ID   CUTI1_COLKA             Reviewed;           7 AA.
AC   P86010;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   03-AUG-2022, entry version 22.
DE   RecName: Full=Cutinase 1 {ECO:0000303|PubMed:17043825};
DE            EC=3.1.1.74 {ECO:0000255|PROSITE-ProRule:PRU10108, ECO:0000255|PROSITE-ProRule:PRU10109, ECO:0000305|PubMed:17043825};
DE   AltName: Full=Cutin hydrolase 1;
DE   Flags: Fragment;
OS   Colletotrichum kahawae (Coffee berry disease fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum gloeosporioides species complex.
OX   NCBI_TaxID=34407;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP   SUBCELLULAR LOCATION, INDUCTION, AND BLOCKAGE OF N-TERMINUS.
RC   STRAIN=Z1 {ECO:0000269|PubMed:17043825};
RX   PubMed=17043825; DOI=10.1007/s00253-006-0605-1;
RA   Chen Z., Franco C.F., Baptista R.P., Cabral J.M.S., Coelho A.V.,
RA   Rodrigues C.J. Jr., Melo E.P.;
RT   "Purification and identification of cutinases from Colletotrichum kahawae
RT   and Colletotrichum gloeosporioides.";
RL   Appl. Microbiol. Biotechnol. 73:1306-1313(2007).
CC   -!- FUNCTION: Catalyzes the hydrolysis of complex carboxylic polyesters
CC       found in the cell wall of plants (PubMed:17043825). Degrades cutin, a
CC       macromolecule that forms the structure of the plant cuticle
CC       (PubMed:17043825). Allows pathogenic fungi to penetrate through the
CC       cuticular barrier into the host plant during the initial stage of
CC       fungal infection (By similarity). {ECO:0000250|UniProtKB:P00590,
CC       ECO:0000269|PubMed:17043825}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cutin + H2O = cutin monomers.; EC=3.1.1.74;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10108, ECO:0000255|PROSITE-
CC         ProRule:PRU10109, ECO:0000305|PubMed:17043825};
CC   -!- ACTIVITY REGULATION: Inhibited by diisopropyl fluorophosphate (DFP).
CC       {ECO:0000269|PubMed:17043825}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17043825}.
CC   -!- INDUCTION: By contact with cutin. {ECO:0000269|PubMed:17043825}.
CC   -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:17043825}.
CC   -!- MISCELLANEOUS: On the 2D-gel the determined MW is: 21.7 kDa.
CC       {ECO:0000269|PubMed:17043825}.
CC   -!- SIMILARITY: Belongs to the cutinase family. {ECO:0000255}.
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   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0050525; F:cutinase activity; IDA:UniProtKB.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase; Secreted; Serine esterase; Virulence.
FT   CHAIN           <1..>7
FT                   /note="Cutinase 1"
FT                   /id="PRO_0000352646"
FT   NON_TER         1
FT                   /evidence="ECO:0000303|PubMed:17043825"
FT   NON_TER         7
FT                   /evidence="ECO:0000303|PubMed:17043825"
SQ   SEQUENCE   7 AA;  881 MW;  740DD9C04B5042A0 CRC64;
     VIYIFAR