ID   FFSH_ASPFV              Reviewed;         564 AA.
AC   A0A7L8UVD5;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   07-APR-2021, sequence version 1.
DT   03-AUG-2022, entry version 5.
DE   RecName: Full=MFS-type efflux transporter ffsH {ECO:0000303|PubMed:32913332};
DE   AltName: Full=Cytochalasans biosynthesis cluster protein ffsH {ECO:0000303|PubMed:32913332};
GN   Name=ffsH {ECO:0000303|PubMed:32913332};
OS   Aspergillus flavipes.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=41900;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=CNL-338;
RX   PubMed=32913332; DOI=10.1038/s41429-020-00368-0;
RA   Heard S.C., Wu G., Winter J.M.;
RT   "Discovery and characterization of a cytochalasan biosynthetic cluster from
RT   the marine-derived fungus Aspergillus flavipes CNL-338.";
RL   J. Antibiot. 73:803-807(2020).
CC   -!- FUNCTION: MFS-type efflux transporter; part of the gene cluster that
CC       mediates the biosynthesis of the cytotoxic leucine-containing
CC       cytochalasans, including aspochalasin C, aspochalasin E, TMC-169,
CC       flavichalasine F, aspergillin PZ, aspochalasin M and flavichalasine G
CC       (PubMed:32913332). FfsH might be involved in the excretion of
CC       cytochalasans (Probable). {ECO:0000269|PubMed:32913332,
CC       ECO:0000305|PubMed:32913332}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC       {ECO:0000305}.
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DR   EMBL; MT586757; QOG08945.1; -; Genomic_DNA.
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; -; 2.
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   3: Inferred from homology;
KW   Cell membrane; Glycoprotein; Membrane; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..564
FT                   /note="MFS-type efflux transporter ffsH"
FT                   /id="PRO_0000454528"
FT   TRANSMEM        43..63
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        98..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        131..151
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        157..177
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        187..207
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        226..246
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        254..274
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        300..320
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        334..354
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        362..382
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        389..409
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        427..447
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        502..522
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          540..564
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..22
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        540..555
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        182
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        553
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   564 AA;  61169 MW;  31F94274180C6950 CRC64;
     MSEAEKKASQ DAQHKEPMAD SETQLDSDSA PSSQAEKPAK TKYPLSFWLA FGALCLTGLI
     SAMEGSIVST SLPSIIAELK AAFQPLYGQL ADLWGRRYVM ILATAIFLLG SGICGGANSM
     DMLIWGRAVQ GIGAGGINML VDLIICDLVP MRERGNFIGL LFLFVSIGTT SGPIIGGALT
     DNTTWRWVFY INLPMGGAAL VLLVLFLQVK WKKELSTRDR LKRIDVVGNA ILVGATFSIL
     YALTYGGTRY PWSAANIVAP FVLGFVGLGI FIAWESNKRW CPYPVMPLHH FNSRTASASF
     FISFMTMILA FWVVYFYPVY FQSVLGNTPT ISGVHLLPFE VSFPIFAAVG GGLVSKTGRY
     KPIHMVATSI VTIAIGASSV LTQHTHKAAW AVLQIFIGMG LGSLISTTLQ AVQAGLPESE
     TAASTATWAY MRSLGTIWGV SVPAAIFNNR FDQLSGQLDP SIRDNFVRGQ AYEHATAQFV
     QSFEPATREV VIGAYTDALR RVWLVSIAFG AVTVLSTLFE KELTLRTELD SEFGLAEKKG
     DAKGDVERGE GQNDSREGGQ NENV