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MDREP_MYCTU
ID   MDREP_MYCTU             Reviewed;        1194 AA.
AC   O53645; I6Y740; L0T5S9;
DT   29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 154.
DE   RecName: Full=Multidrug efflux ATP-binding/permease protein Rv0194 {ECO:0000305};
DE            EC=7.6.2.- {ECO:0000305};
GN   OrderedLocusNames=Rv0194 {ECO:0000312|EMBL:CCP42922.1},
GN   RVBD_0194 {ECO:0000312|EMBL:AFN48045.1};
GN   ORFNames=P425_00203 {ECO:0000312|EMBL:KBJ41303.1};
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RG   The Broad Institute Genome Sequencing Platform;
RA   Galagan J., Kreiswirth B., Dobos K., Fortune S., Fitzgerald M., Young S.K.,
RA   Zeng Q., Gargeya S., Abouelleil A., Alvarado L., Berlin A.M., Chapman S.B.,
RA   Gainer-Dewar J., Goldberg J., Gnerre S., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA   Poon T., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The genome sequence of Mycobacterium tuberculosis H37Rv.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RG   The Broad Institute Genomics Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Earl A.M., Kreiswirth B., Gomez J., Victor T., Desjardins C., Abeel T.,
RA   Young S., Zeng Q., Gargeya S., Abouelleil A., Alvarado L., Chapman S.B.,
RA   Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Larimer J., Murphy C., Naylor J., Pearson M., Poon T.W.,
RA   Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The genome sequence of Mycobacterium tuberculosis H37Rv.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   FUNCTION IN ANTIBIOTIC RESISTANCE, AND ACTIVITY REGULATION.
RC   STRAIN=H37Rv;
RX   PubMed=18458127; DOI=10.1128/aac.00298-08;
RA   Danilchanka O., Mailaender C., Niederweis M.;
RT   "Identification of a novel multidrug efflux pump of Mycobacterium
RT   tuberculosis.";
RL   Antimicrob. Agents Chemother. 52:2503-2511(2008).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC   -!- FUNCTION: Overexpression in M. smegmatis increases resistance to
CC       erythromycin, ampicillin, novobiocin and vancomycin. It also reduces
CC       accumulation of ethidium bromide in the cell.
CC       {ECO:0000269|PubMed:18458127}.
CC   -!- ACTIVITY REGULATION: Efflux is inhibited by reserpine.
CC       {ECO:0000269|PubMed:18458127}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC       membrane protein {ECO:0000255}.
CC   -!- DOMAIN: The ATP-binding domains (NBD) and the transmembrane domains
CC       (TMD) are fused. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. Lipid exporter
CC       (TC 3.A.1.106) family. {ECO:0000305}.
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DR   EMBL; AL123456; CCP42922.1; -; Genomic_DNA.
DR   EMBL; CP003248; AFN48045.1; -; Genomic_DNA.
DR   EMBL; JLDD01000001; KBJ41303.1; -; Genomic_DNA.
DR   RefSeq; NP_214708.1; NC_000962.3.
DR   RefSeq; WP_003911097.1; NZ_NVQJ01000001.1.
DR   AlphaFoldDB; O53645; -.
DR   SMR; O53645; -.
DR   STRING; 83332.Rv0194; -.
DR   ChEMBL; CHEMBL3879861; -.
DR   TCDB; 3.A.1.106.6; the atp-binding cassette (abc) superfamily.
DR   PaxDb; O53645; -.
DR   PRIDE; O53645; -.
DR   GeneID; 886790; -.
DR   KEGG; mtu:Rv0194; -.
DR   KEGG; mtv:RVBD_0194; -.
DR   PATRIC; fig|83332.111.peg.223; -.
DR   TubercuList; Rv0194; -.
DR   eggNOG; COG1132; Bacteria.
DR   OMA; RSDANFW; -.
DR   PhylomeDB; O53645; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR   GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR   GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0015562; F:efflux transmembrane transporter activity; IMP:MTBBASE.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR   GO; GO:1990961; P:xenobiotic detoxification by transmembrane export across the plasma membrane; IMP:MTBBASE.
DR   Gene3D; 1.20.1560.10; -; 2.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR011527; ABC1_TM_dom.
