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
