ID   CHIT_PETHY              Reviewed;         254 AA.
AC   P29021;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Acidic endochitinase;
DE            EC=3.2.1.14;
DE   Flags: Precursor;
OS   Petunia hybrida (Petunia).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Petunioideae; Petunia.
OX   NCBI_TaxID=4102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Leaf;
RX   PubMed=2131096; DOI=10.1094/mpmi-3-252;
RA   Linthorst H.J.M., van Loon L.C., van Rossum C.M.A., Mayer A., Bol J.F.,
RA   van Roekel J., Meulenhof J., Conelissen B.J.C.;
RT   "Analysis of acidic and basic chitinases from tobacco and petunia and their
RT   constitutive expression in transgenic tobacco.";
RL   Mol. Plant Microbe Interact. 3:252-258(1990).
CC   -!- FUNCTION: Defense against chitin-containing fungal pathogens.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide
CC         (1->4)-beta-linkages in chitin and chitodextrins.; EC=3.2.1.14;
CC   -!- SUBCELLULAR LOCATION: Secreted. Note=Extracellular fluid from leaves.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 19 family. Chitinase
CC       class II subfamily. {ECO:0000305}.
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DR   EMBL; X51427; CAA35791.1; -; mRNA.
DR   EMBL; A16118; CAA01262.1; -; Unassigned_RNA.
DR   PIR; S20741; S20741.
DR   AlphaFoldDB; P29021; -.
DR   SMR; P29021; -.
DR   CAZy; GH19; Glycoside Hydrolase Family 19.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004568; F:chitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro.
DR   GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0009607; P:response to biotic stimulus; IEA:UniProtKB-KW.
DR   InterPro; IPR016283; Glyco_hydro_19.
DR   InterPro; IPR000726; Glyco_hydro_19_cat.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   Pfam; PF00182; Glyco_hydro_19; 1.
DR   PIRSF; PIRSF001060; Endochitinase; 1.
DR   SUPFAM; SSF53955; SSF53955; 1.
DR   PROSITE; PS00773; CHITINASE_19_1; 1.
DR   PROSITE; PS00774; CHITINASE_19_2; 1.
PE   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Chitin degradation; Disulfide bond; Glycosidase;
KW   Hydrolase; Pathogenesis-related protein; Plant defense;
KW   Polysaccharide degradation; Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000250"
FT   CHAIN           24..254
FT                   /note="Acidic endochitinase"
FT                   /id="PRO_0000005310"
FT   ACT_SITE        91
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P29022"
FT   DISULFID        213..245
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   254 AA;  27665 MW;  377F494721B1E29B CRC64;
     MKFWGSVLAL SFVVFLFLTG TLAQNVGSIV TSDLFDQMLK NRNDARCFAV RFYTYDAFIA
     AANSFPGFGT TGDDTARKKE IAAFFGQTSH ETTGGTLSPD GPYAGGYCFL REGNQMGNGY
     YGRGPIQLTG QSNYDLAGKA IEQDLVNNPD LVATDATVSF KTAIWFWMTP QGNKPSCHDV
     ITGRWTPSAA DTSANRVPGY GVITNIINGG IECGKGQNAR VEDRIGYYRR NVSIMNVAPG
     DNLDCYNQRN FAEV