ID   E13B_SOLLC              Reviewed;         360 AA.
AC   Q01413;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   24-JAN-2024, entry version 120.
DE   RecName: Full=Glucan endo-1,3-beta-glucosidase B;
DE            EC=3.2.1.39;
DE   AltName: Full=(1->3)-beta-glucan endohydrolase B;
DE            Short=(1->3)-beta-glucanase B;
DE   AltName: Full=Basic beta-1,3-glucanase;
DE   AltName: Full=Beta-1,3-endoglucanase B;
DE   Flags: Precursor;
OS   Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC   Solanum subgen. Lycopersicon.
OX   NCBI_TaxID=4081;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Moneymaker; TISSUE=Leaf;
RX   PubMed=1421154; DOI=10.1007/bf00040610;
RA   van Kan J.A.L., Joosten M.H.A.J., Wagemakers C.A.M.,
RA   van den Berg-Velthuis G.C.M., de Wit P.J.G.M.;
RT   "Differential accumulation of mRNAs encoding extracellular and
RT   intracellular PR proteins in tomato induced by virulent and avirulent races
RT   of Cladosporium fulvum.";
RL   Plant Mol. Biol. 20:513-527(1992).
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 {ECO:0000305}.
CC   -!- DEVELOPMENTAL STAGE: Maximum expression found during days 4 to 6 and
CC       days 4 to 14 after inoculation with an avirulent and a virulent
CC       pathogen respectively.
CC   -!- INDUCTION: Upon infection by virulent and avirulent races of pathogens,
CC       for example fungal pathogen C.fulvum.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 17 family. {ECO:0000305}.
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DR   EMBL; M80608; AAA03618.1; -; mRNA.
DR   PIR; S26241; S26241.
DR   RefSeq; NP_001234805.1; NM_001247876.2.
DR   RefSeq; NP_001299819.1; NM_001312890.1.
DR   AlphaFoldDB; Q01413; -.
DR   SMR; Q01413; -.
DR   STRING; 4081.Q01413; -.
DR   Allergome; 2549; Sola l Glucanase.
DR   CAZy; GH17; Glycoside Hydrolase Family 17.
DR   PaxDb; 4081-Solyc01g059980-2-1; -.
DR   EnsemblPlants; Solyc01g059965.1.1; Solyc01g059965.1.1; Solyc01g059965.1.
DR   GeneID; 101261650; -.
DR   GeneID; 543987; -.
DR   Gramene; Solyc01g059965.1.1; Solyc01g059965.1.1; Solyc01g059965.1.
DR   KEGG; sly:101261650; -.
DR   KEGG; sly:543987; -.
DR   eggNOG; ENOG502QQ3M; Eukaryota.
DR   HOGENOM; CLU_024953_0_0_1; -.
DR   InParanoid; Q01413; -.
DR   OMA; HWDIASK; -.
DR   OrthoDB; 46602at2759; -.
DR   PhylomeDB; Q01413; -.
DR   Proteomes; UP000004994; Chromosome 1.
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   2: Evidence at transcript level;
KW   Glycoprotein; Glycosidase; Hydrolase; Plant defense;
KW   Pyrrolidone carboxylic acid; Reference proteome; Signal; Vacuole.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000250"
FT   CHAIN           26..340
FT                   /note="Glucan endo-1,3-beta-glucosidase B"
FT                   /id="PRO_0000011852"
FT   PROPEP          341..360
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000011853"
FT   ACT_SITE        120
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:O22317"
FT   ACT_SITE        265
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:O22317"
FT   MOD_RES         26
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000250|UniProtKB:P15797"
FT   CARBOHYD        350
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   360 AA;  39719 MW;  EB29C1AB76347EE1 CRC64;
     MATSQIAIIV LLGLLVATNI HITEAQIGVC YGMMGNNLPS HSEVIQLYKS RNIRRLRLYD
     PNHGALNALR GSNIEVILGL PNVDVKHISS GMEHARWWVQ KNVRDFWPHV KIKYIAVGNE
     ISPVTGTSNL APFQVPALVN IYKAIGEAGL GNDIKVSTSV DMTLIGNSYP PSQGSFRNDV
     RWFTDPIVGF LRDTRAPLLV NIYPYFSYSG NPGQISLPYA LFTAPNVVVQ DGSRQYRNLF
     DAMLDSVYAA MDRTGGGSVG IVVSESGWPS AGAFGATHEN AQTYLRNLIQ HAKEGSPRKP
     GPIETYIFAM FDENNKNPEL EKHFGMFSPN KQPKYNLNFG VSERVWDITN STASSLTSEI
//