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MDTC_ECO57
ID   MDTC_ECO57              Reviewed;        1025 AA.
AC   Q7ACM1; Q8X7J3;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Multidrug resistance protein MdtC {ECO:0000255|HAMAP-Rule:MF_01424};
DE   AltName: Full=Multidrug transporter MdtC {ECO:0000255|HAMAP-Rule:MF_01424};
GN   Name=mdtC {ECO:0000255|HAMAP-Rule:MF_01424};
GN   OrderedLocusNames=Z3245, ECs2884;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: The MdtABC tripartite complex confers resistance against
CC       novobiocin and deoxycholate. {ECO:0000255|HAMAP-Rule:MF_01424}.
CC   -!- SUBUNIT: Part of a tripartite efflux system composed of MdtA, MdtB and
CC       MdtC. MdtC forms a heteromultimer with MdtB. {ECO:0000255|HAMAP-
CC       Rule:MF_01424}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01424}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01424}.
CC   -!- INDUCTION: The mdtABC operon is transcriptionally activated by BaeR.
CC   -!- SIMILARITY: Belongs to the resistance-nodulation-cell division (RND)
CC       (TC 2.A.6) family. MdtC subfamily. {ECO:0000255|HAMAP-Rule:MF_01424}.
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DR   EMBL; AE005174; AAG57139.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB36307.1; -; Genomic_DNA.
DR   PIR; D90989; D90989.
DR   PIR; G85834; G85834.
DR   RefSeq; NP_310911.1; NC_002695.1.
DR   RefSeq; WP_000667528.1; NZ_SDVX01000004.1.
DR   AlphaFoldDB; Q7ACM1; -.
DR   SMR; Q7ACM1; -.
DR   STRING; 155864.EDL933_3151; -.
DR   EnsemblBacteria; AAG57139; AAG57139; Z3245.
DR   EnsemblBacteria; BAB36307; BAB36307; ECs_2884.
DR   GeneID; 916586; -.
DR   KEGG; ece:Z3245; -.
DR   KEGG; ecs:ECs_2884; -.
DR   PATRIC; fig|386585.9.peg.3016; -.
DR   eggNOG; COG0841; Bacteria.
DR   HOGENOM; CLU_002755_1_2_6; -.
DR   OMA; WRGVRTD; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; 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:UniProtKB-UniRule.
DR   Gene3D; 3.30.2090.10; -; 2.
DR   HAMAP; MF_01424; MdtC; 1.
DR   InterPro; IPR027463; AcrB_DN_DC_subdom.
DR   InterPro; IPR001036; Acrflvin-R.
DR   InterPro; IPR023931; Multidrug-R_MdtC.
DR   PANTHER; PTHR32063; PTHR32063; 1.
DR   Pfam; PF00873; ACR_tran; 1.
DR   PRINTS; PR00702; ACRIFLAVINRP.
DR   SUPFAM; SSF82714; SSF82714; 2.
PE   2: Evidence at transcript level;
KW   Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..1025
FT                   /note="Multidrug resistance protein MdtC"
FT                   /id="PRO_0000161833"
FT   TOPO_DOM        1..6
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        7..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01424"
FT   TOPO_DOM        30..335
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        336..353
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01424"
FT   TOPO_DOM        354..359
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        360..379
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01424"
FT   TOPO_DOM        380..388
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        389..411
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01424"
FT   TOPO_DOM        412..430
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        431..453
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01424"
FT   TOPO_DOM        454..467
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        468..490
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01424"
FT   TOPO_DOM        491..852
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        853..875
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01424"
FT   TOPO_DOM        876..894
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        895..917
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01424"
FT   TOPO_DOM        918..947
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        948..970
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01424"
FT   TOPO_DOM        971..984
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        985..1007
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01424"
FT   TOPO_DOM        1008..1025
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1025 AA;  111048 MW;  97DEF74B3CD814B9 CRC64;
     MKFFALFIYR PVATILLSVA ITLCGILGFR MLPVAPLPQV DFPVIMVSAS LPGASPETMA
     SSVATPLERS LGRIAGVSEM TSSSSLGSTR IILQFDFDRD INGAARDVQA AINAAQSLLP
     SGMPSRPTYR KANPSDAPIM ILTLTSDTYS QGELYDFAST QLAPTISQID GVGDVDVGGS
     SLPAVRVGLN PQALFNQGVS LDDVRTAISN ANVRKPQGAL EDGTHRWQIQ TNDELKTAAE
     YQPLIIHYNN GGAVRLGDVA TVTDSVQDVR NAGMTNAKPA ILLMIRKLPE ANIIQTVDSI
     RAKLPELQET IPAAIDLQIA QDRSPTIRAS LEEVEQTLII SVALVILVVF LFLRSGRATI
     IPAVAVPVSL IGTFAAMYLC GFSLNNLSLM ALTIATGFVV DDAIVVLENI ARHLEAGMKP
     LQAALQGTRE VGFTVLSMSL SLVAVFLPLL LMGGLPGRLL REFAVTLSVA IGISLLVSLT
     LTPMMCGWML KASKPREQKR LRGFGRMLVA LQQGYGKSLK WVLNHTRLVG MVLLGTIALN
     IWLYISIPKT FFPEQDTGVL MGGIQADQSI SFQAMRGKLQ DFMKIIRDDP AVDNVTGFTG
     GSRVNSGMMF ITLKPRDERS ETAQQIIDRL RVKLAKEPGA NLFLMAVQDI RVGGRQSNAS
     YQYTLLSDDL AALREWEPKI RKKLATLPEL ADVNSDQQDN GAEMNLVYDR DTMARLGIDV
     QAANSLLNNA FGQRQISTIY QPMNQYKVVM EVDPRYTQDI SALEKMFVIN NEGKAIPLSY
     FAKWQPANAP LSVNHQGLSA ASTISFNLPT GKSLSDASAA IDRAMTQLGV PSTVRGSFAG
     TAQVFQETMN SQVILIIAAI ATVYIVLGIL YESYVHPLTI LSTLPSAGVG ALLALELFNA
     PFSLIALIGI MLLIGIVKKN AIMMVDFALE AQRHGNLTPQ EAIFQACLLR FRPIMMTTLA
     ALFGALPLVL SGGDGSELRQ PLGITIVGGL VMSQLLTLYT TPVVYLFFDR LRLRFSRKSK
     QTVTE
 
 
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