BGL2_CANAL
ID BGL2_CANAL Reviewed; 308 AA.
AC Q5AMT2; A0A1D8PLI1;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 2.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Glucan 1,3-beta-glucosidase BGL2;
DE EC=3.2.1.58;
DE AltName: Full=Exo-1,3-beta-glucanase;
DE Flags: Precursor;
GN Name=BGL2; Synonyms=BGL21; OrderedLocusNames=CAALFM_C402250CA;
GN ORFNames=CaO19.12034, CaO19.4565;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP PROTEIN SEQUENCE OF 19-26, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR
RP LOCATION, AND INDUCTION.
RX PubMed=19013773; DOI=10.1016/j.ijantimicag.2008.08.021;
RA Angiolella L., Vitali A., Stringaro A., Mignogna G., Maras B., Bonito M.,
RA Colone M., Palamara A.T., Cassone A.;
RT "Localisation of Bgl2p upon antifungal drug treatment in Candida
RT albicans.";
RL Int. J. Antimicrob. Agents 33:143-148(2009).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=7851411; DOI=10.1111/j.1432-1033.1995.tb20399.x;
RA Goldman R.C., Sullivan P.A., Zakula D., Capobianco J.O.;
RT "Kinetics of beta-1,3 glucan interaction at the donor and acceptor sites of
RT the fungal glucosyltransferase encoded by the BGL2 gene.";
RL Eur. J. Biochem. 227:372-378(1995).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=9043114; DOI=10.1099/00221287-143-2-367;
RA Sarthy A.V., McGonigal T., Coen M., Frost D.J., Meulbroek J.A.,
RA Goldman R.C.;
RT "Phenotype in Candida albicans of a disruption of the BGL2 gene encoding a
RT 1,3-beta-glucosyltransferase.";
RL Microbiology 143:367-376(1997).
RN [7]
RP IDENTIFICATION AS AN IMMUNOGENIC PROTEIN.
RX PubMed=10344278;
RX DOI=10.1002/(sici)1522-2683(19990101)20:4/5<1001::aid-elps1001>3.0.co;2-l;
RA Pitarch A., Pardo M., Jimenez A., Pla J., Gil C., Sanchez M., Nombela C.;
RT "Two-dimensional gel electrophoresis as analytical tool for identifying
RT Candida albicans immunogenic proteins.";
RL Electrophoresis 20:1001-1010(1999).
RN [8]
RP INDUCTION.
RX PubMed=15820985; DOI=10.1093/jac/dki088;
RA Copping V.M.S., Barelle C.J., Hube B., Gow N.A.R., Brown A.J.P., Odds F.C.;
RT "Exposure of Candida albicans to antifungal agents affects expression of
RT SAP2 and SAP9 secreted proteinase genes.";
RL J. Antimicrob. Chemother. 55:645-654(2005).
RN [9]
RP IDENTIFICATION AS AN IMMUNOGENIC PROTEIN.
RX PubMed=16195222; DOI=10.1074/mcp.m500243-mcp200;
RA Pitarch A., Jimenez A., Nombela C., Gil C.;
RT "Decoding serological response to Candida cell wall immunome into novel
RT diagnostic, prognostic, and therapeutic candidates for systemic candidiasis
RT by proteomic and bioinformatic analyses.";
RL Mol. Cell. Proteomics 5:79-96(2006).
RN [10]
RP IDENTIFICATION AS AN IMMUNOGENIC PROTEIN.
RX PubMed=18322056; DOI=10.1128/jcm.02018-07;
RA Clancy C.J., Nguyen M.L., Cheng S., Huang H., Fan G., Jaber R.A.,
RA Wingard J.R., Cline C., Nguyen M.H.;
RT "Immunoglobulin G responses to a panel of Candida albicans antigens as
RT accurate and early markers for the presence of systemic candidiasis.";
RL J. Clin. Microbiol. 46:1647-1654(2008).
RN [11]
RP INDUCTION.
RX PubMed=19527170; DOI=10.1086/599838;
RA Nett J.E., Lepak A.J., Marchillo K., Andes D.R.;
RT "Time course global gene expression analysis of an in vivo Candida
RT biofilm.";
RL J. Infect. Dis. 200:307-313(2009).
RN [12]
RP INDUCTION.
RX PubMed=20402792; DOI=10.1111/j.1567-1364.2010.00626.x;
RA Li X., Du W., Zhao J., Zhang L., Zhu Z., Jiang L.;
RT "The MAP kinase-activated protein kinase Rck2p regulates cellular responses
RT to cell wall stresses, filamentation and virulence in the human fungal
RT pathogen Candida albicans.";
RL FEMS Yeast Res. 10:441-451(2010).
