E13J_TOBAC
ID E13J_TOBAC Reviewed; 160 AA.
AC P52397;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Glucan endo-1,3-beta-glucosidase, acidic isoform PR-O;
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-37;
DE Flags: Fragment;
GN Name=PR0;
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], 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 [2]
RP PROTEIN SEQUENCE OF 70-93; 126-136; 143-152 AND 155-160.
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 -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 17 family. {ECO:0000305}.
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DR EMBL; M60461; AAA34102.1; -; mRNA.
DR AlphaFoldDB; P52397; -.
DR SMR; P52397; -.
DR CAZy; GH17; Glycoside Hydrolase Family 17.
DR Proteomes; UP000084051; Unplaced.
DR GO; GO:0046658; C:anchored component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; 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 InterPro; IPR000490; Glyco_hydro_17.
DR InterPro; IPR044965; Glyco_hydro_17_plant.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR32227; PTHR32227; 1.
DR Pfam; PF00332; Glyco_hydro_17; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00587; GLYCOSYL_HYDROL_F17; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glycosidase; Hydrolase; Plant defense;
KW Reference proteome; Secreted.
FT CHAIN <1..160
FT /note="Glucan endo-1,3-beta-glucosidase, acidic isoform PR-
FT O"
FT /id="PRO_0000205278"
FT ACT_SITE 81
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O22317"
FT CONFLICT 128
FT /note="A -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 135
FT /note="K -> Q (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT NON_TER 1
SQ SEQUENCE 160 AA; 17980 MW; 98C270F390764B7F CRC64;
NSFINPIIQF LARNNLPLLA NVYPYFGHIY NTADVPLSYA LFTQQEANPA GYQNLFDALL
DSMYFAVEKA GGPNVEIIVS ESGWPSEGNS AATIENAQTY YRNLIDHVKR GAGTPKKPGK
TIETYLFAMF DENDKKGEIT EKHFGLFSPD QRAKYQLNFN