ID   CHIB_VITVI              Reviewed;         314 AA.
AC   P51613;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Basic endochitinase;
DE            EC=3.2.1.14;
DE   Flags: Precursor;
GN   Name=CHIT1B;
OS   Vitis vinifera (Grape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; Vitales; Vitaceae; Viteae; Vitis.
OX   NCBI_TaxID=29760;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Pinot;
RX   PubMed=9390436; DOI=10.1104/pp.115.3.1029;
RA   Busam G., Kassemeyer H.H., Matern U.;
RT   "Differential expression of chitinases in Vitis vinifera L. responding to
RT   systemic acquired resistance activators or fungal challenge.";
RL   Plant Physiol. 115:1029-1038(1997).
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 19 family. Chitinase
CC       class I subfamily. {ECO:0000305}.
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DR   EMBL; Z54234; CAA90970.1; -; mRNA.
DR   AlphaFoldDB; P51613; -.
DR   SMR; P51613; -.
DR   STRING; 29760.VIT_03s0038g03400.t01; -.
DR   CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR   CAZy; GH19; Glycoside Hydrolase Family 19.
DR   EnsemblPlants; Vitvi03g00206_t001; Vitvi03g00206_P001; Vitvi03g00206.
DR   Gramene; Vitvi03g00206_t001; Vitvi03g00206_P001; Vitvi03g00206.
DR   eggNOG; KOG4742; Eukaryota.
DR   HOGENOM; CLU_045506_1_0_1; -.
DR   ExpressionAtlas; P51613; baseline and differential.
DR   GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
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   Gene3D; 3.30.60.10; -; 1.
DR   InterPro; IPR001002; Chitin-bd_1.
DR   InterPro; IPR018371; Chitin-binding_1_CS.
DR   InterPro; IPR036861; Endochitinase-like_sf.
DR   InterPro; IPR016283; Glyco_hydro_19.
DR   InterPro; IPR000726; Glyco_hydro_19_cat.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   Pfam; PF00187; Chitin_bind_1; 1.
DR   Pfam; PF00182; Glyco_hydro_19; 1.
DR   PIRSF; PIRSF001060; Endochitinase; 1.
DR   PRINTS; PR00451; CHITINBINDNG.
DR   SMART; SM00270; ChtBD1; 1.
DR   SUPFAM; SSF53955; SSF53955; 1.
DR   SUPFAM; SSF57016; SSF57016; 1.
DR   PROSITE; PS00026; CHIT_BIND_I_1; 1.
DR   PROSITE; PS50941; CHIT_BIND_I_2; 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; Chitin-binding;
KW   Disulfide bond; Glycosidase; Hydrolase; Plant defense;
KW   Polysaccharide degradation; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..314
FT                   /note="Basic endochitinase"
FT                   /id="PRO_0000005338"
FT   DOMAIN          21..61
FT                   /note="Chitin-binding type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   ACT_SITE        130
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P29022"
FT   DISULFID        23..38
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        32..44
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        37..51
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        55..59
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        86..148
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        160..168
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        267..299
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
SQ   SEQUENCE   314 AA;  33429 MW;  3802484ED69BC6C0 CRC64;
     MGLWALVAFC LLSLILVGSA EQCGGQAGGR VCPGGACCSK FGWCGNTADY CGSGCQSQCS
     STGDIGQLIT RSMFNDMLKH RNEGSCPGKG FYTYDAFIAA AKAFPGFGTT GDTTTRKREI
     AAFLAQTSHE TTGGWASAPD GPYAWGYCYL REQGSPGAYC VPSAQWPCAA GRKYYGRGPI
     QISYNYNYGQ AGKAIGVDLV NNPDLVATDA VISFKTAFWF WMTPQSPKPS CHNVITGGWT
     PSGADRSAGR LPGFGVITNI INGGVECGKG VVPQVQDRIG FYKRYCDILR VSYGNNLDCN
     NQRPFGSGLL LDTI