BMR2_BACSU
ID BMR2_BACSU Reviewed; 400 AA.
AC P39843;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Multidrug resistance protein 2;
DE AltName: Full=Multidrug-efflux transporter 2;
GN Name=blt; Synonyms=bmr2, bmt; OrderedLocusNames=BSU26590;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / BD170;
RX PubMed=7608059; DOI=10.1128/jb.177.14.3904-3910.1995;
RA Ahmed M., Lyass L., Markham P.N., Taylor S.S., Vazquez-Laslop N.,
RA Neyfakh A.A.;
RT "Two highly similar multidrug transporters of Bacillus subtilis whose
RT expression is differentially regulated.";
RL J. Bacteriol. 177:3904-3910(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / JH642;
RX PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA Kobayashi Y.;
RT "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT Bacillus subtilis genome containing the skin element and many sporulation
RT genes.";
RL Microbiology 142:3103-3111(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
CC -!- FUNCTION: Energy-dependent efflux pump responsible for decreased drug
CC accumulation in multi-drug-resistant cells. Probably uses a
CC transmembrane proton gradient as the energy source. Causes the efflux
CC of a variety of toxic substances, including such structurally diverse
CC compounds as ethidium bromide, rhodamine and acridine dyes,
CC tetraphenylphosphonium, puromycin, chloramphenicol, doxorubicin, and
CC fluoroquinolone antibiotics.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. TCR/Tet
CC family. {ECO:0000305}.
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DR EMBL; L32599; AAC36944.1; -; Genomic_DNA.
DR EMBL; D84432; BAA12355.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14600.1; -; Genomic_DNA.
DR PIR; I39792; I39792.
DR RefSeq; NP_390536.1; NC_000964.3.
DR RefSeq; WP_003229880.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P39843; -.
DR SMR; P39843; -.
DR STRING; 224308.BSU26590; -.
DR TCDB; 2.A.1.2.8; the major facilitator superfamily (mfs).
DR PaxDb; P39843; -.
DR PRIDE; P39843; -.
DR DNASU; 937646; -.
DR EnsemblBacteria; CAB14600; CAB14600; BSU_26590.
DR GeneID; 937646; -.
DR KEGG; bsu:BSU26590; -.
DR PATRIC; fig|224308.179.peg.2889; -.
DR eggNOG; COG2814; Bacteria.
DR InParanoid; P39843; -.
DR OMA; LYADSFH; -.
DR PhylomeDB; P39843; -.
DR BioCyc; BSUB:BSU26590-MON; -.
DR Proteomes; UP000001570; 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:0042910; F:xenobiotic transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR004734; Multidrug-R.
DR InterPro; IPR005829; Sugar_transporter_CS.
DR InterPro; IPR001958; Tet-R_TetA/multi-R_MdtG.
DR Pfam; PF07690; MFS_1; 1.
DR PRINTS; PR01035; TCRTETA.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00880; 2_A_01_02; 1.
DR PROSITE; PS50850; MFS; 1.
DR PROSITE; PS00216; SUGAR_TRANSPORT_1; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..400
FT /note="Multidrug resistance protein 2"
FT /id="PRO_0000173318"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 78..98
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 253..273
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 297..317
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 346..366
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 368..388
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 400 AA; 43424 MW; 7F3A6EEC344CD4E7 CRC64;
MKKSINEQKT IFIILLSNIF VAFLGIGLII PVMPSFMKIM HLSGSTMGYL VAAFAISQLI
TSPFAGRWVD RFGRKKMIIL GLLIFSLSEL IFGLGTHVSI FYFSRILGGV SAAFIMPAVT
AYVADITTLK ERSKAMGYVS AAISTGFIIG PGAGGFIAGF GIRMPFFFAS AIALIAAVTS
VFILKESLSI EERHQLSSHT KESNFIKDLK RSIHPVYFIA FIIVFVMAFG LSAYETVFSL
FSDHKFGFTP KDIAAIITIS SIVAVVIQVL LFGKLVNKLG EKRMIQLCLI TGAILAFVST
VMSGFLTVLL VTCFIFLAFD LLRPALTAHL SNMAGNQQGF VAGMNSTYTS LGNIFGPALG
GILFDLNIHY PFLFAGFVMI VGLGLTMVWK EKKNDAAALN
