ATRB_EMENI
ID ATRB_EMENI Reviewed; 1425 AA.
AC A0A1U8QKX8; C8VEK3; Q5AT91;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 1.
DT 03-AUG-2022, entry version 22.
DE RecName: Full=ABC multidrug transporter atrB;
GN Name=atrB {ECO:0000303|PubMed:9180695}; ORFNames=AN8489.2;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [3]
RP FUNCTION, INDUCTION, AND CATALYTIC ACTIVITY.
RX PubMed=9180695; DOI=10.1007/s004380050434;
RA Del Sorbo G., Andrade A.C., Van Nistelrooy J.G., Van Kan J.A., Balzi E.,
RA De Waard M.A.;
RT "Multidrug resistance in Aspergillus nidulans involves novel ATP-binding
RT cassette transporters.";
RL Mol. Gen. Genet. 254:417-426(1997).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND CATALYTIC ACTIVITY.
RX PubMed=10931903; DOI=10.1099/00221287-146-8-1987;
RA Andrade A.C., Del Sorbo G., Van Nistelrooy J.G.M., Waard M.A.;
RT "The ABC transporter AtrB from Aspergillus nidulans mediates resistance to
RT all major classes of fungicides and some natural toxic compounds.";
RL Microbiology 146:1987-1997(2000).
RN [5]
RP INDUCTION.
RX PubMed=11872487; DOI=10.1128/aem.68.3.1351-1357.2002;
RA Semighini C.P., Marins M., Goldman M.H., Goldman G.H.;
RT "Quantitative analysis of the relative transcript levels of ABC transporter
RT Atr genes in Aspergillus nidulans by real-time reverse transcription-PCR
RT assay.";
RL Appl. Environ. Microbiol. 68:1351-1357(2002).
CC -!- FUNCTION: Pleiotropic ABC efflux transporter involved in the basal
CC level of drugs susceptibility, including antibiotics, azole fungicides
CC and plant defense toxins (PubMed:9180695). Confers resistance to
CC cycloheximide, chloramphenicol, imazalil, sulfomethuron methyl,
CC pyrimethanil, quintozene, acriflavine, rhodamine 6G, the azoles
CC fenarimol and miconazole, and to the dicarboximides iprodione and
CC vinchlozolin (PubMed:9180695, PubMed:10931903).
CC {ECO:0000269|PubMed:10931903, ECO:0000269|PubMed:9180695}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + cycloheximide(in) + H2O = ADP + cycloheximide(out) +
CC H(+) + phosphate; Xref=Rhea:RHEA:61936, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:27641, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000305|PubMed:9180695};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61937;
CC Evidence={ECO:0000305|PubMed:9180695};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + chloramphenicol(in) + H2O = ADP + chloramphenicol(out) +
CC H(+) + phosphate; Xref=Rhea:RHEA:35287, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17698, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000305|PubMed:9180695};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35288;
CC Evidence={ECO:0000305|PubMed:9180695};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:9180695};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- INDUCTION: Expression is strongly increased in the presence of
CC cycloheximide, imazalil, fenarimol, pisatin, itraconazole and 4-
CC nitroquinoline oxide (4-NQO). {ECO:0000269|PubMed:11872487,
CC ECO:0000269|PubMed:9180695}.
CC -!- DISRUPTION PHENOTYPE: Leads to increased sensitivity to different
CC classes of agricultural fungicides: cyprodinil (anilinopyrimidine),
CC ketoconazole, prochloraz and propiconazole (azoles), carbendazim (a
CC benzimidazole), fenpiclonil and fludioxonil (phenylpyrroles), fluazinam
CC (a phenylpyridianine), azoxystrobin, kresoxim-methyl and
CC trifloxystrobin (strobirulins), 4-nitroquinoline oxide (a mutagenic
CC agent), camptothecin (a plant alkaloid) and the phytoalexin resveratrol
CC (a stilbene). {ECO:0000269|PubMed:10931903}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family.
CC PDR (TC 3.A.1.205) subfamily. {ECO:0000305}.
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DR EMBL; BN001305; CBF80656.1; -; Genomic_DNA.
DR EMBL; AACD01000153; EAA67111.1; -; Genomic_DNA.
DR RefSeq; XP_681758.1; XM_676666.1.
DR AlphaFoldDB; A0A1U8QKX8; -.
DR SMR; A0A1U8QKX8; -.
DR STRING; 227321.Q5AT91; -.
DR EnsemblFungi; CBF80656; CBF80656; ANIA_08489.
DR EnsemblFungi; EAA67111; EAA67111; AN8489.2.
DR GeneID; 2868604; -.
DR KEGG; ani:AN8489.2; -.
DR VEuPathDB; FungiDB:AN8489; -.
DR eggNOG; KOG0065; Eukaryota.
DR HOGENOM; CLU_000604_35_0_1; -.
DR OMA; PWFGWIY; -.
DR OrthoDB; 1022017at2759; -.
