ID   E8Q0N9_ECOLW            Unreviewed;       765 AA.
AC   E8Q0N9;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN   Name=bglX {ECO:0000313|EMBL:ADT75770.1};
GN   OrderedLocusNames=ECW_m2334 {ECO:0000313|EMBL:ADT75770.1};
OS   Escherichia coli (strain ATCC 9637 / CCM 2024 / DSM 1116 / LMG 11080 / NBRC
OS   13500 / NCIMB 8666 / NRRL B-766 / W).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=566546 {ECO:0000313|EMBL:ADT75770.1, ECO:0000313|Proteomes:UP000008525};
RN   [1] {ECO:0000313|EMBL:ADT75770.1, ECO:0000313|Proteomes:UP000008525}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9637 / CCM 2024 / DSM 1116 / LMG 11080 / NBRC 13500 /
RC   NCIMB 8666 / NRRL B-766 / W {ECO:0000313|Proteomes:UP000008525};
RX   PubMed=21208457; DOI=10.1186/1471-2164-12-9;
RA   Archer C.T., Kim J.F., Jeong H., Park J.H., Vickers C.E., Lee S.Y.,
RA   Nielsen L.K.;
RT   "The genome sequence of E. coli W (ATCC 9637): comparative genome analysis
RT   and an improved genome-scale reconstruction of E. coli.";
RL   BMC Genomics 12:9-9(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal, non-reducing beta-D-glucosyl residues
CC         with release of beta-D-glucose.; EC=3.2.1.21;
CC         Evidence={ECO:0000256|ARBA:ARBA00000448};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC       {ECO:0000256|ARBA:ARBA00005336, ECO:0000256|RuleBase:RU361161}.
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DR   EMBL; CP002185; ADT75770.1; -; Genomic_DNA.
DR   RefSeq; WP_000871517.1; NZ_WBMH01000066.1.
DR   AlphaFoldDB; E8Q0N9; -.
DR   GeneID; 75206379; -.
DR   KEGG; elw:ECW_m2334; -.
DR   PATRIC; fig|566546.30.peg.2376; -.
DR   Proteomes; UP000008525; Chromosome.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
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; PTHR30620:SF121; PERIPLASMIC BETA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR30620; PERIPLASMIC BETA-GLUCOSIDASE-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|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361161};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..765
FT                   /note="beta-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5009953704"
FT   DOMAIN          685..754
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   765 AA;  83534 MW;  C27AB4DC8BA64620 CRC64;
     MKWLCSVGIA VSLALQPALA DDLFGNHPLT PEARDAFVTE LLKKMTVDEK IGQLRLISVG
     PDNPKEAIRE MIKDGQVGAI FNTVTRQDIR AMQDQVMELS RLKIPLFFAY DVLHGQRTVF
     PISLGLASSF NLDAVKTVGR VSAYEAADDG LNMTWAPMVD VSRDPRWGRA SEGFGEDTYL
     TSTMGKTMVE AMQGKSPADR YSVMTSVKHF AAYGAVEGGK EYNTVDMSPQ RLFNDYMPPY
     KAGLDAGSGA VMVALNSLNG TPATSDSWLL KDVLRDQWGF KGITVSDHGA IKELIKHGTA
     ADPEDAVRVA LKSGINMSMS DEYYSKYLPG LIKSGKVTME ELDDAARHVL NVKYDMGLFN
     DPYSHLGPKE SDPVDTNAES RLHRKEAREV ARESLVLLKN RLETLPLKKS ATIAVVGPLA
     DSKRDVMGSW SAAGVADQSV TVLTGIKNSV GENGKVLYAK GANVTSDKGI IDFLNQYEEA
     VKVDPRSPQE MIDEAVQTAK QSDVVVAVVG EAQGMAHEAS SRTDITIPQS QRDLIAALKA
     TGKPLVLVLM NGRPLALVKE DQQADAILET WFAGTEGGNA IADVLFGDYN PSGKLPMSFP
     RSVGQIPVYY SHLNTGRPYN ADKPNKYTSR YFDEANGALY PFGYGLSYTT FTVSDVKLSA
     PTMKRDGKVT ASVQVTNTGK REGATVVQMY LQDVTASMSR PVKQLKGFEK ITLKPGETQT
     VSFPIDIEAL KFWNQQMKYD AEPGKFNVFI GTDSARVKKG EFELL
//