MDREP_MYCBP
ID MDREP_MYCBP Reviewed; 1194 AA.
AC A1KF14;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Multidrug efflux ATP-binding/permease protein BCG_0231 {ECO:0000305};
DE EC=7.6.2.- {ECO:0000305};
GN OrderedLocusNames=BCG_0231 {ECO:0000312|EMBL:CAL70215.1};
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 IN ANTIBIOTIC RESISTANCE.
RC STRAIN=BCG / Pasteur 1173P2;
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).
CC -!- FUNCTION: Overexpression increases resistance to chloramphenicol,
CC ampicillin, streptomycin, tetracyclin and vancomycin.
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; AM408590; CAL70215.1; -; Genomic_DNA.
DR RefSeq; WP_011799083.1; NC_008769.1.
DR AlphaFoldDB; A1KF14; -.
DR SMR; A1KF14; -.
DR PRIDE; A1KF14; -.
DR KEGG; mbb:BCG_0231; -.
DR HOGENOM; CLU_000604_17_6_11; -.
DR OMA; RSDANFW; -.
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:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
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; Repeat; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1194
FT /note="Multidrug efflux ATP-binding/permease protein
FT BCG_0231"
FT /id="PRO_0000432860"
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; 129267 MW; 5ADF4BA136C2CFB4 CRC64;
MRTNCWWRLS GYVMRHRRDL LLGFGAALAG TVIAVLVPLV TKRVIDDAIA ADHRPLAPWA
VVLVAAAGAT YLLTYVRRYY GGRIAHLVQH DLRMDAFQAL LRWDGRQQDR WSSGQLIVRT
TNDLQLVQAL LFDVPNVLRH VLTLLLGVAV MTWLSVPLAL LAVLLVPVIG LIAHRSRRLL
AAATHCAQEH KAAVTGVVDA AVCGIRVVKA FGQEERETVK LVMASRALYA AQLRVARLNA
HFGPLLQTLP ALGQMAVFAL GGWMAAQGSI TVGTFVAFWA CLTLLARPAC DLAGMLTIAQ
QARAGAVRVL ELIDSRPTLV DGTKPLSLEA 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