DR Proteomes; UP000000560; Chromosome V.
DR Proteomes; UP000005890; Unassembled WGS sequence.
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 CDD; cd03233; ABCG_PDR_domain1; 1.
DR CDD; cd03232; ABCG_PDR_domain2; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR013525; ABC_2_trans.
DR InterPro; IPR029481; ABC_trans_N.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR043926; ABCG_dom.
DR InterPro; IPR034001; ABCG_PDR_1.
DR InterPro; IPR034003; ABCG_PDR_2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010929; PDR_CDR_ABC.
DR Pfam; PF01061; ABC2_membrane; 2.
DR Pfam; PF19055; ABC2_membrane_7; 1.
DR Pfam; PF00005; ABC_tran; 2.
DR Pfam; PF14510; ABC_trans_N; 1.
DR Pfam; PF06422; PDR_CDR; 1.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Glycoprotein; Membrane; Nucleotide-binding;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1425
FT /note="ABC multidrug transporter atrB"
FT /id="PRO_0000449464"
FT TRANSMEM 489..509
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 520..540
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 569..589
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 601..621
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 628..648
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 710..730
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1161..1181
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1205..1225
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1239..1259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1267..1287
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1300..1320
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1395..1415
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 96..351
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 788..1037
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 14..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 743..782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 746..768
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 830..837
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 43
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 390
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 484
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 672
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 790
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1024
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1338
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1425 AA; 158452 MW; CD5AC92A314F5859 CRC64;
MSTLTVGDTA LPRESRETMV SIRDSDSTTT VLGEDSASTT DPNVSRADGW ALMPQVKEQN
EREAESGFKR RELGVTWQNL SVEVVSADAA VQENFLSQFN VPKLARESRN KPPLRTILDN
SHGCVKPGEM LLVLGRPGSG CTTLLKMLAN QRLGYKAVQG DVRYGSMTAK EAEQYRGQIV
MNTEEELFFP SLTVGETMDF ATRLKVPFRL PNGVESPEAY REEYKKFLLQ SMGISHTVDT
KVGNEFIRGV SGGERKRVSI IECLATRASV FCWDNSTRGL DASTALEWTK AIRAMTDVLG
LSTIVTLYQA GNGIYDLFDK VLVLDEGKQI YYGPMTQARP YMEALGFVCR EGSNVADFLT
GVTVPTERKI RSGFEARFPR NADAMLEEYN KSAVKADMIS EYDYPDSEYA KLRTEDFKQA
IAEEKAKQLP KSSPFTVDFM NQVKICVTRQ YQILWGDKAT FIIKQVSTLI QALIAGSLFY
DAPNNSGGLF VKSGALFFSL LYNSLLAMAE VTESFQGRPV LIKHKSFAFF HPAAFCIAQI
AADIPVLIFQ VTIFALPVYF MVGLEMDAGV FFTYWILVFA TTMAMTAVFR ACGAAFKTFD
DASKVSGFLI SALIMYTGYM IRKPEMHPWF VWIYWIDPLA YGFDALLSNE FHGKIIPCVG
TNLVPAGPGY ENATTQSCTG VGGSIPGRNY VTGDDYLASL SYSHGHVWRN FGILWAWWAL
FVVVTIIATS RWKGASENGP SLLIPRESVE KHRQHGHRDE ESQSNEKTST KGKSEGVQDS
SDIDNQLVRN TSVFTWKDLC YTVKTPSGDR QLLDHVYGWV KPGMLGALMG SSGAGKTTLL
DVLAQRKTAG TIQGSVLVDG RPLPVSFQRS AGYCEQLDVH EPYATVREAL EFSALLRQPR
TTPREEKLKY VDVIIDLLEL HDIADTLIGR VGAGLSVEQR KRVTIGVELV SKPSILIFLD
EPTSGLDGQS AYNTVRFLRK LADVGQAVLV TIHQPSAQLF AEFDSLLLLA KGGKMVYFGD
IGDNGSTVKE YFARHGAPCP PNANPAEHMI DVVSGSLSQG RDWHEVWKAS PEHTNAQKEL
DRIISEAASK PPGTVDDGHE FAMPLWQQTV IVTKRTCLAV YRNTDYVNNK LALHIGSALF
NGFSFWKMGA SVGELQLKLF ALFNFIFVAP GAIAQLQPLF IERRDIYDAR EKKSRMYSWV
AFVTGLIVSE LPYLVLCAVL YFVCFYYQTG LPTSSDKAGA VFFVMLLYEG LYTGIGQFIS
AYAPNAVFAT LTNPLVIGTL VSFCGVLVPY GQIQEFWRYW IYWLNPFNYL MGSLLTFTIF
DVDIKCRESE FATFDPPNGS SCIDYLSTYL QGLGVSANLI NPDATSQCQV CQYTRGSDYL
YSLNLKDYYY GWRDTAIVAL FVLSSYALVY GLMKLRTKAS KKAEE
