ID   GPY2_GIBF5              Reviewed;        1432 AA.
AC   S0ELQ3;
DT   10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT   18-SEP-2013, sequence version 1.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=ABC transporter GPY2 {ECO:0000303|PubMed:27856636};
DE   AltName: Full=Gibepyrone A biosynthetic cluster protein 2 {ECO:0000303|PubMed:27856636};
GN   Name=GPY2 {ECO:0000303|PubMed:27856636}; ORFNames=FFUJ_12021;
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, DISRUPTION PHENOTYPE, AND INDUCTION.
RX   PubMed=27856636; DOI=10.1074/jbc.m116.753053;
RA   Janevska S., Arndt B., Niehaus E.M., Burkhardt I., Roesler S.M.,
RA   Brock N.L., Humpf H.U., Dickschat J.S., Tudzynski B.;
RT   "Gibepyrone biosynthesis in the rice pathogen Fusarium fujikuroi is
RT   facilitated by a small polyketide synthase gene cluster.";
RL   J. Biol. Chem. 291:27403-27420(2016).
CC   -!- FUNCTION: ABC transporter; part of the gene cluster that mediates the
CC       biosynthesis of gibepyrone A, a 2H-pyran-2-one metabolite exhibiting a
CC       moderate antimicrobial activity against Gram-positive bacteria and
CC       yeasts (PubMed:27856636). GPY2 seems to have a minor impact on the
CC       efflux of gibepyrone A out of the cell, but it was shown to repress
CC       expression of the key gene GPY1 (PubMed:27856636).
CC       {ECO:0000269|PubMed:27856636}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- INDUCTION: Members of the velvet complex, VEL1, VEL2, and LAE1,
CC       negatively affect GPY2 gene expression and gibepyrone A product
CC       formation, whereas SGE1 represents a positive regulator of gibepyrone
CC       biosynthesis. {ECO:0000269|PubMed:27856636}.
CC   -!- DISRUPTION PHENOTYPE: Results in a significantly enhanced level of
CC       extracellular gibepyrone A. {ECO:0000269|PubMed:27856636}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC family.
CC       Conjugate transporter (TC 3.A.1.208) subfamily. {ECO:0000305}.
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DR   EMBL; HF679033; CCT75968.1; -; Genomic_DNA.
DR   AlphaFoldDB; S0ELQ3; -.
DR   SMR; S0ELQ3; -.
DR   STRING; 1279085.S0ELQ3; -.
DR   EnsemblFungi; CCT75968; CCT75968; FFUJ_12021.
DR   VEuPathDB; FungiDB:FFUJ_12021; -.
DR   HOGENOM; CLU_000604_27_5_1; -.
DR   Proteomes; UP000016800; Chromosome 11.
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; cd18580; ABC_6TM_ABCC_D2; 1.
DR   Gene3D; 1.20.1560.10; -; 2.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR011527; ABC1_TM_dom.
DR   InterPro; IPR036640; ABC1_TM_sf.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR044726; ABCC_6TM_D2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00664; ABC_membrane; 2.
DR   Pfam; PF00005; ABC_tran; 2.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   SUPFAM; SSF90123; SSF90123; 2.
