ID   ELIB_PHYCR              Reviewed;         118 AA.
AC   P15570;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=Beta-elicitin cryptogein;
DE            Short=CRY;
DE   Flags: Precursor;
OS   Phytophthora cryptogea.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=4786;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Isolate 52;
RA   Panabieres F., Marais A., le Berre J., Penot I., Fournier D., Ricci P.;
RL   Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 21-118.
RC   STRAIN=Isolate 52;
RX   PubMed=2776750; DOI=10.1111/j.1432-1033.1989.tb21084.x;
RA   Ricci P., Bonnet P., Huet J.-C., Sallantin M., Beauvais-Cante F.,
RA   Brunetau M., Billard V., Michel G., Pernollet J.-C.;
RT   "Structure and activity of proteins from pathogenic fungi Phytophthora
RT   eliciting necrosis and acquired resistance in tobacco.";
RL   Eur. J. Biochem. 183:555-563(1989).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX   PubMed=8994969; DOI=10.1016/s0969-2126(96)00150-5;
RA   Boissy G., de la Fortelle E., Kahn R., Huet J.-C., Bricogne G.,
RA   Pernollet J.-C., Brunie S.;
RT   "Crystal structure of a fungal elicitor secreted by Phytophthora cryptogea,
RT   a member of a novel class of plant necrotic proteins.";
RL   Structure 4:1429-1439(1996).
RN   [4]
RP   STRUCTURE BY NMR.
RX   PubMed=9385630; DOI=10.1002/pro.5560061101;
RA   Fefeu S., Bouaziz S., Huet J.-C., Pernollet J.-C., Guittet E.;
RT   "Three-dimensional solution structure of beta cryptogein, a beta elicitin
RT   secreted by a phytopathogenic fungus Phytophthora cryptogea.";
RL   Protein Sci. 6:2279-2284(1997).
CC   -!- FUNCTION: Induces local and distal defense responses (incompatible
CC       hypersensitive reaction) in plants from the solanaceae and cruciferae
CC       families. Elicits leaf necrosis and causes the accumulation of
CC       pathogenesis-related proteins. Might interact with the lipidic
CC       molecules of the plasma membrane.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the elicitin family. {ECO:0000305}.
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   EMBL; Z34459; CAA84224.1; -; Genomic_DNA.
DR   PIR; S49913; S49913.
DR   PDB; 1BEG; NMR; -; A=21-118.
DR   PDB; 1BEO; X-ray; 2.20 A; A=21-118.
DR   PDB; 1BXM; X-ray; 2.15 A; A=23-118.
DR   PDB; 1LRI; X-ray; 1.45 A; A=21-118.
DR   PDBsum; 1BEG; -.
DR   PDBsum; 1BEO; -.
DR   PDBsum; 1BXM; -.
DR   PDBsum; 1LRI; -.
DR   AlphaFoldDB; P15570; -.
DR   SMR; P15570; -.
DR   EvolutionaryTrace; P15570; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0001907; P:killing by symbiont of host cells; IDA:PAMGO_VMD.
DR   GO; GO:0034053; P:modulation by symbiont of host defense-related programmed cell death; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.239.10; -; 1.
DR   InterPro; IPR002200; Elicitin.
DR   InterPro; IPR036470; Elicitin_sf.
DR   Pfam; PF00964; Elicitin; 1.
DR   PRINTS; PR00948; ELICITIN.
DR   SMART; SM01187; Elicitin; 1.
DR   SUPFAM; SSF48647; SSF48647; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond;
KW   Hypersensitive response elicitation; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000269|PubMed:2776750"
FT   CHAIN           21..118
FT                   /note="Beta-elicitin cryptogein"
FT                   /id="PRO_0000007795"
FT   DISULFID        23..91
FT   DISULFID        47..76
FT   DISULFID        71..115
FT   HELIX           25..35
FT                   /evidence="ECO:0007829|PDB:1LRI"
FT   HELIX           36..40
FT                   /evidence="ECO:0007829|PDB:1LRI"
FT   HELIX           42..51
FT                   /evidence="ECO:0007829|PDB:1LRI"
FT   TURN            55..57
FT                   /evidence="ECO:0007829|PDB:1LRI"
FT   HELIX           64..72
FT                   /evidence="ECO:0007829|PDB:1LRI"
FT   HELIX           74..85
FT                   /evidence="ECO:0007829|PDB:1LRI"
FT   STRAND          90..94
FT                   /evidence="ECO:0007829|PDB:1LRI"
FT   TURN            96..98
FT                   /evidence="ECO:0007829|PDB:1LRI"
FT   HELIX           104..109
FT                   /evidence="ECO:0007829|PDB:1LRI"
FT   HELIX           111..117
FT                   /evidence="ECO:0007829|PDB:1LRI"
SQ   SEQUENCE   118 AA;  12193 MW;  94FDFD872F247D71 CRC64;
     MNFTALLAAV AAALVGSANA TACTATQQTA AYKTLVSILS DASFNQCSTD SGYSMLTAKA
     LPTTAQYKLM CASTACNTMI KKIVTLNPPN CDLTVPTSGL VLNVYSYANG FSNKCSSL