DR   InterPro; IPR036640; ABC1_TM_sf.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR039421; Type_1_exporter.
DR   PANTHER; PTHR24221; PTHR24221; 2.
DR   Pfam; PF00664; ABC_membrane; 2.
DR   Pfam; PF00005; ABC_tran; 2.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   SUPFAM; SSF90123; SSF90123; 2.
DR   PROSITE; PS50929; ABC_TM1F; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   1: Evidence at protein level;
KW   Antibiotic resistance; ATP-binding; Cell inner membrane; Cell membrane;
KW   Membrane; Nucleotide-binding; Reference proteome; Repeat; Translocase;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..1194
FT                   /note="Multidrug efflux ATP-binding/permease protein
FT                   Rv0194"
FT                   /id="PRO_0000432861"
FT   TRANSMEM        20..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        56..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        130..150
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        153..173
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        258..278
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        279..299
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        628..648
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        660..680
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        743..763
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        765..785
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        847..867
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        878..898
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          21..301
FT                   /note="ABC transmembrane type-1 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          334..568
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   DOMAIN          628..910
FT                   /note="ABC transmembrane type-1 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          942..1177
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         367..374
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         976..983
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   1194 AA;  129251 MW;  079950FB1BEB581E CRC64;
     MRTNCWWRLS GYVMRHRRDL LLGFGAALAG TVIAVLVPLV TKRVIDDAIA ADHRPLAPWA
     VVLVAAAGAT YLLMYVRRYY GGRIAHLVQH DLRMDAFQAL LRWDGRQQDR WSSGQLIVRT
     TNDLQLVQAL LFDVPNVLRH VLTLLLGVAV MTWLSVPLAL LAVLLVPVIG LIAHRSRRLL
     AAATHCAQEH KAAVTGVVDA AVCGIRVVKA FGQEERETVK LVTASRALYA AQLRVARLNA
     HFGPLLQTLP ALGQMAVFAL GGWMAAQGSI TVGTFVAFWA CLTLLARPAC DLAGMLTIAQ
     QARAGAVRVL ELIDSRPTLV DGTKPLSPEA RLSLEFQRVS FGYVADRPVL REISLSVRAG
     ETLAVVGAPG SGKSTLASLA TRCYDVTQGA VRIGGQDVRE LTLDSLRSAI GLVPEDAVLF
     SGTIGANIAY GRPDATPEQI ATAARAAHIE EFVNTLPDGY QTAVGARGLT LSGGQRQRIA
     LARALLHQPR LLIMDDPTSA VDAVIECGIQ EVLREAIADR TAVIFTRRRS MLTLADRVAV
     LDSGRLLDVG TPDEVWERCP RYRELLSPAP DLADDLVVAE RSPVCRPVAG LGTKAAQHTN
     VHNPGPHDHP PGPDPLRRLL REFRGPLALS LLLVAVQTCA GLLPPLLIRH GIDVGIRRHV
     LSALWWAALA GTATVVIRWV VQWGSAMVAG YTGEQVLFRL RSVVFAHAQR LGLDAFEDDG
     DAQIVTAVTA DVEAIVAFLR TGLVVAVISV VTLVGILVAL LAIRARLVLL IFTTMPVLAL
     ATWQFRRASN WTYRRARHRL GTVTATLREY AAGLRIAQAF RAEYRGLQSY FAHSDDYRRL
     GVRGQRLLAL YYPFVALLCS LATTLVLLDG AREVRAGVIS VGALVTYLLY IELLYTPIGE
     LAQMFDDYQR AAVAAGRIRS LLSTRTPSSP AARPVGTLRG EVVFDAVHYS YRTREVPALA
     GINLRIPAGQ TVVFVGSTGS GKSTLIKLVA RFYDPTHGTV RVDGCDLREF DVDGYRNRLG
     IVTQEQYVFA GTVRDAIAYG RPDATDAQVE RAAREVGAHP MITALDNGYL HQVTAGGRNL
     SAGQLQLLAL ARARLVDPDI LLLDEATVAL DPATEAVVQR ATLTLAARRT TLIVAHGLAI
     AEHADRIVVL EHGTVVEDGA HTELLAAGGH YSRLWAAHTR LCSPEITQLQ CIDA
 
 
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