DR   PROSITE; PS50929; ABC_TM1F; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cell membrane; Glycoprotein; Membrane; Nucleotide-binding;
KW   Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..1432
FT                   /note="ABC transporter GPY2"
FT                   /id="PRO_0000445365"
FT   TRANSMEM        30..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        60..80
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        100..120
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        160..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        266..286
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        306..326
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   TRANSMEM        376..398
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   TRANSMEM        403..425
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   TRANSMEM        487..507
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   TRANSMEM        519..539
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   TRANSMEM        877..897
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   TRANSMEM        924..944
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   TRANSMEM        997..1017
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   TRANSMEM        1021..1041
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   TRANSMEM        1107..1127
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   TRANSMEM        1136..1156
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   DOMAIN          279..550
FT                   /note="ABC transmembrane type-1 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          601..829
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   DOMAIN          882..1161
FT                   /note="ABC transmembrane type-1 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          1197..1428
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         635..642
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         1231..1238
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   CARBOHYD        605
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        677
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        1130
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        1216
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   1432 AA;  157247 MW;  9ED388E3AEEFFE44 CRC64;
     MPPPNCLLHV EDTFGPVVKG CGSNFDFTLL FEETILCILP LCVAICLAIF RVTRLWKKPV
     IFKGCFILPL KLIAWNLVLG SQASVVALFS IRDETRTRAS IAAGSIGIVG SAILACLSFL
     EHQRAVRTSS ILVLYLLSTI PMDAARARTL WRMLDGRDPA IAVMVLGATK VCALVTEMLW
     KCSLANRHEL CDAPEESNGI IERALMLRMM PIFWAGYRTP LQTEHLSKLD TKLQNAELRP
     SEKGPKRKQA PIKLAKEIFF SHTYEFLAPI FPRLCYLSLT FAQPFLVRRA IDYISKPKTE
     GSGERGDGLI AAYALVYYGI AFVSSLYEQS AVRATTVVRA DLSMRIYQQS LLLDRVVDTG
     DSSTTMMTAD VERVQLGVRK LHDAWASFVS VAIGLWLIEA QLGLAALVTL GLIGGSLLLG
     GYWSGRASRF QKNWMAAIEK RLHKTVQVLK GIKSIKQMGA APAIKTMLED ERQSEIKLSK
     KFRLQLIALV TLSFTSLTML PALGLSVHNA VSDKSSGRIL TAQTAFQVMT LFNIVSSSIQ
     DCTSHVMAIM VGLGSLQRIE SFLNQHTWTD PRKSIRDASI STDESSVGGT SEKKVLTDVA
     VKIQNVSAKW TEDGEAIIRD ATFDVPAHGL TVVAGPTGSG KSTLLRVVLG DLAPSSGTVS
     VDDSQVAFCD QTPWIANISI KENIVGALPF YEERYRMALH ACALDQDIED LTDGDKHLCG
     LNGQSVSGGQ KVRIALARAI YSKATLVLLD DCLVGLDTNT ERHILGEIFA PRGLLSSAPT
     TTILATSSPR YLPFANYIIL IDADGRIVRQ GTYAEIAPHI EQLEHDVLQV SDHAATAREP
     RAQDSDELPN TAITNDIAFK KGANGDWAVY KWYFGVIGWM DFVVFLFLCL GFVIGVIFPQ
     IYLGLWSEKS LQNQIDTLPS FYGIFFGVGS MAWVALFSAC VWLFLRIAVR TAALFHHLIL
     TTTLNARMDF FSQTDSGVTL NRFSQDLQIT DMELPLAFVG ATMNLLMLIA QCIVVTIQSH
     YAGFAILAIA VVIGFFHEFY LRTSRRLRVM DIEARSPVLS LLLESLDGLA TVRAYGWAAW
     YLRRGIEVLE RSQVPFHFLQ SAQVTLNLSV DLFVATLALV VISIAVVQMN TSGGSLGLAL
     FNIVGLGQSV KGVVFFWTSL EITLGAVARI RDFTEDTKSE HESDTKPPVE WPSRGEIHFS
     DVTLTHSTSL PPTISNLTLD IKPGSKMAIC GRTGSGKSTL VNSLLGLVQV SSGIITIDDV
     DISTLAKDEV RSRFVVLPQE SLILSVSIRE YAKLFGISDE QEIIQGLKKT GLWQTIEQGG
     GLDMIASSDT FSHGERQLFA MTLACLKKGK LVLMDEPTSH VDNDIQTQLR QAVFDTFPDS
     TVLCVTHQVA TIVDFDIVLV LDDGKIVEQG DPKELLHQPT SRFAQLYSAG EL