E13D_TOBAC
ID E13D_TOBAC Reviewed; 351 AA.
AC P23433;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Glucan endo-1,3-beta-glucosidase;
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 Flags: Precursor;
GN Name=SP41B;
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, PYROGLUTAMATE
RP FORMATION AT GLN-33, GLYCOSYLATION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=2120041; DOI=10.1002/j.1460-2075.1990.tb07550.x;
RA Ori N., Sessa G., Lotan T., Himmelhoch S., Fluhr R.;
RT "A major stylar matrix polypeptide (sp41) is a member of the pathogenesis-
RT related proteins superclass.";
RL EMBO J. 9:3429-3436(1990).
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, extracellular
CC matrix {ECO:0000269|PubMed:2120041}. Note=Stylar secretory matrix.
CC -!- DEVELOPMENTAL STAGE: Maximal level of accumulation during anthesis.
CC {ECO:0000269|PubMed:2120041}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:2120041}.
CC -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:2120041}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 17 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X54431; CAA38303.1; -; mRNA.
DR PIR; S12014; S12014.
DR RefSeq; NP_001312176.1; NM_001325247.1.
DR AlphaFoldDB; P23433; -.
DR SMR; P23433; -.
DR CAZy; GH17; Glycoside Hydrolase Family 17.
DR GeneID; 107777766; -.
DR KEGG; nta:107777766; -.
DR Proteomes; UP000084051; Unplaced.
DR GO; GO:0046658; C:anchored component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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:0009626; P:plant-type hypersensitive 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; Extracellular matrix; Glycoprotein; Glycosidase;
KW Hydrolase; Hypersensitive response; Pathogenesis-related protein;
KW Plant defense; Pyrrolidone carboxylic acid; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..32
FT CHAIN 33..351
FT /note="Glucan endo-1,3-beta-glucosidase"
FT /id="PRO_0000011876"
FT ACT_SITE 128
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O22317"
FT ACT_SITE 268
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O22317"
FT MOD_RES 33
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:2120041"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 235
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 351 AA; 39262 MW; C13273CFA59A3F8E CRC64;
MALWYLFNKR SLGAAVLILV GLLMCNIQIT GAQSNIGVCY GEIANNLPSE QDVINLYKAN
GIRKMRIYYP DTNIFKALNG SNIEIILEVP NQDLEALANS SIANGWVQDN IRSHFPYVKF
KYISIGNEVS PTNNGQYSQF LLHAMKNVYN ALAAAGLQDK IKVSTATYSG LLANTYPPKD
SIFREELKSF INPIIEFLAR NNLPLLANIY PYFGHIYNTV DVPLSYALFN QQETNSTGYQ
NLFDALLDSI YFAVEKAGGP NVEIIVSESG WPSEGNSAAT IENAQTYYRN LVNHVKGGAG
TPKKPGRIIE TYLFAMFDEN EKQGEITEKH FGLFYPNRAA KYQLNFMYSD S