ATRA_ASPOR
ID ATRA_ASPOR Reviewed; 1483 AA.
AC Q2TXA7;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=ABC multidrug transporter atrA;
GN Name=atrA {ECO:0000303|PubMed:30011258}; ORFNames=AO090010000219;
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 slight 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}.
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; AP007175; BAE66116.1; -; Genomic_DNA.
DR RefSeq; XP_001827249.1; XM_001827197.2.
DR AlphaFoldDB; Q2TXA7; -.
DR SMR; Q2TXA7; -.
DR STRING; 510516.Q2TXA7; -.
DR EnsemblFungi; BAE66116; BAE66116; AO090010000219.
DR GeneID; 5999383; -.
DR KEGG; aor:AO090010000219; -.
DR VEuPathDB; FungiDB:AO090010000219; -.
DR HOGENOM; CLU_000604_35_0_1; -.
DR OMA; YASTFTH; -.
DR Proteomes; UP000006564; Chromosome 8.
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..1483
FT /note="ABC multidrug transporter atrA"
FT /id="PRO_0000449462"
FT TRANSMEM 512..532
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 539..559
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 595..615
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 620..640
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 654..674
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 759..779
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1179..1199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1215..1235
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1254..1274
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1293..1313
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1320..1340
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1444..1464
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 147..398
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 840..1083
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 1..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 876..883
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 718
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 780
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 947
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1413
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1471
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1483 AA; 166735 MW; F601B8AAFD306DB4 CRC64;
MASHKKSEDP LVVKDRQEQE CESSDSTIAS ENASEHRSPM GLIDEDGIET LNRIASQSSR
RRSSVYPPNV PTRTSTLATI SENDPAVDPQ GPSFDLNKWL KMVLRESERQ GREAHRTGIV
FKNFTVSGTG AALQLQDTVS SMLSAPFRIG EMMKNRHSPP KRILNEFNGL LKSGELLLVL
GRPGSGCSTF LKSLCGELHG LSMSKESVIH YDGVPQQRMI KEFKGEVVYN QEVDKHFPHL
TVGQTLEFAA LARTPAQRIR DMSREEFAKH ITQVVMAVFG LSHTYNTKVG NDFVRGVSGG
ERKRVSIAEM ALAHSPLAAW DNSTRGLDSA TALKFVEALR LFADLSGSAH AVAIYQASQS
IYDIFNKVVV LYEGRQIYYG PAKDAKSYFE RQGWECPQRQ TTGDFLTSVT NPSERKARPG
MENQVPRTAE DFEAYWRKSP EYQKLMSEIS HYEQEHPLEE EGDALATFQQ KKREIQAKHT
RPQSPYLLSV PMQIKLNTKR AYQRVWNDIS STVSTVISQI IMALIIGSVF YGTPDATAGF
TAKGATLFFA VLLNALIAMN EINSLYSQRP IVEKHNSYAF YHPATEAIAG VVSDIPVKFV
IAVVFNLILY FLAGLHRSAG QFFLYLLVTF IVMFVMSAVF RTMAAITQTV SQAMGLAGIL
ILALIVYTGF VLPVPSMHPW FEWIHYLNPI YYAFEMLIAN EFHGRDFICS QFIPAYPNLS
GNSFVCSSAG AKAGQRAISG DDYIQVNYQY SYGHVWRNFG ILIAFLVGFM MIYFIATELN
SSTSSTAEVL VFRRGHEPAY LRTDSKKPDA ESAVELSAMK PTTESGEGDM SIIPPQKDIF
TWRDVCYDIE IKGEPRRLLD HVSGWVKPGT LTALMGVSGA GKTTLLDVLA HRTSMGVITG
DMFVNGRGLD QSFQRSTGYV QQQDLHLETA TVRESLRFSA LLRQPPNVSI QEKYDYVEDV
IRMLKMEDFA EAVVGVPGQG LNVEQRKLLT IGVELAAKPK LLLFLDEPTS GLDSQSSWAI
CAFLRRLADS GQAVLCTIHQ PSAILFQQFD QLLFLARGGK TVYFGPIGQN SNTLLNYFES
NGARKCADDE NPAEWMLEIV NAGTNSEGEN WFDVWKRSSE CQGVQTEIDR IHREQQSKTQ
ASDKDNESWS KSEFAMPFWF QLYQVTYRVF QQYWRMPEYI ASKWVLGILS GLFIGFSFFQ
AKSSLQGMQT IVYSLFMLCS IFSSLVQQVM PLFVTQRSLY EVRERPSKTY SWKAFLIANI
IVEIPYQIMM GILTYACYYY AVVGVQDSER QGLVLLLCIQ FFIYASTFAH MAIAAMPDTE
TASAIVVLLF AMSLTFCGVM QTPTALPGFW IFMYRVSPFT YWVSAMAATQ LHDRVVQCSP
SEMSIFDPPS GQTCGEYMSS FMSMAGGQLS NPNATSDCNY CSVAVADDFL SSVNIYWSER
WRNFGLMWVY IVFNIFLATM LYYTFRVKKW NLSGLKERFS KKK
