ID   E13B_TOBAC              Reviewed;         371 AA.
AC   P15797;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 2.
DT   24-JAN-2024, entry version 103.
DE   RecName: Full=Glucan endo-1,3-beta-glucosidase, basic vacuolar isoform;
DE            EC=3.2.1.39;
DE   AltName: Full=(1->3)-beta-glucan endohydrolase;
DE            Short=(1->3)-beta-glucanase;
DE   AltName: Full=Beta-1,3-endoglucanase, basic;
DE   Flags: Precursor;
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 [MRNA], PARTIAL PROTEIN SEQUENCE, AND PYROGLUTAMATE
RP   FORMATION AT GLN-34.
RX   PubMed=16593965; DOI=10.1073/pnas.85.15.5541;
RA   Shinshi H., Wenzler H., Neuhaus J.-M., Felix G., Hofsteenge J.,
RA   Meins F. Jr.;
RT   "Evidence for N- and C-terminal processing of a plant defence-related
RT   enzyme: the primary structure of tobacco pre-pro-beta-1,3-glucanase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 85:5541-5545(1988).
RN   [2]
RP   PROTEIN SEQUENCE OF 67-91; 106-110; 194-217; 263-291 AND 344-349.
RX   PubMed=16594025; DOI=10.1073/pnas.86.8.2673;
RA   van den Bulcke M., Bauw G., Castresana C., van Montagu M.,
RA   Vandekerckhove J.;
RT   "Characterization of vacuolar and extracellular beta(1,3)-glucanases of
RT   tobacco: evidence for a strictly compartmentalized plant defense system.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:2673-2677(1989).
CC   -!- FUNCTION: Implicated in the defense of plants against pathogens.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-
CC         beta-D-glucans.; EC=3.2.1.39;
CC   -!- SUBCELLULAR LOCATION: Vacuole.
CC   -!- TISSUE SPECIFICITY: Is expressed primarily in epidermal cell of healthy
CC       plant, and following induction by ethylene, accumulates in mesophyll
CC       cells.
CC   -!- INDUCTION: By ethylene.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 17 family. {ECO:0000305}.
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DR   EMBL; M20618; AAA34080.1; -; mRNA.
DR   EMBL; M20619; AAA34081.1; -; mRNA.
DR   EMBL; M20620; AAA34082.1; -; mRNA.
DR   PIR; A30758; A30758.
DR   AlphaFoldDB; P15797; -.
DR   SMR; P15797; -.
DR   STRING; 4097.P15797; -.
DR   CAZy; GH17; Glycoside Hydrolase Family 17.
DR   PaxDb; 4097-P15797; -.
DR   Proteomes; UP000084051; Unplaced.
DR   GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR   GO; GO:0042973; F:glucan endo-1,3-beta-D-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR000490; Glyco_hydro_17.
DR   InterPro; IPR044965; Glyco_hydro_17_plant.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR32227:SF251; GLUCAN ENDO-1,3-BETA-GLUCOSIDASE B; 1.
DR   PANTHER; PTHR32227; GLUCAN ENDO-1,3-BETA-GLUCOSIDASE BG1-RELATED-RELATED; 1.
DR   Pfam; PF00332; Glyco_hydro_17; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS00587; GLYCOSYL_HYDROL_F17; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycoprotein; Glycosidase; Hydrolase;
KW   Plant defense; Pyrrolidone carboxylic acid; Reference proteome; Signal;
KW   Vacuole.
FT   SIGNAL          1..33
FT   CHAIN           34..349
FT                   /note="Glucan endo-1,3-beta-glucosidase, basic vacuolar
FT                   isoform"
FT                   /id="PRO_0000011869"
FT   PROPEP          350..371
FT                   /note="Removed in mature form"
FT                   /id="PRO_0000011870"
FT   ACT_SITE        129
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:O22317"
FT   ACT_SITE        274
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:O22317"
FT   MOD_RES         34
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:16593965"
FT   CARBOHYD        362
FT                   /note="N-linked (GlcNAc...) asparagine"
FT   VARIANT         193
FT                   /note="T -> V"
FT   VARIANT         296
FT                   /note="N -> Y"
FT   VARIANT         299
FT                   /note="Q -> P"
FT   VARIANT         346
FT                   /note="I -> L"
SQ   SEQUENCE   371 AA;  40510 MW;  8BB1C273104974C8 CRC64;
     MSTSSHKHNT PQMAAITLLG LLLVASSIDI AGAQSIGVCY GMLGNNLPNH WEVIQLYKSR
     NIGRLRLYDP NHGALQALKG SNIEVMLGLP NSDVKHIASG MEHARWWVQK NVKDFWPDVK
     IKYIAVGNEI SPVTGTSYLT SFLTPAMVNI YKAIGEAGLG NNIKVSTSVD MTLIGNSYPP
     SQGSFRNDAR WFTDPIVGFL RDTRAPLLVN IYPYFSYSGN PGQISLPYSL FTAPNVVVQD
     GSRQYRNLFD AMLDSVYAAL ERSGGASVGI VVSESGWPSA GAFGATYDNA ATYLRNLIQH
     AKEGSPRKPG PIETYIFAMF DENNKNPELE KHFGLFSPNK QPKYNINFGV SGGVWDSSVE
     TNATASLVSE M
//