ID   CUTI_PYRBR              Reviewed;         203 AA.
AC   Q9Y7G8;
DT   11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Cutinase pbc1 {ECO:0000303|Ref.1};
DE            EC=3.1.1.74 {ECO:0000305|PubMed:12795380};
DE   AltName: Full=Cutin hydrolase;
DE   Flags: Precursor;
GN   Name=pbc1 {ECO:0000303|Ref.1};
OS   Pyrenopeziza brassicae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Ploettnerulaceae; Pyrenopeziza.
OX   NCBI_TaxID=76659;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
RC   STRAIN=JH26 {ECO:0000303|Ref.1};
RX   DOI=10.1006/pmpp.2000.0282;
RA   Davies K.A., De Lorono I., Foster S.J., Li D., Johnstone K., Ashby A.M.;
RT   "Evidence for a role of cutinase in pathogenicity of Pyrenopeziza brassicae
RT   on brassicas.";
RL   Physiol. Mol. Plant Pathol. 57:63-75(2000).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, INDUCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=NH10 {ECO:0000303|PubMed:12795380};
RX   PubMed=12795380; DOI=10.1094/mpmi.2003.16.6.545;
RA   Li D., Ashby A.M., Johnstone K.;
RT   "Molecular evidence that the extracellular cutinase Pbc1 is required for
RT   pathogenicity of Pyrenopeziza brassicae on oilseed rape.";
RL   Mol. Plant Microbe Interact. 16:545-552(2003).
CC   -!- FUNCTION: Catalyzes the hydrolysis of complex carboxylic polyesters
CC       found in the cell wall of plants (Probable) (PubMed:12795380). Degrades
CC       cutin, a macromolecule that forms the structure of the plant cuticle
CC       (Probable) (PubMed:12795380). Allows pathogenic fungi to penetrate
CC       through the cuticular barrier into the host plant during the initial
CC       stage of fungal infection (Probable) (PubMed:12795380).
CC       {ECO:0000269|PubMed:12795380, ECO:0000305|Ref.1}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cutin + H2O = cutin monomers.; EC=3.1.1.74;
CC         Evidence={ECO:0000305|PubMed:12795380};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P11373}.
CC   -!- INDUCTION: By contact with cutin. {ECO:0000269|PubMed:12795380,
CC       ECO:0000269|Ref.1}.
CC   -!- PTM: The 2 disulfide bonds play a critical role in holding the
CC       catalytic residues in juxta-position; reduction of the disulfide
CC       bridges results in the complete inactivation of the enzyme.
CC       {ECO:0000250|UniProtKB:P11373}.
CC   -!- DISRUPTION PHENOTYPE: Abolishes penetration of the host cuticle
CC       (PubMed:12795380). Abolishes conidiomata formation on the host
CC       (PubMed:12795380). {ECO:0000269|PubMed:12795380}.
CC   -!- SIMILARITY: Belongs to the cutinase family. {ECO:0000305}.
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DR   EMBL; AJ009953; CAB40372.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9Y7G8; -.
DR   SMR; Q9Y7G8; -.
DR   ESTHER; pyrbr-Q9Y7G8; Cutinase.
DR   BRENDA; 3.1.1.74; 13817.
DR   PHI-base; PHI:407; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0052689; F:carboxylic ester hydrolase activity; IMP:UniProtKB.
DR   GO; GO:0050525; F:cutinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0044409; P:entry into host; IMP:UniProtKB.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000675; Cutinase/axe.
DR   InterPro; IPR043580; CUTINASE_1.
DR   InterPro; IPR011150; Cutinase_monf.
DR   Pfam; PF01083; Cutinase; 1.
DR   PRINTS; PR00129; CUTINASE.
DR   SMART; SM01110; Cutinase; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS00155; CUTINASE_1; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; Hydrolase; Secreted; Serine esterase; Signal; Virulence.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..203
FT                   /note="Cutinase pbc1"
FT                   /id="PRO_0000006445"
FT   ACT_SITE        118
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10108"
FT   ACT_SITE        170
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10108"
FT   ACT_SITE        183
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10108"
FT   SITE            119
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
FT   DISULFID        32..107
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
FT   DISULFID        166..173
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
SQ   SEQUENCE   203 AA;  20525 MW;  01FB0B0BC42F7C46 CRC64;
     MKVTALGNTL TGFGQALATT LGVDTTSSSP NCAEMMVVFA RGTSEPGNVG LFSGPTFFDA
     LEVMMGAGAV SVQGVEYGAS IEGFLQGGDP AGSAAMAGIV EGTVQNCPNA KIVMSGYSQG
     GQLVHNAAAM LPAATMAKIS SLVIFGDPND GKPIANADPS KVMVVCHPGH NICDGRDLVL
     VEHLTYSRDA VEAATFAAAR AKA