BGL2_YEAST
ID BGL2_YEAST Reviewed; 313 AA.
AC P15703; D6VV59;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Glucan 1,3-beta-glucosidase;
DE EC=3.2.1.58;
DE AltName: Full=Exo-1,3-beta-glucanase;
DE AltName: Full=GP29;
DE AltName: Full=Soluble cell wall protein 9;
DE Flags: Precursor;
GN Name=BGL2; Synonyms=SCW9; OrderedLocusNames=YGR282C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=2509432; DOI=10.1128/jb.171.11.6259-6264.1989;
RA Klebl F., Tanner W.;
RT "Molecular cloning of a cell wall exo-beta-1,3-glucanase from Saccharomyces
RT cerevisiae.";
RL J. Bacteriol. 171:6259-6264(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9090054;
RX DOI=10.1002/(sici)1097-0061(19970315)13:3<251::aid-yea63>3.0.co;2-r;
RA Volckaert G., Voet M., Robben J.;
RT "Sequence analysis of a near-subtelomeric 35.4 kb DNA segment on the right
RT arm of chromosome VII from Saccharomyces cerevisiae carrying the MAL1 locus
RT reveals 15 complete open reading frames, including ZUO1, BGL2 and BIO2
RT genes and an ABC transporter gene.";
RL Yeast 13:251-259(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP PROTEIN SEQUENCE OF 24-34, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 96099 / S288c / SEY6210;
RX PubMed=9748433; DOI=10.1128/jb.180.19.5030-5037.1998;
RA Cappellaro C., Mrsa V., Tanner W.;
RT "New potential cell wall glucanases of Saccharomyces cerevisiae and their
RT involvement in mating.";
RL J. Bacteriol. 180:5030-5037(1998).
RN [7]
RP PROTEIN SEQUENCE OF 24-31.
RC STRAIN=ATCC 38531 / Y41;
RX PubMed=8935650; DOI=10.1111/j.1574-6968.1996.tb08073.x;
RA Norbeck J., Blomberg A.;
RT "Protein expression during exponential growth in 0.7 M NaCl medium of
RT Saccharomyces cerevisiae.";
RL FEMS Microbiol. Lett. 137:1-8(1996).
RN [8]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
CC -!- FUNCTION: Glucanases possibly play a role in cell expansion during
CC growth, in cell-cell fusion during mating, and in spore release during
CC sporulation. This enzyme may be involved in beta-glucan degradation and
CC also function biosynthetically as a transglycosylase.
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;
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:9748433}.
CC Note=Tightly bound to cell wall.
CC -!- MISCELLANEOUS: This protein strongly binds to glucan and chitin.
CC -!- MISCELLANEOUS: Present with 45000 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 17 family. {ECO:0000305}.
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DR EMBL; M31072; AAA34648.1; -; Genomic_DNA.
DR EMBL; Z73067; CAA97313.1; -; Genomic_DNA.
DR EMBL; AY558101; AAS56427.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08370.1; -; Genomic_DNA.
DR PIR; A33499; A33499.
DR RefSeq; NP_011798.1; NM_001181411.1.
DR AlphaFoldDB; P15703; -.
DR SMR; P15703; -.
DR BioGRID; 33532; 138.
DR DIP; DIP-6341N; -.
DR IntAct; P15703; 32.
DR MINT; P15703; -.
DR STRING; 4932.YGR282C; -.
DR CAZy; GH17; Glycoside Hydrolase Family 17.
DR CLAE; EXG17B_YEAST; -.
DR iPTMnet; P15703; -.
DR COMPLUYEAST-2DPAGE; P15703; -.
DR MaxQB; P15703; -.
DR PaxDb; P15703; -.
DR PRIDE; P15703; -.
DR EnsemblFungi; YGR282C_mRNA; YGR282C; YGR282C.
DR GeneID; 853199; -.
DR KEGG; sce:YGR282C; -.
DR SGD; S000003514; BGL2.
DR VEuPathDB; FungiDB:YGR282C; -.
DR eggNOG; ENOG502QQE6; Eukaryota.
DR GeneTree; ENSGT00940000176321; -.
DR HOGENOM; CLU_028820_2_0_1; -.
DR InParanoid; P15703; -.
DR OMA; WKPDTSG; -.
DR BioCyc; YEAST:YGR282C-MON; -.
DR PRO; PR:P15703; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P15703; protein.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:SGD.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR GO; GO:0042124; F:1,3-beta-glucanosyltransferase activity; IBA:GO_Central.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR GO; GO:0042973; F:glucan endo-1,3-beta-D-glucosidase activity; IDA:SGD.
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:0071555; P:cell wall organization; IBA:GO_Central.
DR GO; GO:0031505; P:fungal-type cell wall organization; IGI:SGD.
DR InterPro; IPR000490; Glyco_hydro_17.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
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 Cell wall; Cell wall biogenesis/degradation; Chitin-binding;
KW Direct protein sequencing; Glycoprotein; Glycosidase; Hydrolase;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:8935650,
FT ECO:0000269|PubMed:9748433"
FT CHAIN 24..313
FT /note="Glucan 1,3-beta-glucosidase"
FT /id="PRO_0000011896"
FT ACT_SITE 124
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O22317"
FT ACT_SITE 233
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O22317"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 284
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 313 AA; 34119 MW; 118D75528C5AD383 CRC64;
MRFSTTLATA ATALFFTASQ VSAIGELAFN LGVKNNDGTC KSTSDYETEL QALKSYTSTV
KVYAASDCNT LQNLGPAAEA EGFTIFVGVW PTDDSHYAAE KAALQTYLPK IKESTVAGFL
VGSEALYRND LTASQLSDKI NDVRSVVADI SDSDGKSYSG KQVGTVDSWN VLVAGYNSAV
IEASDFVMAN AFSYWQGQTM QNASYSFFDD IMQALQVIQS TKGSTDITFW VGETGWPTDG
TNFESSYPSV DNAKQFWKEG ICSMRAWGVN VIVFEAFDED WKPNTSGTSD VEKHWGVFTS
SDNLKYSLDC DFS
