CHI2_TOBAC
ID CHI2_TOBAC Reviewed; 324 AA.
AC P24091;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 25-MAY-2022, entry version 130.
DE RecName: Full=Endochitinase B;
DE Short=CHN-B;
DE EC=3.2.1.14;
DE Flags: Precursor;
GN Name=CHN50;
OS Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Bright Yellow 4; TISSUE=Leaf;
RX PubMed=1888889; DOI=10.1007/bf00017912;
RA Fukuda Y., Ohme M., Shinshi H.;
RT "Gene structure and expression of a tobacco endochitinase gene in
RT suspension-cultured tobacco cells.";
RL Plant Mol. Biol. 16:1-10(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Havana 425; TISSUE=Leaf;
RX PubMed=1588915; DOI=10.1007/bf00266251;
RA van Buuren M., Neuhaus J.-M., Shinshi H., Ryals J., Meins F. Jr.;
RT "The structure and regulation of homeologous tobacco endochitinase genes of
RT Nicotiana sylvestris and N. tomentosiformis origin.";
RL Mol. Gen. Genet. 232:460-469(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE OF 15-324, AND PROTEIN SEQUENCE OF 24-53.
RC STRAIN=cv. Havana;
RX PubMed=16593796; DOI=10.1073/pnas.84.1.89;
RA Shinshi H., Mohnen D., Meins F. Jr.;
RT "Regulation of a plant pathogenesis-related enzyme: inhibition of chitinase
RT and chitinase mRNA accumulation in cultured tobacco tissues by auxin and
RT cytokinin.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:89-93(1987).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=1946457; DOI=10.1073/pnas.88.22.10362;
RA Neuhaus J.-M., Sticher L., Meins F. Jr., Boller T.;
RT "A short C-terminal sequence is necessary and sufficient for the targeting
RT of chitinases to the plant vacuole.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:10362-10366(1991).
RN [5]
RP HYDROXYLATION AT PRO-67 AND PRO-69, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=1496378; DOI=10.1126/science.1496378;
RA Sticher L., Hofsteenge J., Milani A., Neuhaus J.-M., Meins F. Jr.;
RT "Vacuolar chitinases of tobacco: a new class of hydroxyproline-containing
RT proteins.";
RL Science 257:655-657(1992).
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: Vacuole {ECO:0000269|PubMed:1946457}.
CC Note=Vacuolar and protoplast.
CC -!- INDUCTION: By ethylene.
CC -!- PTM: The 4-hydroxyproline residues are not glycosylated in this plant
CC vacuolar protein.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 19 family. Chitinase
CC class I subfamily. {ECO:0000305}.
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DR EMBL; X51599; CAA35945.1; -; Genomic_DNA.
DR EMBL; X64519; CAA45822.1; -; Genomic_DNA.
DR EMBL; M15173; AAA34070.1; -; mRNA.
DR PIR; S20981; S20981.
DR RefSeq; XP_016509308.1; XM_016653822.1.
DR AlphaFoldDB; P24091; -.
DR SMR; P24091; -.
DR CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR CAZy; GH19; Glycoside Hydrolase Family 19.
DR GeneID; 107826794; -.
DR KEGG; nta:107826794; -.
DR OMA; GNFYSYN; -.
DR OrthoDB; 1132954at2759; -.
DR PhylomeDB; P24091; -.
DR Proteomes; UP000084051; Unplaced.
DR GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR GO; GO:0004568; F:chitinase activity; IBA:GO_Central.
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:0050832; P:defense response to fungus; IBA:GO_Central.
DR GO; GO:0009626; P:plant-type hypersensitive 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 1: Evidence at protein level;
KW Carbohydrate metabolism; Chitin degradation; Chitin-binding;
KW Direct protein sequencing; Disulfide bond; Glycosidase; Hydrolase;
KW Hydroxylation; Hypersensitive response; Pathogenesis-related protein;
KW Plant defense; Polysaccharide degradation; Reference proteome; Signal;
KW Vacuole.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:16593796"
FT CHAIN 24..317
FT /note="Endochitinase B"
FT /id="PRO_0000005332"
FT PROPEP 318..324
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000005333"
FT DOMAIN 24..65
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT ACT_SITE 140
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P29022"
FT MOD_RES 67
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:1496378"
FT MOD_RES 69
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:1496378"
FT DISULFID 26..41
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 35..47
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 40..54
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 59..63
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 96..158
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 170..178
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 277..309
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
SQ SEQUENCE 324 AA; 34721 MW; FA65DC2113B33EB6 CRC64;
MRLREFTALS SLLFSLLLLS ASAEQCGSQA GGARCASGLC CSKFGWCGNT NDYCGPGNCQ
SQCPGGPTPP GGGDLGSIIS SSMFDQMLKH RNDNACQGKG FYSYNAFINA ARSFPGFGTS
GDTTARKREI AAFFAQTSHE TTGGWATAPD GPYAWGYCWL REQGSPGDYC TPSGQWPCAP
GRKYFGRGPI QISHNYNYGP CGRAIGVDLL NNPDLVATDP VISFKSALWF WMTPQSPKPS
CHDVIIGRWQ PSSADRAANR LPGFGVITNI INGGLECGRG TDSRVQDRIG FYRRYCSILG
VSPGDNLDCG NQRSFGNGLL VDTM
