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TAP_MYCFO
ID   TAP_MYCFO               Reviewed;         409 AA.
AC   O32859;
DT   05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Multidrug efflux pump Tap {ECO:0000305};
DE   AltName: Full=Tetracycline-aminoglycoside resistance protein {ECO:0000303|PubMed:9811639};
GN   Name=tap {ECO:0000303|PubMed:9811639};
OS   Mycolicibacterium fortuitum (Mycobacterium fortuitum).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=1766;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX   PubMed=9811639; DOI=10.1128/jb.180.22.5836-5843.1998;
RA   Ainsa J.A., Blokpoel M.C., Otal I., Young D.B., De Smet K.A., Martin C.;
RT   "Molecular cloning and characterization of Tap, a putative multidrug efflux
RT   pump present in Mycobacterium fortuitum and Mycobacterium tuberculosis.";
RL   J. Bacteriol. 180:5836-5843(1998).
RN   [2]
RP   FUNCTION, ACTIVITY REGULATION, AND SUBCELLULAR LOCATION.
RX   PubMed=16373429; DOI=10.1093/jac/dki436;
RA   Ramon-Garcia S., Martin C., Ainsa J.A., De Rossi E.;
RT   "Characterization of tetracycline resistance mediated by the efflux pump
RT   Tap from Mycobacterium fortuitum.";
RL   J. Antimicrob. Chemother. 57:252-259(2006).
CC   -!- FUNCTION: Efflux pump that contributes to intrinsic antibiotic
CC       resistance (PubMed:9811639, PubMed:16373429). The pump uses the
CC       electrochemical gradient as a source of energy (PubMed:16373429).
CC       Confers low-level resistance to tetracycline and to several
CC       aminoglycosides, including streptomycin, gentamicin, 2'-N-
CC       ethylnetilmicin and 6'-N-ethylnetilmicin (PubMed:9811639,
CC       PubMed:16373429). {ECO:0000269|PubMed:16373429,
CC       ECO:0000269|PubMed:9811639}.
CC   -!- ACTIVITY REGULATION: Efflux activity is inhibited by carbonyl cyanide
CC       m-chlorophenylhydrazone (CCCP) and reserpine, but not by o-vanadate or
CC       chlorpromazine (CPZ). {ECO:0000269|PubMed:16373429}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000305|PubMed:16373429}; Multi-pass membrane protein
CC       {ECO:0000255}.
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; AJ000283; CAA03986.1; -; Genomic_DNA.
DR   AlphaFoldDB; O32859; -.
DR   SMR; O32859; -.
DR   STRING; 1766.XA26_44520; -.
DR   TCDB; 2.A.1.21.4; the major facilitator superfamily (mfs).
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; IPR004751; Drug_antiport.
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   TIGRFAMs; TIGR00900; 2A0121; 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..409
FT                   /note="Multidrug efflux pump Tap"
FT                   /id="PRO_0000447329"
FT   TRANSMEM        10..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        46..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        80..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        104..123
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        144..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        174..193
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   409 AA;  42528 MW;  E17FC353BFE27185 CRC64;
     MTNTKRGPLL LILFAALTAG AGNGITIVAF PWLVLQHNGS ALDASIVAMA GTLPLLVATL
     IAGAAVDYLG RRRVSMISDL LSALSVAAVP VLALIFGVDA VNVAVLAVLA GLGAFFDPAG
     MTARETMLPE AAGRAGWTLD HANSVYEAVF NLGYIVGPGI GGLMIATLGG INTMWVTAGA
     FCCSILAISV LRLEGAGAPD RSVLTEAVLA GIVEGLRFVW YTPVLRTLAI VDLVATGLYM
     PMESVLFPKY FTDRNEPTEL GWVLMALSIG GLLGALGYAV MSRYMSRRAT MLTAVITLGV
     AMTVIAFLPP LPLILVLCAI VGFVYGPIAP IYNYVMQTTA PQHLRGRVVG VMGSLAYAAG
     PLGLILAGPL ADAAGLHATF LALSLPMLLL GVVAVFLPRL RELDLASKP
 
 
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