TR03_CURCL
ID TR03_CURCL Reviewed; 996 AA.
AC A0A348AXX6;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 07-NOV-2018, sequence version 1.
DT 25-MAY-2022, entry version 10.
DE RecName: Full=KK-1 biosynthesis cluster protein TR03 {ECO:0000303|PubMed:29686660};
GN Name=TR03 {ECO:0000303|PubMed:29686660}; ORFNames=TRAF135003;
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: Part of the gene cluster that mediates the biosynthesis of
CC KK-1, a novel cyclic decapeptide compound with potent antifungal
CC activity (PubMed:29686660). The nonribosomal peptide synthetase (NRPS)
CC catalyzes the elongation and cyclization of the decapeptide chain
CC composed of 1 pipecolic acid residue (Pip), 1 alanine residue (Ala), 1
CC aspartic acid residue (Asp), 1 isoleucine residue (Ile), 1 glycine
CC residue (Gly), 1 tyrosine residue (Tyr) and 4 valine residues (Val)
CC (PubMed:29686660). The Asp, Ile and 3 Val residues are N-methylated by
CC the 5 methyltransferase domains from the NRPS (found in modules 3, 5,
CC 6, 7 and 9), whereas the Tyr residue is O-methylated, probably by the
CC cluster encoded O-methyltransferase OMT (PubMed:29686660). The other
CC tailoring enzymes from the cluster may be involved in further
CC modifications leading to the synthesis of KK-1 (Probable).
CC {ECO:0000269|PubMed:29686660, ECO:0000305|PubMed:29686660}.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000305|PubMed:29686660}.
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DR EMBL; LC371755; BBC83959.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A348AXX6; -.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
PE 4: Predicted;
KW Antibiotic biosynthesis.
FT CHAIN 1..996
FT /note="KK-1 biosynthesis cluster protein TR03"
FT /id="PRO_0000450435"
FT REGION 307..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 425..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 489..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 571..602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..333
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..525
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..543
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 996 AA; 110139 MW; 9AC610F22A5AAB8F CRC64;
MALQERRAAV TSSDILSAHA ISSPALAAAA INFAASFHRD ARTCCSAHER SQLQKVYRDK
ILANDKFTAN IAAAFLSVLG PNAGRNDAGA ERERWGDFDR LAQRGKNMRD RESQHLQHQS
GIIAAWGPRC FEYYGWHVLP LPLLRQVHDL AVLIPSWDDA VELLNSRMLL RHELRVLHGN
NKALRIGEHS AASKVQDSRS PVERTDIVAA LDWARANATS AAARQAVKEA AQGMNGTPIN
TFGLKRDCYG MVVPSVGPYD PDGDDDNDED VVDVSPRPAK HIKLSAAEPL RLMFPGSLSH
VQACQRHDTD GEKASTAPIR SNKLSQSKQP ELDTAAESLR TRHIHNERIN EPLDEVSDCS
LSLQTIAVGG GSAQEETPDQ DVEHAHPEVE ITSAISSELR KVDERTDGIR IGRVIMRRSH
CMVREQDNQT NEEGTGEVQS QRDRRARDLG KDMETDMDID SQLEEMLDIH ALEAQRNHEE
MSDGEDVVAG VAGPGTPTHR AAEEGGCREK EAENAKTDEE QVQDKAALDQ AGNTNTNREV
ENAAPKAHSQ EGALRASRTG TIVERTVELH STHSIHQRAS VNTTAPTVAR SSDSDDSDSL
HSPTALQNLQ AYIDTRTHQL TQVLSQLNST PDVRHHAQLQ LDWLSPQRWA SVYVEPEHHM
GATSSASSDS ADIWCLDWDT FHQYADSNHV FRRPVVIKQK FQDSGMYEVD RYVDMLWQRF
PEQHIEVQNS ITGTSRLMSM AEYCSTALTV TEAGTSLSDN TTSVSNAVNL RCLARADEPL
LTRLERFQLL STLASRVAGT IGRTEHSPPS NLESLLGFDA LSFADAFSSS HANLFGGSWV
RCLDGLKIYA IAADLDAEDW RRFADEGYKW SPRGKGRLIA LEEDDVLFIP PGLRAIHASF
TPEPCLMEGG MLWDECAIPE ILDELLWIAR HQAGTVQPLE FQLSSLIDAL EQWLNENNHI
NQSSPSHTAA EERQTLKASI QSLRDCLSGR SAAFPS