MDTB_SALTY
ID MDTB_SALTY Reviewed; 1040 AA.
AC Q8ZNQ2;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=STM2127;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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; AE006468; AAL21031.1; -; Genomic_DNA.
DR RefSeq; NP_461072.1; NC_003197.2.
DR RefSeq; WP_001197805.1; NC_003197.2.
DR AlphaFoldDB; Q8ZNQ2; -.
DR SMR; Q8ZNQ2; -.
DR STRING; 99287.STM2127; -.
DR PaxDb; Q8ZNQ2; -.
DR EnsemblBacteria; AAL21031; AAL21031; STM2127.
DR GeneID; 1253648; -.
DR KEGG; stm:STM2127; -.
DR PATRIC; fig|99287.12.peg.2252; -.
DR HOGENOM; CLU_002755_1_1_6; -.
DR OMA; FIIPCFY; -.
DR PhylomeDB; Q8ZNQ2; -.
DR BioCyc; SENT99287:STM2127-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; IBA:GO_Central.
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; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1040
FT /note="Multidrug resistance protein MdtB"
FT /id="PRO_0000161827"
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; 111988 MW; 12518CD688D3E783 CRC64;
MQVLPPGSTG GPSRLFILRP VATTLLMAAI LLAGIIGYRF LPVAALPEVD YPTIQVVTLY
PGASPDVMTS AVTAPLERQF GQMSGLKQMS SQSSGGASVV TLQFQLTLPL DVAEQEVQAA
INAATNLLPS DLPNPPIYSK VNPADPPIMT LAVTSNSMPM 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 IPGVELYLQP
TQDLTIDTQV SRTQYQFTLQ ATTLDALSHW VPKLQNALQS LPQLSEVSSD WQDRGLAAWV
NVDRDSASRL GISMADVDNA LYNAFGQRLI STIYTQANQY RVVLEHNTAS MPGLAALETI
RLTSRDGGTV PLSAIARIEQ RFAPLSINHL DQFPVTTFSF NVPESYSLGD AVQAILDTEK
TLALPADITT QFQGSTLAFQ AALGSTVWLI VAAVVAMYIV LGVLYESFIH PITILSTLPT
AGVGALLALI IAGSELDIIA IIGIILLIGI VKKNAIMMID FALAAEREQG MSPRDAIFQA
CLLRFRPILM TTLAALLGAL PLMLSTGVGT ELRRPLGIAM VGGLLVSQVL TLFTTPVIYL
LFDRLSLYVK SRFPRHKEEA
