ABCI_ASPFU
ID ABCI_ASPFU Reviewed; 1485 AA.
AC Q4WUS1;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=ABC multidrug transporter I {ECO:0000303|PubMed:32209680};
GN Name=abcI {ECO:0000303|PubMed:32209680}; ORFNames=AFUA_5G09460;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION,
RP AND INDUCTION.
RX PubMed=32209680; DOI=10.1128/mbio.00338-20;
RA Esquivel B.D., Rybak J.M., Barker K.S., Fortwendel J.R., Rogers P.D.,
RA White T.C.;
RT "Characterization of the efflux capability and substrate specificity of
RT Aspergillus fumigatus PDR5-like ABC transporters expressed in Saccharomyces
RT cerevisiae.";
RL MBio 11:0-0(2020).
CC -!- FUNCTION: ABC efflux transporter that confers resistance to fluconazole
CC (FLC) but shows no resistance to other azoles (PubMed:32209680). Is
CC also able to transport rhodamine 6G (R-6G), a known substrate for many
CC ABC transporters (PubMed:32209680). {ECO:0000269|PubMed:32209680}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + fluconazole(in) + H2O = ADP + fluconazole(out) + H(+) +
CC phosphate; Xref=Rhea:RHEA:61916, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:46081, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:32209680};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61917;
CC Evidence={ECO:0000269|PubMed:32209680};
CC -!- ACTIVITY REGULATION: The efflux inhibitor FK506 does not impair the
CC transport activity. {ECO:0000269|PubMed:32209680}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:32209680};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- INDUCTION: Expression is highly induced in a single triazole-resistant
CC isolate (DI16-8). {ECO:0000269|PubMed:32209680}.
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; AAHF01000003; EAL91655.1; -; Genomic_DNA.
DR RefSeq; XP_753693.1; XM_748600.1.
DR AlphaFoldDB; Q4WUS1; -.
DR SMR; Q4WUS1; -.
DR STRING; 330879.Q4WUS1; -.
DR EnsemblFungi; EAL91655; EAL91655; AFUA_5G09460.
DR GeneID; 3511229; -.
DR KEGG; afm:AFUA_5G09460; -.
DR eggNOG; KOG0065; Eukaryota.
DR HOGENOM; CLU_000604_35_0_1; -.
DR InParanoid; Q4WUS1; -.
DR OMA; GCTDPFE; -.
DR OrthoDB; 324553at2759; -.
DR Proteomes; UP000002530; Chromosome 5.
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..1485
FT /note="ABC multidrug transporter I"
FT /id="PRO_0000452662"
FT TRANSMEM 522..542
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 556..576
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 600..620
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 623..643
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 664..684
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 691..711
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 774..794
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1184..1204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1211..1231
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1268..1288
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1299..1319
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1325..1345
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1449..1469
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 163..411
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 846..1089
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 75..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 882..889
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 12
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 132
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 335
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 451
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1396
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1418
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1485 AA; 167186 MW; 5312078A9E391675 CRC64;
MDEKPAVSES SNGSDVDSLS TASAYEQHRE RLRDANPQGV TSHRSGVNVK EAEEEFSELN
RQFSTISHQA HCLSKQISRA SKPTGKTEDV ERSDSPADSD EPWDLETALR GNRDAETAAG
IRSKRIGVIW DNLTVRGMGG VKTYIKTFPD AIIDFFNVPE TIMHMLGYGK KGKEFEILRN
FRGVLQPGEM VLVLGRPGSG CTTFLKTITN QRFGYTSIDG DVLYGIFDAD TFAKRFRGEA
VYNQEDDVHQ PTLTVKQTLG FALDTKTPGK RPLGVSKAEF REKVINMLLK MFNIEHTANT
VIGNQFIRGV SGGERRRVSI AEMMITSATV LAWDNSTRGL DASTALDFAK SLRIMTNIYK
TTTFVSLYQA SENIYKQFDK VLVIDSGRQV FFGPASEARS YFESLGFKER PRQTTPDYLT
GCTDPFEREF KEGRSEDDVP STPDSLVEAF NRSSYSERLA QEMDAYRKKL EQEKHVYEDF
EIANQEAKRK FTPKSSVYSI PFHLQIWALM QRQFLIKWQD RFAQTVSWIT STGVAIILGT
VWLRLPKTSA GAFTRGGLLF ISLLFNGFQA FSELVSTMMG RSIVNKHRQF TFYRPSALWI
AQILVDTTFA IARILVFSII VYFMCGLVLD AGAFFTFILI IVLGYLCMTC FFRVIGCMSP
DFDYAMKFAS VVITLFVLTS GYLIQWSSEQ EWLRWLYYIN PFGLGFAALM VNEFKDLTMT
CTADSLVPSG PGYDDMASRV CTLAGGEPGS VIIPGASYLA KTFSYFPGDL WRNFGIMVAL
TVGFLTLNLY HGETLQFGAG GRTVTFYQKE NKERRALNGA LMEKRTNRES KDQSAANLKI
TSKSVFTWED VCYDVPVPSG TRRLLQSVYG YVQPGKLTAL MGASGAGKTT LLDVLASRKN
IGVISGNILV DGAPPPGSFL RTVSYAEQLD IHEPMQTVRE ALRFSADLRQ PYETPQSEKY
EYVEGIIQLL ELEDLADAII GTPETGLSVE ERKRVTIGVE LAAKPELLLF LDEPTSGLDS
QSAFNIIRFL RKLAAAGQAI LCTIHQPNSA LFENFDRLLL LQRGGECVYF GDIGEDSHVL
LDYFRRNGAD CPPDANPAEW MLDAIGAGQT RRIGDRDWGE IWRTSSEFEQ VKREIIQIKA
QRAEEVRQSG GSQIIVREYA TPLWHQIKVV CKRTNIVFWR SRNYGFTRLF NHVVIALVTG
LAFLNLDDSR ASLQYRIFVI FNVTVLPAII LQQVEPRFEF SRLVFFRESA CKSYSQFAFA
LSMVIAELPY SILCAVCFFL PLYYIPGFQA APSRAGYQFL MVLITELFSV TLGQMISALT
PNSFIASQIN PPIVIIFSLF CGVAIPRPQM PGFWRAWLYQ LDPFTRLISG MVTTELHGRT
VSCSPSEFNR FQAPENQTCG EYMLPFFERG GLGYLADNTT QACEYCAYKI GDEFYSAFSM
SFNTRWRDLG IFLAFIGSNL IILFLAVSFM SPRCRLRYKL IYDIF
