ID   E13G_TOBAC              Reviewed;         343 AA.
AC   P23547;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   24-JAN-2024, entry version 100.
DE   RecName: Full=Glucan endo-1,3-beta-glucosidase, acidic isoform GI9;
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;
DE   AltName: Full=PR-2B;
DE   AltName: Full=PR-36;
DE   Flags: Precursor;
GN   Name=PR2;
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. Samsun NN;
RX   PubMed=2247445; DOI=10.1073/pnas.87.22.8756;
RA   Linthorst H.J.M., Melchers L.S., Mayer A., van Roekel J.S.C.,
RA   Cornelissen B.J.C., Bol J.F.;
RT   "Analysis of gene families encoding acidic and basic beta-1,3-glucanases of
RT   tobacco.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:8756-8760(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=cv. Xanthi NC; TISSUE=Leaf;
RX   PubMed=16668198; DOI=10.1104/pp.96.2.390;
RA   Ward E.R., Payne G.B., Moyer M.B., Williams S.C., Dincher S.S.,
RA   Sharkey K.C., Beck J.J., Taylor H.T., Ahl-Goy P., Meins F., Ryals J.A.;
RT   "Differential regulation of beta-1,3-glucanase messenger RNAs in response
RT   to pathogen infection.";
RL   Plant Physiol. 96:390-397(1991).
RN   [3]
RP   PROTEIN SEQUENCE OF 39-115; 157-158; 253-276 AND 338-343.
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: Secreted, extracellular space.
CC   -!- INDUCTION: Not found in healthy tissues, but accumulates to high levels
CC       in the extracellular compartment of leaves in response to pathogen
CC       infection or treatment with salicylic acid.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 17 family. {ECO:0000305}.
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DR   EMBL; M59443; AAA63542.1; -; Genomic_DNA.
DR   EMBL; M60460; AAA34103.1; -; mRNA.
DR   PIR; B38257; B38257.
DR   PIR; C38257; C38257.
DR   AlphaFoldDB; P23547; -.
DR   SMR; P23547; -.
DR   STRING; 4097.P23547; -.
DR   CAZy; GH17; Glycoside Hydrolase Family 17.
DR   PaxDb; 4097-P23547; -.
DR   Proteomes; UP000084051; Unplaced.
DR   GO; GO:0005576; C:extracellular region; 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:SF383; GLUCAN ENDO-1,3-BETA-GLUCOSIDASE A; 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; Glycosidase; Hydrolase; Plant defense;
KW   Pyrrolidone carboxylic acid; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000305"
FT   CHAIN           30..343
FT                   /note="Glucan endo-1,3-beta-glucosidase, acidic isoform
FT                   GI9"
FT                   /id="PRO_0000011877"
FT   ACT_SITE        124
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:O22317"
FT   ACT_SITE        264
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:O22317"
FT   MOD_RES         30
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000250|UniProtKB:P15797"
FT   CONFLICT        54
FT                   /note="N -> D (in Ref. 2; AAA34103)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        172
FT                   /note="Y -> N (in Ref. 2; AAA34103)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        303
FT                   /note="K -> N (in Ref. 2; AAA34103)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        323
FT                   /note="Missing (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   343 AA;  37723 MW;  22854FFAFE6B97E3 CRC64;
     MTLCIKNGFL AAALVLVGLL ICSIQMIGAQ SIGVCYGKHA NNLPSDQDVI NLYNANGIRK
     MRIYNPDTNV FNALRGSNIE IILDVPLQDL QSLTDPSRAN GWVQDNIINH FPDVKFKYIA
     VGNEVSPGNN GQYAPFVAPA MQNVYNALAA AGLQDQIKVS TATYSGILAN TYPPKDSIFR
     GEFNSFINPI IQFLVQHNLP LLANVYPYFG HIFNTADVPL SYALFTQQEA NPAGYQNLFD
     ALLDSMYFAV EKAGGQNVEI IVSESGWPSE GNSAATIENA QTYYENLINH VKSGAGTPKK
     PGKAIETYLF AMFDENNKEG DITEKHFGLF SPDQRAKYQL NFN
//