MDTB_ECOLI
ID MDTB_ECOLI Reviewed; 1040 AA.
AC P76398; O08005;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 155.
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}; Synonyms=yegN;
GN OrderedLocusNames=b2075, JW2060;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
RC STRAIN=K12;
RX PubMed=12107133; DOI=10.1128/jb.184.15.4161-4167.2002;
RA Nagakubo S., Nishino K., Hirata T., Yamaguchi A.;
RT "The putative response regulator BaeR stimulates multidrug resistance of
RT Escherichia coli via a novel multidrug exporter system, MdtABC.";
RL J. Bacteriol. 184:4161-4167(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP FUNCTION, AND INDUCTION.
RX PubMed=12107134; DOI=10.1128/jb.184.15.4168-4176.2002;
RA Baranova N., Nikaido H.;
RT "The baeSR two-component regulatory system activates transcription of the
RT yegMNOB (mdtABCD) transporter gene cluster in Escherichia coli and
RT increases its resistance to novobiocin and deoxycholate.";
RL J. Bacteriol. 184:4168-4176(2002).
CC -!- FUNCTION: The MdtABC tripartite complex confers resistance against
CC novobiocin and deoxycholate. MdtABC requires TolC for its function.
CC {ECO:0000255|HAMAP-Rule:MF_01423, ECO:0000269|PubMed:12107133,
CC ECO:0000269|PubMed:12107134}.
CC -!- SUBUNIT: Part of a tripartite efflux system composed of MdtA, MdtB and
CC MdtC. MdtB forms a heteromultimer with MdtC.
CC -!- INTERACTION:
CC P76398; P76399: mdtC; NbExp=4; IntAct=EBI-561416, EBI-1116694;
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 {ECO:0000255|HAMAP-Rule:MF_01423, ECO:0000269|PubMed:12107133,
CC ECO:0000269|PubMed:12107134}.
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; AB089188; BAC06608.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75136.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15929.1; -; Genomic_DNA.
DR PIR; B64974; B64974.
DR RefSeq; NP_416579.1; NC_000913.3.
DR RefSeq; WP_001197875.1; NZ_STEB01000002.1.
DR AlphaFoldDB; P76398; -.
DR SMR; P76398; -.
DR BioGRID; 4262010; 465.
DR ComplexPortal; CPX-2119; MdtABC-TolC multidrug efflux transport complex.
DR DIP; DIP-11884N; -.
DR IntAct; P76398; 3.
DR STRING; 511145.b2075; -.
DR TCDB; 2.A.6.2.12; the resistance-nodulation-cell division (rnd) superfamily.
DR jPOST; P76398; -.
DR PaxDb; P76398; -.
DR PRIDE; P76398; -.
DR EnsemblBacteria; AAC75136; AAC75136; b2075.
DR EnsemblBacteria; BAA15929; BAA15929; BAA15929.
DR GeneID; 946606; -.
DR KEGG; ecj:JW2060; -.
DR KEGG; eco:b2075; -.
DR PATRIC; fig|511145.12.peg.2152; -.
DR EchoBASE; EB3810; -.
DR eggNOG; COG0841; Bacteria.
DR HOGENOM; CLU_002755_1_2_6; -.
DR InParanoid; P76398; -.
DR OMA; FIIPCFY; -.
DR PhylomeDB; P76398; -.
DR BioCyc; EcoCyc:B2075-MON; -.
DR BioCyc; MetaCyc:B2075-MON; -.
DR PRO; PR:P76398; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:1990281; C:efflux pump complex; IC:ComplexPortal.
DR GO; GO:0005887; C:integral component of plasma membrane; ISM:EcoCyc.
DR GO; GO:0098567; C:periplasmic side of plasma membrane; IC:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0015125; F:bile acid transmembrane transporter activity; IMP:EcoCyc.
DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015721; P:bile acid and bile salt transport; IMP:EcoCyc.
DR GO; GO:0140330; P:xenobiotic detoxification by transmembrane export across the cell outer membrane; IC:ComplexPortal.
DR GO; GO:0042908; P:xenobiotic transport; IMP:EcoCyc.
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 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1040
FT /note="Multidrug resistance protein MdtB"
FT /id="PRO_0000161821"
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; 112078 MW; 195E3D989C7AC6F0 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
AGVGALLALL IAGSELDVIA IIGIILLIGI VKKNAIMMID FALAAEREQG MSPREAIYQA
CLLRFRPILM TTLAALLGAL PLMLSTGVGA ELRRPLGIGM VGGLIVSQVL TLFTTPVIYL
LFDRLALWTK SRFARHEEEA
