ID   MDTB_YERP1              Reviewed;        1052 AA.
AC   D0JNB0;
DT   16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, sequence version 2.
DT   25-MAY-2022, entry version 43.
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=YPD8_2453;
OS   Yersinia pestis (strain D182038).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=637385;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D182038;
RX   PubMed=19815893; DOI=10.4269/ajtmh.2009.09-0174;
RA   Zhang Z., Hai R., Song Z., Xia L., Liang Y., Cai H., Liang Y., Shen X.,
RA   Zhang E., Xu J., Yu D., Yu X.J.;
RT   "Spatial variation of Yersinia pestis from Yunnan Province of China.";
RL   Am. J. Trop. Med. Hyg. 81:714-717(2009).
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   -!- SIMILARITY: Belongs to the resistance-nodulation-cell division (RND)
CC       (TC 2.A.6) family. MdtB subfamily. {ECO:0000255|HAMAP-Rule:MF_01423}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ACY63128.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=ACY63128.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CP001589; ACY63128.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; D0JNB0; -.
DR   SMR; D0JNB0; -.
DR   KEGG; ypx:YPD8_2453; -.
DR   PATRIC; fig|637385.3.peg.3284; -.
DR   HOGENOM; CLU_002755_1_2_6; -.
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   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..1052
FT                   /note="Multidrug resistance protein MdtB"
FT                   /id="PRO_0000414032"
FT   TRANSMEM        16..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01423"
FT   TRANSMEM        342..362
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01423"
FT   TRANSMEM        373..393
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        1002..1022
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01423"
FT   REGION          1032..1052
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1052 AA;  113533 MW;  FFC2D74E485E2B61 CRC64;
     MQVMPPTPGG GPSRLFILRP VATTLFMIAI LLAGIIGYRA LPVSALPEVD YPTIQVVTLY
     PGASPDVVTS SITAPLERQF GQMSGLKQMA SQSSGGASVI TLQFQLTLPL DVAEQEVQAA
     INAATNLLPS DLPYPPIYNK VNPADPPILT LAVTATAIPM TQVEDMVETR IAQKISQVTG
     VGLVTLSGGQ RPAVRVKLNA PAVAALGLDS ETIRTAISNA NVNSAKGSLD GPTRSVTLSA
     NDQMKSAEEY RDLIIAYQNG APIRLQDVAT IEQGAENNKL AAWANTQSAI VLNIQRQPGV
     NVIATADSIR EMLPELIKSL PKSVDVKVLT DRTSTIRASV NDVQFELLLA IALVVMVIYL
     FLRNAAATII PSIAVPLSLV GTFAAMYFLG FSINNLTLMA LTIATGFVVD DAIVVIENIS
     RYIEKGEKPL DAALKGAGEI GFTIISLTFS LIAVLIPLLF MEDIVGRLFR EFAVTLAVAI
     LISAVVSLTL TPMMCARMLS YESLRKQNRL SRASEKFFDW VIAHYAVALK KVLNHPWLTL
     SVAFSTLVLT VILYLLIPKG FFPLQDNGLI QGTLEAPQSV SFSNMAERQQ QVAAIILKDP
     AVESLTSFVG VDGTNATLNN GRLQINLKPL SERDDRIPQI ITRLQESVSG VPGIKLYLQP
     VQDLTIDTQL SRTQYQFTLQ ATSLEELSTW VPKLVNELQQ KAPFQDVTSD WQDQGLVAFV
     NVDRDSASRL GITMAAIDNA LYNAFGQRLI STIYTQSNQY RVVLEHDVQA TPGLAAFNDI
     RLTGIDGKGV PLSSIATIEE RFGPLSINHL NQFPSATVSF NLAQGYSLGE AVAAVTLAEK
     EIQLPADITT RFQGSTLAFQ AALGSTLWLI IAAIVAMYIV LGVLYESFIH PITILSTLPT
     AGVGALLALM LTGNELDVIA IIGIILLIGI VKKNAIMMID FALAAERDQG MTPYDAIYQA
     CLLRFRPILM TTLAALFGAL PLMLSTGVGA ELRQPLGVCM VGGLIVSQVL TLFTTPVIYL
     LFDKLARNTR GKNRHRDEDI DSSELLNGQE PQ