ATRG_ASPOR
ID ATRG_ASPOR Reviewed; 1494 AA.
AC Q2U0M6;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=ABC multidrug transporter atrG;
GN Name=atrG {ECO:0000303|PubMed:30011258}; ORFNames=AO090011000378;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
RN [2]
RP FUNCTION, INDUCTION, DISRUPTION PHENOTYPE, AND CATALYTIC ACTIVITY.
RX PubMed=30011258; DOI=10.1080/09168451.2018.1497941;
RA Miura D., Sugiyama K., Ito A., Ohba-Tanaka A., Tanaka M., Shintani T.,
RA Gomi K.;
RT "The PDR-type ABC transporters AtrA and AtrG are involved in azole drug
RT resistance in Aspergillus oryzae.";
RL Biosci. Biotechnol. Biochem. 82:1840-1848(2018).
CC -!- FUNCTION: Pleiotropic ABC efflux transporter involved in the basal
CC level of azole susceptibility (PubMed:30011258). Confers resistance to
CC miconazole and clotrimazole (PubMed:30011258).
CC {ECO:0000269|PubMed:30011258}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-miconazole(in) + ATP + H2O = (R)-miconazole(out) + ADP +
CC H(+) + phosphate; Xref=Rhea:RHEA:61928, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:82894, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000305|PubMed:30011258};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61929;
CC Evidence={ECO:0000305|PubMed:30011258};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:30011258};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- INDUCTION: Expression is highly up-regulated in azole resistant strains
CC and in the presence of miconazole. {ECO:0000269|PubMed:30011258}.
CC -!- DISRUPTION PHENOTYPE: Leads to strong miconazole susceptibility.
CC {ECO:0000269|PubMed:30011258}.
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; AP007171; BAE64889.1; -; Genomic_DNA.
DR RefSeq; XP_001826022.1; XM_001825970.2.
DR AlphaFoldDB; Q2U0M6; -.
DR SMR; Q2U0M6; -.
DR STRING; 510516.Q2U0M6; -.
DR EnsemblFungi; BAE64889; BAE64889; AO090011000378.
DR GeneID; 5998125; -.
DR KEGG; aor:AO090011000378; -.
DR VEuPathDB; FungiDB:AO090011000378; -.
DR HOGENOM; CLU_000604_35_0_1; -.
DR OMA; IAEATLC; -.
DR Proteomes; UP000006564; Chromosome 7.
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; 2.
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..1494
FT /note="ABC multidrug transporter atrG"
FT /id="PRO_0000449470"
FT TRANSMEM 527..547
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 561..581
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 636..656
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 669..689
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 778..798
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1191..1211
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1227..1247
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1276..1296
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1312..1332
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1351..1371
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1463..1483
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 162..416
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 852..1095
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 84..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 888..895
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 41
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 340
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 622
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 835
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1410
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1432
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1494 AA; 167380 MW; 8F8395C4580F0589 CRC64;
MSLLGTINPN LNPARAVGAQ GDAEGAAPVS GGEPMPIFEG NDSARTSDTA LDKLGKDESK
YDEQIAEAEV TRLAQQLTRQ STRFSVSQNA ENPFLETKED STLNPLGPNF KAKNWMKNLL
ALTSRDPERH PRREAGVSFR NLSVHGYGSP TDYQKDVFNM VLQVGALFRA VTGTGKQKIQ
ILRDFDGLVK SGEMLVVLGR PGSGCSTFLK TLAGEMNGIY MDDKSDLNYQ GIPAKQMRRQ
FRGEAIYNAE TDVHFPQLSV GDTLKFAALT RCPRNRFPGV SREQYATHMR DVVMAMLGLT
HTINTRVGND FVRGVSGGER KRVSIAEATL SGSPLQCWDN STRGLDSANA LEFCKTLNLM
TKYAGATVAV AIYQASQSAY DVFDKVTVLY EGRQIYFGRT DEAKEFFTTM GFECPERQTT
ADFLTSLTSP SERIVKKGYE GKVPRTPDEF AAAWKNSEAY AKLIREIEEY NREFPLGGES
VQKFVESRRA MQAKNQRVGS PYTVSIYEQV RLCMIRGFQR LKGDSSLTMS QLIGNFIMAL
IIGSVFYNLQ HDTSSFYSRG ALLFFAVLLN AFSSALEILT LYAQRPIVEK QARYAMYHPF
AEAIASMLCD MPYKITNAII FNITLYFMTN LRREPGPFFV FLLFTFVTTM TMSMLFRTIA
ASSRTLSQAL VPAAILILGL VIYTGFTIPT RNMLGWSRWM NYLDPIAYGF ESLMVNEFHN
TKWKCSSAEL IPNYEGASLA NKICSTVGAV AGSEYVYGDD YLEQSFQYYE SHKWRNLGIM
FAFMVFFLAT YLTATEYISE AKSKGEVLLF RRGHYSRGAA DVETHNEVSA TEKTNESSDG
AGAAIQRQEA IFHWQDVCYD IKIKGEPRRI LDHVDGWVKP GTCTALMGVS GAGKTTLLDV
LATRVTMGVV TGEMLVDGRL RDQSFQRKTG YVQQQDLHLH TTTVREALRF SAILRQPAHV
SRQEKLDYVE EVIKLLGMEA YADAVVGVPG EGLNVEQRKR LTIGVELAAK PQLLLFLDEP
TSGLDSQTSW SILDLIDTLT KHGQAILCTI HQPSAMLFQR FDRLLFLAKG GKTVYFGEIG
ERSSTLASYF ERNGAPKLPV EANPAEWMLE VIGAAPGSHS DIDWPAVWRE SPEREAVRNH
LAELKSTLSQ KSVDSSHSDE SSFKEFAAPF SVQLYECLVR VFSQYWRTPV YIYSKAVLCI
LTSLYIGFSF FHAENSRQGL QNQMFSIFML MTIFGNLVQQ IMPNFVTQRA LYEARERPSK
AYSWKAFMTA NILVELPWNA LMSVIIFVCW YYPIGLYRNA EPTDSVHERG ALMWLLILSF
LLFTSTFAHM MIAGIELAET GGNLANLLFS LCLIFCGVLA TPETLPGFWI FMYRVSPFTY
LVSGMLATGV GRTTAVCEKV EFLHLTPPAN TTCYDYMSDY IGSFGGYLEN DNATDSCSFC
QISSTDTFLS AVSSYYEDRW RNFGIMWAFI VFNIAAAVFI YWLARVPKGS RSKN
