MDTB_YERPS
ID MDTB_YERPS Reviewed; 1052 AA.
AC Q668C6;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 89.
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=YPTB2814;
OS Yersinia pseudotuberculosis serotype I (strain IP32953).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=273123;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IP32953;
RX PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA Derbise A., Hauser L.J., Garcia E.;
RT "Insights into the evolution of Yersinia pestis through whole-genome
RT comparison with Yersinia pseudotuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
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}.
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DR EMBL; BX936398; CAH22052.1; -; Genomic_DNA.
DR RefSeq; WP_011192782.1; NZ_CP009712.1.
DR AlphaFoldDB; Q668C6; -.
DR SMR; Q668C6; -.
DR EnsemblBacteria; CAH22052; CAH22052; YPTB2814.
DR GeneID; 66844763; -.
DR KEGG; ypo:BZ17_3817; -.
DR KEGG; yps:YPTB2814; -.
DR PATRIC; fig|273123.14.peg.4006; -.
DR OMA; FIIPCFY; -.
DR Proteomes; UP000001011; 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 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_0000161830"
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"
FT REGION 1032..1052
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1052 AA; 113534 MW; 6728D74D31D42B66 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
RLTGSDGKGV PLNSIATIEE 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