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TAP_MYCBP
ID   TAP_MYCBP               Reviewed;         419 AA.
AC   A0A0H3M5L9;
DT   05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT   16-SEP-2015, sequence version 1.
DT   25-MAY-2022, entry version 28.
DE   RecName: Full=Multidrug efflux pump Tap {ECO:0000305};
GN   Name=tap {ECO:0000303|PubMed:22232275};
GN   OrderedLocusNames=BCG_1316c {ECO:0000312|EMBL:CAL71303.1};
OS   Mycobacterium bovis (strain BCG / Pasteur 1173P2).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=410289;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCG / Pasteur 1173P2;
RX   PubMed=17372194; DOI=10.1073/pnas.0700869104;
RA   Brosch R., Gordon S.V., Garnier T., Eiglmeier K., Frigui W., Valenti P.,
RA   Dos Santos S., Duthoy S., Lacroix C., Garcia-Pelayo C., Inwald J.K.,
RA   Golby P., Garcia J.N., Hewinson R.G., Behr M.A., Quail M.A., Churcher C.,
RA   Barrell B.G., Parkhill J., Cole S.T.;
RT   "Genome plasticity of BCG and impact on vaccine efficacy.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:5596-5601(2007).
RN   [2]
RP   FUNCTION, ACTIVITY REGULATION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=BCG / Pasteur 1173P2;
RX   PubMed=22232275; DOI=10.1128/aac.05946-11;
RA   Ramon-Garcia S., Mick V., Dainese E., Martin C., Thompson C.J.,
RA   De Rossi E., Manganelli R., Ainsa J.A.;
RT   "Functional and genetic characterization of the tap efflux pump in
RT   Mycobacterium bovis BCG.";
RL   Antimicrob. Agents Chemother. 56:2074-2083(2012).
CC   -!- FUNCTION: Efflux pump that contributes to intrinsic antibiotic
CC       resistance. The pump uses the electrochemical gradient as a source of
CC       energy. Confers resistance to various antibiotics, including
CC       tetracycline, acriflavine, spectinomycin and p-aminosalicylate. May be
CC       involved in export of toxic by-products that accumulate during
CC       stationary phase when nutrients are limited.
CC       {ECO:0000269|PubMed:22232275}.
CC   -!- ACTIVITY REGULATION: Efflux activity is inhibited by carbonyl cyanide
CC       m-chlorophenylhydrazone (CCCP). {ECO:0000269|PubMed:22232275}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC       membrane protein {ECO:0000255}.
CC   -!- DISRUPTION PHENOTYPE: Disruption mutant shows changes in morphology,
CC       growth defects and a progressive loss of viability upon subcultivation
CC       in liquid medium. Disruption leads to an extensive change in gene
CC       expression patterns during stationary phase, with no changes during
CC       exponential growth. It also alters susceptibility to many antibiotics.
CC       {ECO:0000269|PubMed:22232275}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. Drug:H(+)
CC       antiporter-3 (DHA3) (TC 2.A.1.21) family. {ECO:0000305}.
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DR   EMBL; AM408590; CAL71303.1; -; Genomic_DNA.
DR   RefSeq; WP_003406359.1; NC_008769.1.
DR   AlphaFoldDB; A0A0H3M5L9; -.
DR   SMR; A0A0H3M5L9; -.
DR   KEGG; mbb:BCG_1316c; -.
DR   HOGENOM; CLU_034180_2_0_11; -.
DR   OMA; MVVNIPM; -.
DR   Proteomes; UP000001472; 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:InterPro.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.1250.20; -; 2.
DR   InterPro; IPR011701; MFS.
DR   InterPro; IPR020846; MFS_dom.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   Pfam; PF07690; MFS_1; 1.
DR   SUPFAM; SSF103473; SSF103473; 1.
DR   PROSITE; PS50850; MFS; 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance; Cell inner membrane; Cell membrane; Membrane;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..419
FT                   /note="Multidrug efflux pump Tap"
FT                   /id="PRO_0000447328"
FT   TRANSMEM        7..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        44..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        73..95
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        100..122
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        149..171
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        175..197
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        218..240
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        260..282
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        289..308
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        313..335
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        348..370
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        375..397
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   419 AA;  43287 MW;  69EA46BBFF653037 CRC64;
     MRNSNRGPAF LILFATLMAA AGDGVSIVAF PWLVLQREGS AGQASIVASA TMLPLLFATL
     VAGTAVDYFG RRRVSMVADA LSGAAVAGVP LVAWGYGGDA VNVLVLAVLA ALAAAFGPAG
     MTARDSMLPE AAARAGWSLD RINGAYEAIL NLAFIVGPAI GGLMIATVGG ITTMWITATA
     FGLSILAIAA LQLEGAGKPH HTSRPQGLVS GIAEGLRFVW NLRVLRTLGM IDLTVTALYL
     PMESVLFPKY FTDHQQPVQL GWALMAIAGG GLVGALGYAV LAIRVPRRVT MSTAVLTLGL
     ASMVIAFLPP LPVIMVLCAV VGLVYGPIQP IYNYVIQTRA AQHLRGRVVG VMTSLAYAAG
     PLGLLLAGPL TDAAGLHATF LALALPIVCT GLVAIRLPAL RELDLAPQAD IDRPVGSAQ
 
 
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