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BFOC_ASPBC
ID   BFOC_ASPBC              Reviewed;         561 AA.
AC   A0A1L9UQW4;
DT   26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2017, sequence version 1.
DT   25-MAY-2022, entry version 21.
DE   RecName: Full=Efflux pump bfoC {ECO:0000303|PubMed:31067027};
DE   AltName: Full=Bifonsecin B biosynthesis cluster protein C {ECO:0000303|PubMed:31067027};
GN   Name=bfoC {ECO:0000303|PubMed:31067027}; ORFNames=ASPBRDRAFT_39216;
OS   Aspergillus brasiliensis (strain CBS 101740 / IMI 381727 / IBT 21946).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=767769;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 101740 / IMI 381727 / IBT 21946;
RX   PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA   de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA   Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA   Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA   Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA   Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA   Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA   Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA   Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA   Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA   Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA   Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA   Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA   Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA   Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA   Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA   Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA   van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA   Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA   Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA   Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA   Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT   "Comparative genomics reveals high biological diversity and specific
RT   adaptations in the industrially and medically important fungal genus
RT   Aspergillus.";
RL   Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
RN   [2]
RP   FUNCTION.
RX   PubMed=31067027; DOI=10.1021/acs.biochem.9b00291;
RA   Obermaier S., Mueller M.;
RT   "Biaryl-forming enzymes from Aspergilli exhibit substrate-dependent
RT   stereoselectivity.";
RL   Biochemistry 58:2589-2593(2019).
CC   -!- FUNCTION: Efflux pump; part of the gene cluster that mediates the
CC       biosynthesis of bifonsecin B, a dimeric gamma-naphthopyrone.
CC       {ECO:0000305|PubMed:31067027}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. TCR/Tet
CC       family. {ECO:0000305}.
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DR   EMBL; KV878681; OJJ74128.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1L9UQW4; -.
DR   SMR; A0A1L9UQW4; -.
DR   EnsemblFungi; OJJ74128; OJJ74128; ASPBRDRAFT_39216.
DR   VEuPathDB; FungiDB:ASPBRDRAFT_39216; -.
DR   OrthoDB; 627633at2759; -.
DR   Proteomes; UP000184499; 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:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR   Gene3D; 1.20.1250.20; -; 1.
DR   InterPro; IPR011701; MFS.
DR   InterPro; IPR020846; MFS_dom.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   InterPro; IPR005829; Sugar_transporter_CS.
DR   Pfam; PF07690; MFS_1; 1.
DR   SUPFAM; SSF103473; SSF103473; 1.
DR   PROSITE; PS50850; MFS; 1.
DR   PROSITE; PS00217; SUGAR_TRANSPORT_2; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..561
FT                   /note="Efflux pump bfoC"
FT                   /id="PRO_0000448929"
FT   TRANSMEM        59..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        103..123
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        128..148
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        164..184
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        194..214
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        222..242
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        257..277
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        293..313
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        335..355
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        378..398
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        425..445
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        457..477
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        530..550
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..34
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        35..55
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   561 AA;  59867 MW;  FB5FE9182BB91923 CRC64;
     MSDTARILGG PSASSSRDGG MELNSFTEVS QTNSRSHSTK EEEGQVDDQQ RPAREEETGV
     LGGYKLVLVT IGLCFCIFCT SLDNTIVATA VPRITQQFHS LDDVGWYASA YLLTTCAVTL
     TFGRLYTFFP IKWVYLSALL IFELGSFICG ITPSSLGLIL GRAVAGLGGG GLLSGSLLII
     SQCVPSARRP AFSGFIMSIF AVASVIAPLM GGAFTDHVSW RWCFYINLPF GLVSAVVILF
     TFQHTKPVIQ ASLREKAVGL DPLGTATFLP GIVCLLLATQ WGGAQYPWGD GRVVALFVLF
     GVLLVCFIGL QLWARERATV PPRLLRGRNI WGSALYGFCL NGAMFTFVYY LPIWFQAVQG
     ASATESGIRN LPLVISNVVF AIISGVLVSM TGYLGPFMLL SAAMASISAG LLSTLQPSSG
     AGEWIGYQVL LGLSIGVGFQ VPIFVVQTTL ASTDIPTATA LMTFIQLLGG AIFVSVAQNM
     FRNQLATDIR TVLPMLDPTA VINAGPTSLR GMYSGETLTT LVALYNDAVV HTFYLAIGLA
     AASFLAATVI QWRPLAKAVG E
 
 
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