ID   BIK6_GIBF5              Reviewed;         485 AA.
AC   S0DZN4;
DT   08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT   18-SEP-2013, sequence version 1.
DT   25-MAY-2022, entry version 29.
DE   RecName: Full=Efflux pump bik6 {ECO:0000305};
DE   AltName: Full=Bikaverin biosynthesis protein 6 {ECO:0000303|PubMed:19400779};
GN   Name=bik6 {ECO:0000303|PubMed:19400779}; ORFNames=FFUJ_06747;
OS   Gibberella fujikuroi (strain CBS 195.34 / IMI 58289 / NRRL A-6831) (Bakanae
OS   and foot rot disease fungus) (Fusarium fujikuroi).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium fujikuroi species complex.
OX   NCBI_TaxID=1279085;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 195.34 / IMI 58289 / NRRL A-6831;
RX   PubMed=23825955; DOI=10.1371/journal.ppat.1003475;
RA   Wiemann P., Sieber C.M.K., von Bargen K.W., Studt L., Niehaus E.-M.,
RA   Espino J.J., Huss K., Michielse C.B., Albermann S., Wagner D.,
RA   Bergner S.V., Connolly L.R., Fischer A., Reuter G., Kleigrewe K., Bald T.,
RA   Wingfield B.D., Ophir R., Freeman S., Hippler M., Smith K.M., Brown D.W.,
RA   Proctor R.H., Muensterkoetter M., Freitag M., Humpf H.-U., Gueldener U.,
RA   Tudzynski B.;
RT   "Deciphering the cryptic genome: genome-wide analyses of the rice pathogen
RT   Fusarium fujikuroi reveal complex regulation of secondary metabolism and
RT   novel metabolites.";
RL   PLoS Pathog. 9:E1003475-E1003475(2013).
RN   [2]
RP   FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=19400779; DOI=10.1111/j.1365-2958.2009.06695.x;
RA   Wiemann P., Willmann A., Straeten M., Kleigrewe K., Beyer M., Humpf H.U.,
RA   Tudzynski B.;
RT   "Biosynthesis of the red pigment bikaverin in Fusarium fujikuroi: genes,
RT   their function and regulation.";
RL   Mol. Microbiol. 72:931-946(2009).
CC   -!- FUNCTION: Efflux pump; part of the gene cluster that mediates the
CC       biosynthesis of bikaverin, a red pigment also considered as a mycotoxin
CC       (PubMed:19400779). {ECO:0000269|PubMed:19400779}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- INDUCTION: Expression is repressed by glutamine and at alkaline ambient
CC       pH and highly induced under nitrogen starvation and acidic pH
CC       conditions (PubMed:19400779). {ECO:0000269|PubMed:19400779}.
CC   -!- DISRUPTION PHENOTYPE: Leads to decreased production of bikaverin
CC       (PubMed:19400779). {ECO:0000269|PubMed:19400779}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC       {ECO:0000255}.
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; HF679027; CCT67996.1; -; Genomic_DNA.
DR   AlphaFoldDB; S0DZN4; -.
DR   SMR; S0DZN4; -.
DR   EnsemblFungi; CCT67996; CCT67996; FFUJ_06747.
DR   VEuPathDB; FungiDB:FFUJ_06747; -.
DR   HOGENOM; CLU_008455_11_4_1; -.
DR   Proteomes; UP000016800; Chromosome 5.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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   Pfam; PF07690; MFS_1; 1.
DR   SUPFAM; SSF103473; SSF103473; 1.
DR   PROSITE; PS50850; MFS; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..485
FT                   /note="Efflux pump bik6"
FT                   /id="PRO_0000436343"
FT   TRANSMEM        42..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        86..106
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        108..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        139..159
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        172..192
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        199..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        269..289
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        306..326
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        353..373
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        379..399
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        417..437
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        447..467
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        241
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   485 AA;  53583 MW;  90D34E9650FDD47F CRC64;
     MNEESNMGGV FKEEEAQSGD VVDFEGDSDT HNPQNWPMGK KVYTTALWAL TTCWITFASA
     IYSAGTAEIS EEFHVSYEVA NAGTSLLIFG FALGPMLWAP LCEVYGRKWP ALAPYFISAA
     FAFGTATAKD IQTILITRFF AGVFGSSPIS ITGGSIVDIW TPRQRGTPMV CYGITIAAAP
     TLGPIIGGAF IASGCGWRWT EYLTGIVMMV QFVLDALWLD ESHADVLLTR KASRLRRSTG
     NFSLHAKWEE TSPTFKSLLS TYLVRPFQML LDPICLLLTI YTSFVYAILY ASLESFALEY
     GRFRRWGPVV SQLPFLSLLI GCLFAAAANI FNNIYYGKKL VANNFKPVPE ARLPPMMVGG
     FAFSAGLFLF GWTSVEHVSS PWPSIIGVFL TGVGFTTIFQ SSLQYLVDTF TRYSASAIAA
     NTFVRSMAAG AFPLFVWPMY EKIGIDWGST IFACISVLLL PAPFLFFKWG YRIRARGEFS
     KLSTY