RN [13]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22876186; DOI=10.1371/journal.ppat.1002848;
RA Taff H.T., Nett J.E., Zarnowski R., Ross K.M., Sanchez H., Cain M.T.,
RA Hamaker J., Mitchell A.P., Andes D.R.;
RT "A Candida biofilm-induced pathway for matrix glucan delivery: implications
RT for drug resistance.";
RL PLoS Pathog. 8:E1002848-E1002848(2012).
CC -!- FUNCTION: Cell wall glucan 1,3-beta-glucosidase involved in cell wall
CC biosynthesis and virulence. Crucial for delivery of beta-1,3-glucan to
CC the biofilm matrix and for accumulation of mature matrix biomass. Plays
CC a role as a major antigen in human systemic candidiasis patients.
CC {ECO:0000269|PubMed:22876186, ECO:0000269|PubMed:7851411,
CC ECO:0000269|PubMed:9043114}.
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:0000269|PubMed:7851411};
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000269|PubMed:19013773}. Cytoplasm {ECO:0000269|PubMed:19013773}.
CC Note=Tightly bound to cell wall. A fraction of unprecessed protein is
CC found in the cytoplasm.
CC -!- INDUCTION: Induced during biofilm formation and by fluconazole and
CC micafungin. Expression is also regulated by RCK2.
CC {ECO:0000269|PubMed:15820985, ECO:0000269|PubMed:19013773,
CC ECO:0000269|PubMed:19527170, ECO:0000269|PubMed:20402792}.
CC -!- DISRUPTION PHENOTYPE: Exhibits diminished extracellular biofilm
CC material, renders cells more dependent on chitin for wall integrity,
CC and attenuates virulence in mice. {ECO:0000269|PubMed:22876186,
CC ECO:0000269|PubMed:9043114}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 17 family. {ECO:0000305}.
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DR EMBL; CP017626; AOW28996.1; -; Genomic_DNA.
DR RefSeq; XP_722637.2; XM_717544.2.
DR AlphaFoldDB; Q5AMT2; -.
DR SMR; Q5AMT2; -.
DR BioGRID; 1218576; 1.
DR STRING; 237561.Q5AMT2; -.
DR PRIDE; Q5AMT2; -.
DR GeneID; 3635691; -.
DR KEGG; cal:CAALFM_C402250CA; -.
DR CGD; CAL0000186956; BGL2.
DR VEuPathDB; FungiDB:C4_02250C_A; -.
DR eggNOG; ENOG502QQE6; Eukaryota.
DR HOGENOM; CLU_028820_2_0_1; -.
DR InParanoid; Q5AMT2; -.
DR OMA; WKPDTSG; -.
DR OrthoDB; 966331at2759; -.
DR PRO; PR:Q5AMT2; -.
DR Proteomes; UP000000559; Chromosome 4.
DR GO; GO:0009986; C:cell surface; IDA:CGD.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IDA:CGD.
DR GO; GO:1903561; C:extracellular vesicle; IDA:CGD.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:CGD.
DR GO; GO:0030445; C:yeast-form cell wall; IDA:CGD.
DR GO; GO:0042124; F:1,3-beta-glucanosyltransferase activity; IMP:CGD.
DR GO; GO:0042973; F:glucan endo-1,3-beta-D-glucosidase activity; IBA:GO_Central.
DR GO; GO:0004338; F:glucan exo-1,3-beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0042123; F:glucanosyltransferase activity; IDA:CGD.
DR GO; GO:0044406; P:adhesion of symbiont to host; IDA:CGD.
DR GO; GO:0051701; P:biological process involved in interaction with host; IMP:CGD.
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; IMP:CGD.
DR GO; GO:0044407; P:single-species biofilm formation in or on host organism; IMP:CGD.
DR GO; GO:0044011; P:single-species biofilm formation on inanimate substrate; IMP:CGD.
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; Cytoplasm;
KW Direct protein sequencing; Glycoprotein; Glycosidase; Hydrolase;
KW Reference proteome; Secreted; Signal; Virulence.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:19013773"
FT CHAIN 19..308
FT /note="Glucan 1,3-beta-glucosidase BGL2"
FT /id="PRO_0000428632"
FT ACT_SITE 119
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O22317"
FT ACT_SITE 228
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O22317"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 308 AA; 33670 MW; 0C9100BBEB6F8EF4 CRC64;
MQIKFLTTLA TVLTSVAAMG DLAFNLGVKN DDGTCKDVST FEGDLDFLKS HSKIIKTYAV
SDCNTLQNLG PAAEAEGFQI QLGIWPNDDA HFEAEKEALQ NYLPKISVST IKIFLVGSEA
LYREDLTASE LASKINEIKD LVKGIKDKNG KSYSSVPVGT VDSWNVLVDG ASKPAIDAAD
VVYSNSFSYW QKNSQANASY SLFDDVMQAL QTLQTAKGST DIEFWVGETG WPTDGSSYGD
SVPSVENAAD QWQKGICALR AWGINVAVYE AFDEAWKPDT SGTSSVEKHW GVWQSDKTLK
YSIDCKFN
