ID   BGL2_ARTBC              Reviewed;         308 AA.
AC   D4B2W4;
DT   11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 51.
DE   RecName: Full=Glucan 1,3-beta-glucosidase ARB_02797 {ECO:0000305};
DE            EC=3.2.1.58 {ECO:0000250|UniProtKB:Q5AMT2};
DE   AltName: Full=Exo-1,3-beta-glucanase {ECO:0000250|UniProtKB:Q5AMT2};
DE   Flags: Precursor;
GN   ORFNames=ARB_02797;
OS   Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS   mentagrophytes).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], IDENTIFICATION BY MASS
RP   SPECTROMETRY, SUBCELLULAR LOCATION, AND INDUCTION.
RC   STRAIN=ATCC MYA-4681 / CBS 112371 {ECO:0000312|Proteomes:UP000008866};
RX   PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA   Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA   Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA   Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA   Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA   Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT   "Comparative and functional genomics provide insights into the
RT   pathogenicity of dermatophytic fungi.";
RL   Genome Biol. 12:R7.1-R7.16(2011).
RN   [2]
RP   SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=21919205; DOI=10.1002/pmic.201100234;
RA   Sriranganadane D., Waridel P., Salamin K., Feuermann M., Mignon B.,
RA   Staib P., Neuhaus J.M., Quadroni M., Monod M.;
RT   "Identification of novel secreted proteases during extracellular
RT   proteolysis by dermatophytes at acidic pH.";
RL   Proteomics 11:4422-4433(2011).
CC   -!- FUNCTION: Cell wall glucan 1,3-beta-glucosidase involved in cell wall
CC       biosynthesis and virulence (By similarity). Crucial for delivery of
CC       beta-1,3-glucan to the biofilm matrix and for accumulation of mature
CC       matrix biomass (By similarity). {ECO:0000250|UniProtKB:Q5AMT2}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Successive hydrolysis of beta-D-glucose units from the non-
CC         reducing ends of (1->3)-beta-D-glucans, releasing alpha-glucose.;
CC         EC=3.2.1.58; Evidence={ECO:0000250|UniProtKB:Q5AMT2};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21247460,
CC       ECO:0000269|PubMed:21919205}. Secreted, cell wall
CC       {ECO:0000250|UniProtKB:Q5AMT2}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q5AMT2}.
CC   -!- INDUCTION: Expression is down-regulated in presence of human
CC       keratinocytes. {ECO:0000269|PubMed:21247460}.
CC   -!- ALLERGEN: May cause an allergic reaction in human. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 17 family. {ECO:0000305}.
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DR   EMBL; ABSU01000031; EFE30260.1; -; Genomic_DNA.
DR   RefSeq; XP_003010900.1; XM_003010854.1.
DR   AlphaFoldDB; D4B2W4; -.
DR   SMR; D4B2W4; -.
DR   STRING; 663331.D4B2W4; -.
DR   EnsemblFungi; EFE30260; EFE30260; ARB_02797.
DR   GeneID; 9525013; -.
DR   KEGG; abe:ARB_02797; -.
DR   eggNOG; ENOG502QQE6; Eukaryota.
DR   HOGENOM; CLU_028820_2_0_1; -.
DR   OMA; WKPDTSG; -.
DR   Proteomes; UP000008866; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0009277; C:fungal-type cell wall; IEA:EnsemblFungi.
DR   GO; GO:0042973; F:glucan endo-1,3-beta-D-glucosidase activity; IEA:EnsemblFungi.
DR   GO; GO:0004338; F:glucan exo-1,3-beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0031505; P:fungal-type cell wall organization; IEA:EnsemblFungi.
DR   InterPro; IPR000490; Glyco_hydro_17.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF00332; Glyco_hydro_17; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   1: Evidence at protein level;
KW   Allergen; Cell wall; Cytoplasm; Glycoprotein; Glycosidase; Hydrolase;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..308
FT                   /note="Glucan 1,3-beta-glucosidase ARB_02797"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000434662"
FT   ACT_SITE        120
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:O22317"
FT   ACT_SITE        220
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:O22317"
FT   CARBOHYD        126
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   308 AA;  32977 MW;  1F2B8EEF76BF9267 CRC64;
     MRFSTALSLA LAVSPAAVFA AGNLGFSLGV KRPDGQCKDQ ADFEKDFDTL KAHGTTVRTY
     AAADCGSASL ILPAAKSKGF KVVLGIWPDV EESYKADVDA LKKAVPGNED VVAAITVGSE
     TLYRGNFTGP ELLKKIKEVQ KVFPKITIGT ADSWNKYADG TADALIEGGV KYLLVNAFAF
     WQGKAIEQAP KTLFDDLVGA AKRIADKAPQ GSSPYVAIGE TGWPTDGGTD YGAAKAGTKN
     AEKFYKEGVC AMLAWGVDAF YFEAFDEPWK PKSIGDNGNA ADETHWGMYT ADRKPKFNAD
     CKVNKKKD