ID   CHIB_SOLLC              Reviewed;         247 AA.
AC   Q05540;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   16-JUN-2009, entry version 68.
DE   RecName: Full=Acidic 27 kDa endochitinase;
DE            EC=3.2.1.14;
DE   Flags: Precursor;
GN   Name=CHI17;
OS   Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae;
OC   Solanum; Lycopersicon.
OX   NCBI_TaxID=4081;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 112-115; 182-188
RP   AND 218-221.
RC   STRAIN=cv. Moneymaker;
RX   MEDLINE=94003061; PubMed=8400122; DOI=10.1007/BF00028974;
RA   Danhash N., Wagemakers C.A.M., van Kan J.A.L., de Wit P.J.G.M.;
RT   "Molecular characterization of four chitinase cDNAs obtained from
RT   Cladosporium fulvum-infected tomato.";
RL   Plant Mol. Biol. 22:1017-1029(1993).
CC   -!- FUNCTION: Defense against chitin containing fungal pathogens.
CC   -!- CATALYTIC ACTIVITY: Random hydrolysis of N-acetyl-beta-D-
CC       glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC   -!- INDUCTION: By fungal infection.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 19 family. Chitinase
CC       class II subfamily.
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DR   EMBL; Z15139; CAA78844.1; -; mRNA.
DR   PIR; S37342; S37342.
DR   UniGene; Les.3779; -.
DR   HSSP; O81934; 1DXJ.
DR   CAZy; GH19; Glycoside Hydrolase Family 19.
DR   BRENDA; 3.2.1.14; 281054.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR   GO; GO:0004568; F:chitinase activity; IEA: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   PANTHER; PTHR22595; Glyco_hydro_19_cat; 1.
DR   Pfam; PF00182; Glyco_hydro_19; 1.
DR   PIRSF; PIRSF001060; Endochitinase; 1.
DR   ProDom; PD354900; Glyco_hydro_19; 1.
DR   PROSITE; PS00773; CHITINASE_19_1; 1.
DR   PROSITE; PS00774; CHITINASE_19_2; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Chitin degradation;
KW   Direct protein sequencing; Disulfide bond; Glycosidase; Hydrolase;
KW   Pathogenesis-related protein; Plant defense;
KW   Polysaccharide degradation; Secreted; Signal.
FT   SIGNAL        1     16       By similarity.
FT   CHAIN        17    247       Acidic 27 kDa endochitinase.
FT                                /FTId=PRO_0000005300.
FT   DISULFID    206    238       By similarity.
SQ   SEQUENCE   247 AA;  26584 MW;  C1163ED1D272A5E5 CRC64;
     MVLCCVFLLF LTGSFAQDVG TIVTSDLFNE MLKNRNDDRC PAKGFYTYDA FIAAANSFPG
     FGTTGDDTAR KKEIAAFFGQ TSHETTGGSL SADGPFAGGY CFVREGNQMG SGFYGRGPIQ
     LTGQSNYDLA GQAIGQDLVN NPDLVATDAT VSFKTAIWFW MTAQGNKPSC HDVITGQWTP
     SAADASANRQ PGYGVITNII NGGIECGKGQ NPQVEDRIGF YRRYCTILNV APGDNLDCYD
     QRNFAEA
//