ID   TR09_CURCL              Reviewed;         307 AA.
AC   A0A348AXY2;
DT   12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT   07-NOV-2018, sequence version 1.
DT   25-MAY-2022, entry version 14.
DE   RecName: Full=Probable thioesterase TR09 {ECO:0000303|PubMed:29686660};
DE            EC=3.1.-.- {ECO:0000305|PubMed:29686660};
DE   AltName: Full=KK-1 biosynthesis cluster protein TR09 {ECO:0000303|PubMed:29686660};
GN   Name=TR09 {ECO:0000303|PubMed:29686660}; ORFNames=TRAF135009;
OS   Curvularia clavata.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Curvularia.
OX   NCBI_TaxID=95742;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
RC   STRAIN=BAUA-2787;
RX   PubMed=29686660; DOI=10.3389/fmicb.2018.00690;
RA   Yoshimi A., Yamaguchi S., Fujioka T., Kawai K., Gomi K., Machida M.,
RA   Abe K.;
RT   "Heterologous Production of a Novel Cyclic Peptide Compound, KK-1, in
RT   Aspergillus oryzae.";
RL   Front. Microbiol. 9:690-690(2018).
CC   -!- FUNCTION: Probable thioesterase; part of the gene cluster that mediates
CC       the biosynthesis of KK-1, a novel cyclic decapeptide compound with
CC       potent antifungal activity (PubMed:29686660). The nonribosomal peptide
CC       synthetase (NRPS) catalyzes the elongation and cyclization of the
CC       decapeptide chain composed of 1 pipecolic acid residue (Pip), 1 alanine
CC       residue (Ala), 1 aspartic acid residue (Asp), 1 isoleucine residue
CC       (Ile), 1 glycine residue (Gly), 1 tyrosine residue (Tyr) and 4 valine
CC       residues (Val) (PubMed:29686660). The Asp, Ile and 3 Val residues are
CC       N-methylated by the 5 methyltransferase domains from the NRPS (found in
CC       modules 3, 5, 6, 7 and 9), whereas the Tyr residue is O-methylated,
CC       probably by the cluster encoded O-methyltransferase OMT
CC       (PubMed:29686660). The other tailoring enzymes from the cluster may be
CC       involved in further modifications leading to the synthesis of KK-1
CC       (Probable). {ECO:0000269|PubMed:29686660, ECO:0000305|PubMed:29686660}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000305|PubMed:29686660}.
CC   -!- SIMILARITY: Belongs to the AMT4 thioesterase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LC371755; BBC83965.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A348AXY2; -.
DR   SMR; A0A348AXY2; -.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001031; Thioesterase.
DR   Pfam; PF00975; Thioesterase; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   3: Inferred from homology;
KW   Antibiotic biosynthesis; Hydrolase.
FT   CHAIN           1..307
FT                   /note="Probable thioesterase TR09"
FT                   /id="PRO_0000450438"
SQ   SEQUENCE   307 AA;  34405 MW;  6809678D7EE0392C CRC64;
     MESEDNPLRI QTGSLCSFQR PTPLVLIHDS SGTTFSYFRL GSLNRDVWAI HDPHFDKSTP
     WKGGFGEIAE HYIKLIETAG IRGSILLGGW SLGGYLALTI AHKLTAITNP TFSVTGILLV
     DSPYHTPMSK LPPHAPDPNF QHLPELVRKS FENYDVLLDR WELPPWTAPA LEGKTIRCSA
     GGKTFTVANG RILYKPLGKG WEDVKMQSFE HGTSTLERYI ELPPAALIRC AQAIPTDTDS
     KMPCFVDRFR HETLLGWDSN FPSFIKAAVD TNTHHFNIFE SQNLKRLTIQ LNECLEVLDS
     CCPMGYC