CTB11_CERBT
ID CTB11_CERBT Reviewed; 374 AA.
AC A0A2G5I8H1;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 31-JAN-2018, sequence version 1.
DT 25-MAY-2022, entry version 11.
DE RecName: Full=Fasciclin-like arabinogalactan protein CTB11 {ECO:0000303|PubMed:29844193};
DE AltName: Full=Cercosporin toxin biosynthesis cluster protein 11 {ECO:0000303|PubMed:29844193};
DE Flags: Precursor;
GN Name=CTB11 {ECO:0000303|PubMed:29844193}; ORFNames=CB0940_00844;
OS Cercospora beticola (Sugarbeet leaf spot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Cercospora.
OX NCBI_TaxID=122368;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], FUNCTION, DISRUPTION
RP PHENOTYPE, AND PATHWAY.
RC STRAIN=09-40;
RX PubMed=29844193; DOI=10.1073/pnas.1712798115;
RA de Jonge R., Ebert M.K., Huitt-Roehl C.R., Pal P., Suttle J.C.,
RA Spanner R.E., Neubauer J.D., Jurick W.M. II, Stott K.A., Secor G.A.,
RA Thomma B.P.H.J., Van de Peer Y., Townsend C.A., Bolton M.D.;
RT "Gene cluster conservation provides insight into cercosporin biosynthesis
RT and extends production to the genus Colletotrichum.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:E5459-E5466(2018).
RN [2]
RP REVIEW ON CERCOSPORIN.
RX PubMed=11701851; DOI=10.1146/annurev.phyto.38.1.461;
RA Daub M.E., Ehrenshaft M.;
RT "The photoactivated cercospora toxin cercosporin: contributions to plant
RT disease and fundamental biology.";
RL Annu. Rev. Phytopathol. 38:461-490(2000).
CC -!- FUNCTION: Fasciclin-like arabinogalactan protein; part of the gene
CC cluster that mediates the biosynthesis of cercosporin, a light-
CC activated, non-host-selective toxin (PubMed:29844193). The
CC perylenequinone chromophore of cercosporin absorbs light energy to
CC attain an electronically-activated triplet state and produces active
CC oxygen species such as the hydroxyl radical, superoxide, hydrogen
CC peroxide or singlet oxygen upon reaction with oxygen molecules
CC (PubMed:11701851). These reactive oxygen species cause damage to
CC various cellular components including lipids, proteins and nucleic
CC acids (PubMed:11701851). The first step of cercosporin biosynthesis is
CC performed by the polyketide synthase CTB1 which catalyzes the formation
CC of nor-toralactone (Probable). The starter unit acyltransferase (SAT)
CC domain of CTB1 initiates polyketide extension by the selective
CC utilization of acetyl-CoA, which is elongated to the heptaketide in the
CC beta-ketoacyl synthase (KS) domain by successive condensations with six
CC malonyl units introduced by the malonyl acyltransferase (MAT) domain.
CC The product template (PT) domain catalyzes C4-C9 and C2-C11 aldol
CC cyclizations and dehydrations to a trihydroxynaphthalene, which is
CC thought to be delivered to the thioesterase (TE) domain for product
CC release (Probable). The bifunctional enzyme CTB3 then methylates nor-
CC toralactone to toralactone before conducting an unusual oxidative
CC aromatic ring opening (Probable). The O-methyltransferase CTB2 further
CC methylates the nascent OH-6 of the CBT3 product, blocking further
CC oxidation at this site before the reductase CTB6 reduces the 2-
CC oxopropyl ketone at position C7, giving naphthalene (Probable). The
CC FAD-dependent monooxygenase CTB5 in concert with the multicopper
CC oxidase CTB12 are responsible for homodimerization of naphthalene with
CC CTB7 installing the dioxepine moiety, finally producing cercosporin
CC (Probable). The fasciclin domain-containing protein CTB11 might act
CC with CTB5 and CTB12 whereas the roles of CTB9 and CTB10 have still to
CC be elucidated (By similarity). {ECO:0000250|UniProtKB:Q0UHZ9,
CC ECO:0000269|PubMed:29844193, ECO:0000303|PubMed:11701851,
CC ECO:0000305|PubMed:29844193}.
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:29844193}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Abolishes the production of cercosporin.
CC {ECO:0000269|PubMed:29844193}.
CC -!- SIMILARITY: Belongs to the fasciclin-like AGP family. {ECO:0000305}.
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DR EMBL; LKMD01000100; PIB01156.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5I8H1; -.
DR SMR; A0A2G5I8H1; -.
DR OrthoDB; 984651at2759; -.
DR Proteomes; UP000230605; Chromosome 1.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR Gene3D; 2.30.180.10; -; 2.
DR InterPro; IPR036378; FAS1_dom_sf.
DR InterPro; IPR000782; FAS1_domain.
DR Pfam; PF02469; Fasciclin; 2.
DR SMART; SM00554; FAS1; 2.
DR SUPFAM; SSF82153; SSF82153; 2.
DR PROSITE; PS50213; FAS1; 2.
PE 3: Inferred from homology;
KW Glycoprotein; Membrane; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..374
FT /note="Fasciclin-like arabinogalactan protein CTB11"
FT /id="PRO_5013579449"
FT TRANSMEM 328..348
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 19..171
FT /note="FAS1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082"
FT DOMAIN 173..302
FT /note="FAS1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 132
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 374 AA; 40552 MW; 18E0FE624F7C91EB CRC64;
MHFPALAVAG CLLSRATAQS LDQVLAKRDS FSLLRDLLHQ HGLVDELEFT ANATFFAMTN
QALRSLADFG INLTTADPNI ARAIFKYAQL DAIYTTDTVK ALHHEAKVVQ TALQPHLFNN
LTRGQAAKLR SNRTGGANGI LVESGLGVLT PVVEADIPYD HGVIHAIDAN MVLPHNISET
ARLGGMTEFL NLLERSDSVA RLESLSDVTI FIPQDEALAK LQPILDMLTS EQLKSVVAQH
AVPNRVLYQS LFDGVETLET LDGSTLRIRR GKRGEIFVNG AEVVRTDLLL YGGVAHLIDG
ALLPEKDASC STGLFAAAAG GSSRVWKILA SHQLTLLAVL AMALVSILYK AYQSRKQSHQ
LIRPSDGLGN YEKV
