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Database: UniProt
Entry: A0A087CPE9_9BIFI
LinkDB: A0A087CPE9_9BIFI
Original site: A0A087CPE9_9BIFI 
ID   A0A087CPE9_9BIFI        Unreviewed;       978 AA.
AC   A0A087CPE9;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Putative beta-glucosidase {ECO:0000313|EMBL:KFI85149.1};
DE            EC=3.2.1.21 {ECO:0000313|EMBL:KFI85149.1};
GN   ORFNames=BREU_1971 {ECO:0000313|EMBL:KFI85149.1};
OS   Bifidobacterium reuteri DSM 23975.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=1437610 {ECO:0000313|EMBL:KFI85149.1, ECO:0000313|Proteomes:UP000028984};
RN   [1] {ECO:0000313|EMBL:KFI85149.1, ECO:0000313|Proteomes:UP000028984}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23975 {ECO:0000313|EMBL:KFI85149.1,
RC   ECO:0000313|Proteomes:UP000028984};
RA   Ventura M., Milani C., Lugli G.A.;
RT   "Genomics of Bifidobacteria.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC       {ECO:0000256|ARBA:ARBA00005336, ECO:0000256|RuleBase:RU361161}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KFI85149.1}.
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DR   EMBL; JGZK01000010; KFI85149.1; -; Genomic_DNA.
DR   RefSeq; WP_044089283.1; NZ_JGZK01000010.1.
DR   AlphaFoldDB; A0A087CPE9; -.
DR   STRING; 1437610.BREU_1971; -.
DR   eggNOG; COG1472; Bacteria.
DR   OrthoDB; 3187562at2; -.
DR   Proteomes; UP000028984; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008422; F:beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR   Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR026891; Fn3-like.
DR   InterPro; IPR019800; Glyco_hydro_3_AS.
DR   InterPro; IPR002772; Glyco_hydro_3_C.
DR   InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR   InterPro; IPR001764; Glyco_hydro_3_N.
DR   InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR42715:SF10; BETA-GLUCOSIDASE F-RELATED; 1.
DR   Pfam; PF14310; Fn3-like; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   Pfam; PF01915; Glyco_hydro_3_C; 1.
DR   PRINTS; PR00133; GLHYDRLASE3.
DR   SMART; SM01217; Fn3_like; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR   PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|RuleBase:RU361161, ECO:0000313|EMBL:KFI85149.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028984};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        56..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        930..948
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          444..518
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   978 AA;  106364 MW;  E7577D6C75EE7A00 CRC64;
     MLSINWSDVW NVIASIAPQL IAIAVVFVLA LALTIGVNKK TVKNVGTRKL IHSESWLVFL
     VAVVVAVSMM LFGPLASLLN SATATKYELS QTTISNANKL AKEIQAEAIT MLKNEDGNLP
     LANKKVNVFG WGSTNPVYGG TGSGSMNQNY KTTSLLDGLK EAGIETNADL SKLYTDYRAD
     RPVVAMAEQD WTLPEVPADQ YSDSLISKAK SFSDEAVVVI TRVGGEGADL PTNMKAKGIT
     YTNNSKDYED FKDGESFLEL SQTEKNMIDL VTKNFDKVTV VYNGANAFEL GFVDQYPQIK
     SVLWCPPAGQ TGFSALGDVL SGETNPSGKT SDTFIKDLTQ QPSYNNFGDF KYDNMSEFPT
     ENFEEGETSP AFVNYAEGIY VGYKYWETAA DEGAINYDDY VQYPFGYGLS YTTFDQKMGD
     VTYSGGKVSF DVTVTNTGDV AGKDVVETYY NPPYTNGGIE KASANLVAFE KTKELAPGES
     ETVKISFDDD DMASYDSKNA KAYVLEKGDY DISIQSDSHT TIAEQTITVG DTITYDSDSN
     THNGDKTVAT NVFDDASGDE LGVTYLSRAD HFANYAKATA APTNYTLPED LKADFRNNSN
     YKASETNNDS DEMPTTGAKN GVRLADLTGK DYDDPLWDQL LDQLTFDEMD NLIAFGGYGT
     QAVNSIGKIA LTDVDGPASL NNNFTGVGSI GFPSSTSVAC TWNKDLAKQF GDGIGNMAHD
     MHVAGWYAPA MNIHRNAFAG RNFEYFSEDA LLSGTMASQQ VAGAQAKGVY AFMKHFALND
     QETNRLSELN TWASEQSIRE IYLKPFEMSV KEGGAGAVMS SFNYIGIEWA GSHSGLLNTV
     LRDEWGFRGM VLTDYFGGYG YQNADRAIRG GNDVMLATTD VTNHITDKSA TSIKAMRTAS
     HNILYTAANS WLYENGEPDV PTPIWKTITY VVWGVTAVLV IGLEFLTIQK YLKRRKQATV
     SIAAPAADGG SEAPASEA
//
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