HEPF_ASPOR
ID HEPF_ASPOR Reviewed; 483 AA.
AC Q2U0J8;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=MFS-type transporter hepF {ECO:0000303|PubMed:30466366};
DE AltName: Full=Heptelidic acid biosynthesis cluster protein F {ECO:0000303|PubMed:30466366};
GN Name=hepF; ORFNames=AO090011000413;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=30466366; DOI=10.1080/09168451.2018.1549934;
RA Shinohara Y., Nishimura I., Koyama Y.;
RT "Identification of a gene cluster for biosynthesis of the sesquiterpene
RT antibiotic, heptelidic acid, in Aspergillus oryzae.";
RL Biosci. Biotechnol. Biochem. 83:1506-1513(2019).
CC -!- FUNCTION: MFS-type transporter; part of the gene cluster that mediates
CC the biosynthesis of heptelidic acid (HA), a sesquiterpene lactone that
CC acts as an inhibitor of glyceraldehyde-3-phosphatedehydrogenase (GAPDH)
CC and a growth inhibitor of the salt-tolerant lactic acid bacteria in soy
CC sauce brewing (PubMed:30466366). Might be required for efficient
CC secretion of heptelidic acid (Probable). {ECO:0000269|PubMed:30466366,
CC ECO:0000305|PubMed:30466366}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Does not affect the biosynthesis of heptelidic
CC acid. {ECO:0000269|PubMed:30466366}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC {ECO:0000305}.
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DR EMBL; AP007171; BAE64917.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2U0J8; -.
DR EnsemblFungi; BAE64917; BAE64917; AO090011000413.
DR HOGENOM; CLU_008455_1_1_1; -.
DR Proteomes; UP000006564; Chromosome 7.
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 Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
PE 3: Inferred from homology;
KW Cell membrane; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..483
FT /note="MFS-type transporter hepF"
FT /id="PRO_0000450833"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 311..331
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 357..377
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 385..405
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 416..436
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 448..468
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 483 AA; 53129 MW; F954F5E34ED19960 CRC64;
METPAGKADR PRDHDSEQSQ DNVVSWEGED DPTNPLNWSP LAKWVHVAII SIGTFTIARE
KSPLASSIFA PGVVELAHEF HEENQLLTTI VVSIFVLGLA FGPLLAAPIS EMYGRWICYT
VFNILYTIFT VACGVSTNIS MLIVFRFFAG VTGSAPLTIG GGTVADLFPM HQRGLALSFV
TLGQAVAPAI GPVAGGFLTQ NLGWRWVFWL LTIVNGTITI CQILFTRETY AMTILNRRAK
RLRKTTVHSS VTHRSVNFAI FFYSLVRPCK LLLLSPISLI VALCCAVIYG ILYVLVTTFS
PVFQDTYHFS IGISGLGYLG LGIGNLVGLW IFSMTSDRYM VAQANRFGSA KPEHRLPMMI
LSGPVIAAGL FWYGWSVQAR IHWMMPIVGS GIVGLGNMFF FMPMVSYLVD SFPTYAASAI
AANAVLRSIG GAVLPLAGQR MYDTLGFGWG NSILAFMALV FNPLLIAIYR YGEYIRTRWQ
VKL
