MDTB_SALA4
ID MDTB_SALA4 Reviewed; 1040 AA.
AC B5EXV7;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 25-MAY-2022, entry version 64.
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=SeAg_B2257;
OS Salmonella agona (strain SL483).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=454166;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SL483;
RX PubMed=21602358; DOI=10.1128/jb.00297-11;
RA Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA Leclerc J.E., Ravel J., Cebula T.A.;
RT "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT CRISPR-mediated adaptive sublineage evolution.";
RL J. Bacteriol. 193:3556-3568(2011).
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 ---------------------------------------------------------------------------
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; CP001138; ACH48807.1; -; Genomic_DNA.
DR RefSeq; WP_001197797.1; NC_011149.1.
DR AlphaFoldDB; B5EXV7; -.
DR SMR; B5EXV7; -.
DR EnsemblBacteria; ACH48807; ACH48807; SeAg_B2257.
DR KEGG; sea:SeAg_B2257; -.
DR HOGENOM; CLU_002755_1_1_6; -.
DR OMA; FIIPCFY; -.
DR Proteomes; UP000008819; 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..1040
FT /note="Multidrug resistance protein MdtB"
FT /id="PRO_1000145657"
FT TRANSMEM 25..45
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 910..930
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; 111823 MW; 8DB77110FC1D36B5 CRC64;
MQVLPPGSTG GPSRLFILRP VATTLLMAAI LLAGIIGYRF LPVAALPEVD YPTIQVVTLY
PGASPDVMTS AVTAPLERQF GQMSGLKQMS SQSSGGASVV TLQFQLTLPL DVAEQEVQAA
INAATNLLPS DLPNPPIYSK VNPADPPIMT LAVTSNAMPM TQVEDMVETR VAQKISQVSG
VGLVTLAGGQ RPAVRVKLNA QAVAALGLTS ETVRTAITGA NVNSAKGSLD GPERAVTLSA
NDQMQSADEY RRLIIAYQNG APVRLGDVAT VEQGAENSWL GAWANQAPAI VMNVQRQPGA
NIIATADSIR QMLPQLTESL PKSVKVTVLS DRTTNIRASV RDTQFELMLA IALVVMIIYL
FLRNIPATII PGVAVPLSLI GTFAVMVFLD FSINNLTLMA LTIATGFVVD DAIVVIENIS
RYIEKGEKPL AAALKGAGEI GFTIISLTFS LIAVLIPLLF MGDIVGRLFR EFAVTLAVAI
LISAVVSLTL TPMMCARMLS QQSLRKQNRF SRACERMFDR VIASYGRGLA KVLNHPWLTL
SVAFATLLLS VMLWIVIPKG FFPVQDNGII QGTLQAPQSS SYASMAQRQR QVAERILQDP
AVQSLTTFVG VDGANPTLNS ARLQINLKPL DARDDRVQQV ISRLQTAVAT IPGVALYLQP
TQDLTIDTQV SRTQYQFTLQ ATTLDALSHW VPKLQNALQS LPQLSEVSSD WQDRGLAAWV
NVDRDSASRL GISMADVDNA LYNAFGQRLI STIYTQANQY RVVLEHNTAS TPGLAALETI
RLTSRDGGTV PLSAIARIEQ RFAPLSINHL DQFPVTTFSF NVPEGYSLGD AVQAILDTEK
TLALPADITT QFQGSTLAFQ AALGSTVWLI VAAVVAMYIV LGVLYESFIH PITILSTLPT
AGVGALLALI IAGSELDIIA IIGIILLIGI VKKNAIMMID FALAAEREQG MSPRDAIFQA
CLLRFRPILM TTLAALLGAL PLMLSTGVGA ELRRPLGIAM VGGLLVSQVL TLFTTPVIYL
LFDRLSLYVK SRFPRHKEEA