(data stored in SCRATCH zone)

SWISSPROT: 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   11-DEC-2019, entry version 126.
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}.
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   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; BSU26590.
DR   GeneID; 937646; -.
DR   KEGG; bsu:BSU26590; -.
DR   PATRIC; fig|224308.179.peg.2889; -.
DR   eggNOG; COG0477; LUCA.
DR   HOGENOM; HOG000266878; -.
DR   InParanoid; P39843; -.
DR   KO; K08153; -.
DR   OMA; LYADSFH; -.
DR   PhylomeDB; P39843; -.
DR   BioCyc; BSUB:BSU26590-MONOMER; -.
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   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;
DR   PRODOM; P39843.
DR   SWISS-2DPAGE; P39843.
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
//

If you have problems or comments...

PBIL Back to PBIL home page