ID   EF102_EPIFF             Reviewed;         479 AA.
AC   Q4H425;
DT   23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 1.
DT   25-MAY-2022, entry version 32.
DE   RecName: Full=MFS-type transporter EF102 {ECO:0000303|PubMed:16091042};
DE   AltName: Full=Peramine biosynthesis cluster protein EF102 {ECO:0000303|PubMed:16091042};
GN   Name=EF102 {ECO:0000303|PubMed:16091042};
OS   Epichloe festucae (strain Fl1).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Epichloe.
OX   NCBI_TaxID=877507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=Fl1;
RX   PubMed=16091042; DOI=10.1111/j.1365-2958.2005.04747.x;
RA   Tanaka A., Tapper B.A., Popay A., Parker E.J., Scott B.;
RT   "A symbiosis expressed non-ribosomal peptide synthetase from a mutualistic
RT   fungal endophyte of perennial ryegrass confers protection to the symbiotum
RT   from insect herbivory.";
RL   Mol. Microbiol. 57:1036-1050(2005).
RN   [2]
RP   INDUCTION.
RX   PubMed=20519633; DOI=10.1104/pp.110.158451;
RA   Eaton C.J., Cox M.P., Ambrose B., Becker M., Hesse U., Schardl C.L.,
RA   Scott B.;
RT   "Disruption of signaling in a fungal-grass symbiosis leads to
RT   pathogenesis.";
RL   Plant Physiol. 153:1780-1794(2010).
CC   -!- FUNCTION: MFS-type transporter; part of the gene cluster that mediates
CC       the biosynthesis of peramine, a pyrrolopyrazine synthesized in
CC       association with the grass host that protects the plant from insect
CC       herbivory (PubMed:16091042). Probably involved in peramine transport
CC       (PubMed:16091042). {ECO:0000269|PubMed:16091042}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- INDUCTION: Expression is down-regulated when the stress-activated
CC       mitogen-activated protein kinase (sakA) is deleted (PubMed:20519633).
CC       {ECO:0000269|PubMed:20519633}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC       {ECO:0000305}.
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DR   EMBL; AB205145; BAE06844.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q4H425; -.
DR   SMR; Q4H425; -.
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; -; 2.
DR   InterPro; IPR011701; MFS.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   Pfam; PF07690; MFS_1; 1.
DR   SUPFAM; SSF103473; SSF103473; 1.
PE   2: Evidence at transcript level;
KW   Membrane; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..479
FT                   /note="MFS-type transporter EF102"
FT                   /id="PRO_0000444312"
FT   TRANSMEM        55..75
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        95..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        121..141
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        149..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        184..204
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        218..238
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        268..288
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        305..325
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        331..351
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        363..383
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        399..419
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        433..453
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   479 AA;  51457 MW;  FEF9AEDD2F8A0F77 CRC64;
     MSGHGDKDRD RKLGSQHSTL HERGFGGNGA VDAEQESSMS DNEQPTEYRT YRRRWIGLLT
     LTLMNVVVSW DWLTFAPVAD LSATYYGVSK LAINWVSIAF FLAFVAVFPI TIAILHRGPK
     LAFMIAAVLI IIGNWVRYAG SASSTGGRYG AIMAGEIIIG FAQPFILAAP TRYSDMWFTN
     RGRVAATALT SLANPLGGAL GQLINPRWAK QSADISNMVL YVSIISTVCS LPAFVVPAAP
     PTPVGPAAET PKLSLKESLK VLTHSIELWL VLIPFFVYVG FFNSISSLLN QIMIPYGFSD
     DEAGIGGAIL ILVGLLFSAV TSPIIDRTKK FLLALKLFMP VIGICYLTFV WMPETRNVAG
     PYAVLAVLGA ASFALVPIAL EFLTELGHPL SPEVTSTTAW AGGQLLGAIF VIISGALTAG
     DDGNPPQNMN RALVFQAVVA LLVCPLPLFL GLFGRGDKII LKRVRSDTRG VPSGVRIIA