
DR   OMA; FIIPCFY; -.
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_1000145650"
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;  112130 MW;  D58762C9F03D6038 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 NDTQFELMMA IALVVMIIYL
     FLRNIPATII PGFAVPLSLI 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 VPELMEKLQQ 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 MSPRDAIYQA
     CLLRFRPILM TTLAALLGAL PLMLSTGVGA ELRRPLGIGM VGGLIVSQVL TLFTTPVIYL
     LFDRLALWTK SRFARHEEEA