ID Q0S3H9_RHOJR Unreviewed; 322 AA.
AC Q0S3H9;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 123.
DE SubName: Full=ABC drug resistance transporter, ATP-binding protein {ECO:0000313|EMBL:ABG97907.1};
GN OrderedLocusNames=RHA1_ro06130 {ECO:0000313|EMBL:ABG97907.1};
OS Rhodococcus jostii (strain RHA1).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=101510 {ECO:0000313|EMBL:ABG97907.1, ECO:0000313|Proteomes:UP000008710};
RN [1] {ECO:0000313|Proteomes:UP000008710}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RHA1 {ECO:0000313|Proteomes:UP000008710};
RX PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA Eltis L.D.;
RT "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT catabolic powerhouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000431; ABG97907.1; -; Genomic_DNA.
DR RefSeq; WP_011598157.1; NC_008268.1.
DR AlphaFoldDB; Q0S3H9; -.
DR KEGG; rha:RHA1_ro06130; -.
DR PATRIC; fig|101510.16.peg.6178; -.
DR eggNOG; COG1131; Bacteria.
DR HOGENOM; CLU_000604_1_2_11; -.
DR OrthoDB; 9804819at2; -.
DR Proteomes; UP000008710; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0043215; P:daunorubicin transport; IEA:InterPro.
DR GO; GO:1900753; P:doxorubicin transport; IEA:InterPro.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR005894; DrrA.
DR InterPro; IPR025302; DUF4162.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR01188; drrA; 1.
DR PANTHER; PTHR42711; ABC TRANSPORTER ATP-BINDING PROTEIN; 1.
DR PANTHER; PTHR42711:SF18; DOXORUBICIN RESISTANCE ATP-BINDING PROTEIN DRRA; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR Pfam; PF13732; DUF4162; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 4: Predicted;
KW Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:ABG97907.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000008710};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 8..238
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
SQ SEQUENCE 322 AA; 34366 MW; 59A254E332FDE94A CRC64;
MPAPDTAVLV EGIEKSFGDV AALRGVSFEV PRGTVLGILG PNGAGKTTTV NVLSTLLRPD
AGRAFVAGHD VVEESANVRR SIMMTGQYAA LDESLTGREN LVLFGRLMGL PKASAKSRAQ
DLLSQFDLLE AGDRKVSGYS GGMRRRVDIA CGLVIRPEVV FLDEPTTGLD PRSRQGVWSL
VSALKEQGIT ILLTTQYLEE ADLLSDNIVV IDKGTVIAEG TADELKARTG GSYCEVVPVS
LDDLPRVREI LTSLCPPGRA IEEGTDRLSI PAEHGAQTLA EVLRRLDLAG VTLADIALRR
PSLDDVFLSL TGHVRVDESL PS
//