ID   TWMC_TALWO              Reviewed;         363 AA.
AC   A0A2L0P0K0;
DT   07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT   25-APR-2018, sequence version 1.
DT   25-MAY-2022, entry version 12.
DE   RecName: Full=Wortmanamides biosynthesis cluster protein C {ECO:0000303|PubMed:29343058};
GN   Name=TwnC {ECO:0000303|PubMed:29343058};
OS   Talaromyces wortmannii (Penicillium wortmannii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Islandici.
OX   NCBI_TaxID=28567;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
RC   STRAIN=ATCC 26942 / CBS 387.67 / CCM F-175 / VKM F-2091;
RX   PubMed=29343058; DOI=10.1021/jacs.7b13350;
RA   Hai Y., Tang Y.;
RT   "Biosynthesis of long-chain N-acyl amide by a truncated polyketide
RT   synthase-nonribosomal peptide synthetase hybrid megasynthase in fungi.";
RL   J. Am. Chem. Soc. 140:1271-1274(2018).
CC   -!- FUNCTION: Part of the gene cluster that mediates the biosynthesis of
CC       wortmanamides A and B, reduced long-chain polyketides amidated with a
CC       specific omega-amino acid, 5-aminopentanoic acid (5PA)
CC       (PubMed:29343058). The PKS modules of TwmB are involved in the
CC       synthesis of the polyketide backbone, whereas the non-canonical C
CC       domain of TwmB is a bonafide condensation domain that specifically
CC       selects 5PA and catalyzes amidation to release polyketide chain
CC       (PubMed:29343058). The C domain clearly prefers C16 and C18 fatty acyl
CC       substrates, which is consistent with simultaneous formation of both
CC       octaketide and nonaketide acyl amides wortmanamides A and B
CC       (PubMed:29343058). Because TwmB lacks a designated enoylreductase (ER)
CC       domain, the required activity is provided the enoyl reductase TwmE
CC       (PubMed:29343058). The roles of the remaining enzymes have still to be
CC       clarified (Probable). {ECO:0000269|PubMed:29343058,
CC       ECO:0000305|PubMed:29343058}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000305|PubMed:29343058}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the SAT4 family. {ECO:0000305}.
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DR   EMBL; MG837520; AUY61971.1; -; Genomic_DNA.
DR   EMBL; MH399766; QBC19711.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2L0P0K0; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
PE   3: Inferred from homology;
KW   Glycoprotein; Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN           1..363
FT                   /note="Wortmanamides biosynthesis cluster protein C"
FT                   /id="PRO_0000452488"
FT   TRANSMEM        15..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        48..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        95..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        129..149
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        175..195
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        210..230
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        237..257
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          293..312
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          344..363
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        321
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   363 AA;  40572 MW;  3DA3BE92F06E5F67 CRC64;
     MAFEIPEDST QLSQFVTLLI FTPLGIVVTA LRFVAVRRVT RKVGFEDWLA VIATIFFILT
     NLAGLMAISI LNGRQLTQEV IESPSDYSRM RKWDIAGLFF YFAQTLSVKL SILAFYHRIF
     GISSTRCRIC IYLLAAAQTI LFIAFCIFQG FQCIPLQRYF DLSVPGECKD EGTVILGGEL
     PNSLVDFAMV ILAMIMIRPL QLSFSDKFRV TVLFGLGFVV GIIGFVKIAV TYSTSELYAF
     SMIALWTGVQ MFTALLCCSL PMYNTFLPIV ADFWNRLSHH SLGWVSRVRS SQSSSKNSRK
     HGPYDSDQSP GPGWDDLVAY NGTKGLTLPQ APYHGDNHAL GNVSPITHPQ AYSKQTTRQF
     DVV