ID   SAT4_STACB              Reviewed;         268 AA.
AC   A0A084B9Z2;
DT   22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT   29-OCT-2014, sequence version 1.
DT   03-AUG-2022, entry version 12.
DE   RecName: Full=Satratoxin biosynthesis SC1 cluster protein 4 {ECO:0000303|PubMed:25015739};
GN   Name=SAT4 {ECO:0000303|PubMed:25015739}; ORFNames=S7711_07278;
OS   Stachybotrys chartarum (strain CBS 109288 / IBT 7711) (Toxic black mold)
OS   (Stilbospora chartarum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Stachybotryaceae; Stachybotrys.
OX   NCBI_TaxID=1280523;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], IDENTIFICATION, AND
RP   FUNCTION.
RC   STRAIN=CBS 109288 / IBT 7711;
RX   PubMed=25015739; DOI=10.1186/1471-2164-15-590;
RA   Semeiks J., Borek D., Otwinowski Z., Grishin N.V.;
RT   "Comparative genome sequencing reveals chemotype-specific gene clusters in
RT   the toxigenic black mold Stachybotrys.";
RL   BMC Genomics 15:590-590(2014).
CC   -!- FUNCTION: Part of the satratoxin SC1 cluster involved in the
CC       biosynthesis of satratoxins, trichothecene mycotoxins that are
CC       associated with human food poisonings (PubMed:25015739). Satratoxins
CC       are suggested to be made by products of multiple gene clusters (SC1,
CC       SC2 and SC3) that encode 21 proteins in all, including polyketide
CC       synthases, acetyltransferases, and other enzymes expected to modify the
CC       trichothecene skeleton (PubMed:25015739). SC1 encodes 10 proteins, SAT1
CC       to SAT10 (PubMed:25015739). The largest are SAT8, which encodes a
CC       putative polyketide synthase (PKS) with a conventional non-reducing
CC       architecture, and SAT10, a putative protein containing four ankyrin
CC       repeats and thus may be involved in protein scaffolding
CC       (PubMed:25015739). The putative short-chain reductase SAT3 may assist
CC       the PKS in some capacity (PubMed:25015739). SAT6 contains a secretory
CC       lipase domain and acts probably as a trichothecene esterase
CC       (PubMed:25015739). SAT5 encodes a putative acetyltransferase, and so,
CC       with SAT6, may affect endogenous protection from toxicity
CC       (PubMed:25015739). The probable transcription factor SAT9 may regulate
CC       the expression of the SC1 cluster (PubMed:25015739). SC2 encodes
CC       proteins SAT11 to SAT16, the largest of which encodes the putative
CC       reducing PKS SAT13 (PubMed:25015739). SAT11 is a cytochrome P450
CC       monooxygenase, while SAT14 and SAT16 are probable acetyltransferases
CC       (PubMed:25015739). The SC2 cluster may be regulated by the
CC       transcription factor SAT15 (PubMed:25015739). SC3 is a small cluster
CC       that encodes 5 proteins, SAT17 to SAT21 (PubMed:25015739). SAT21 is a
CC       putative MFS-type transporter which may have a role in exporting
CC       secondary metabolites (PubMed:25015739). The four other proteins
CC       putatively encoded in SC3 include the taurine hydroxylase-like protein
CC       SAT17, the O-methyltransferase SAT18, the acetyltransferase SAT19, and
CC       the Cys6-type zinc finger SAT20, the latter being probably involved in
CC       regulation of SC3 expression (PubMed:25015739).
CC       {ECO:0000305|PubMed:25015739}.
CC   -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:25015739}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- MISCELLANEOUS: Trichothecenes are sesquiterpenoid toxins that act by
CC       inhibiting protein biosynthesis. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the SAT4 family. {ECO:0000305}.
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DR   EMBL; KL647604; KEY74371.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A084B9Z2; -.
DR   EnsemblFungi; KEY74371; KEY74371; S7711_07278.
DR   HOGENOM; CLU_1038910_0_0_1; -.
DR   OrthoDB; 1433063at2759; -.
DR   Proteomes; UP000028045; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
PE   3: Inferred from homology;
KW   Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN           1..268
FT                   /note="Satratoxin biosynthesis SC1 cluster protein 4"
FT                   /id="PRO_0000442391"
FT   TRANSMEM        34..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        78..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        113..133
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        145..165
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   268 AA;  29914 MW;  9C5933121749144D CRC64;
     MNGIYALQQT FVKFSLLALY HRLFWVNRHF VRSVWLVGIV QGCWGIAILL VHIFLCTPME
     KIWTPWMVEG TCVDVNTLFA IYEALNSVLD FIVAGLAIWM LPSLQIRKST RWHLAGLFVL
     GAFSGFIGII KIVEAYDSAQ RNFQAVIWNV VQMSISIICC CAPIYRSILP KMGMSSIPSW
     ASWSLRGSSR RSKAVASTAD GTSKFSMRSY QGEGKAGGTS VSGNWINLDG SSQRALAWVD
     AESHGKDQST YQDIPMGRMK VERSVEVI