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Database: UniProt
Entry: G5Q4S3_SALMO
LinkDB: G5Q4S3_SALMO
Original site: G5Q4S3_SALMO 
ID   G5Q4S3_SALMO            Unreviewed;       755 AA.
AC   G5Q4S3;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN   ORFNames=LTSEMON_3091 {ECO:0000313|EMBL:EHC77663.1};
OS   Salmonella enterica subsp. enterica serovar Montevideo str. S5-403.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=913242 {ECO:0000313|EMBL:EHC77663.1, ECO:0000313|Proteomes:UP000003221};
RN   [1] {ECO:0000313|EMBL:EHC77663.1, ECO:0000313|Proteomes:UP000003221}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S5-403 {ECO:0000313|EMBL:EHC77663.1,
RC   ECO:0000313|Proteomes:UP000003221};
RX   PubMed=21859443; DOI=10.1186/1471-2164-12-425;
RA   den Bakker H.C., Moreno Switt A.I., Govoni G., Cummings C.A., Ranieri M.L.,
RA   Degoricija L., Hoelzer K., Rodriguez-Rivera L.D., Brown S., Bolchacova E.,
RA   Furtado M.R., Wiedmann M.;
RT   "Genome sequencing reveals diversification of virulence factor content and
RT   possible host adaptation in distinct subpopulations of Salmonella
RT   enterica.";
RL   BMC Genomics 12:425-425(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}.
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:EHC77663.1}.
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DR   EMBL; AFCS01000732; EHC77663.1; -; Genomic_DNA.
DR   AlphaFoldDB; G5Q4S3; -.
DR   PATRIC; fig|913242.3.peg.2673; -.
DR   Proteomes; UP000003221; Unassembled WGS sequence.
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}.
FT   DOMAIN          675..744
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
FT   REGION          355..375
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   755 AA;  82321 MW;  5DFFCD7B7F80B14A CRC64;
     MSLAMQPALA ENLFGNHPLT PEARDAFVTD LLKKMTVDEK IGQLRLISVG PDNPKEAIRE
     MIKDGQVGAI FNTVTRQDIR QMQDQVMALS RLKIPLFFAY DVVHGQRTVF PISLGLASSF
     NLDAVRTVGR VSAYEAADDG LNMTWAPMVD VSRDPRWGRA SEGFGEDTYL TSIMGETMVK
     AMQGKSPADR YSVMTSVKHF AAYGAVEGGK EYNTVDMSSQ RLFNDYMPPY KAGLDAGSGA
     VMVALNSLNG TPATSDSWLL KDVLRDEWGF KGITVSDHGA IKELIKHGTA ADPEDAVRVA
     LKAGVDMSMA DEYYSKYLPG LIKSGKVTMA ELDDATRHVL NVKYDMGLFN DPYSHLGPKE
     SDPADTNAES RLHRKEAREV ARESVVLLKN RLETLPLKKS GTIAVVGPLA DSQRDVMGSW
     SAAGVANQSV TVLAGIQNAV GDGAKILYAK GANITNDKGI VDFLNLYEEA VKIDPRSPQA
     MIDEAVQAAK QADVVVAVVG ESQGMAHEAS SRTNITIPQS QRDLITALKA TGKPLVLVLM
     NGRPLALVKE DQQADAILET WFAGTEGGNA IADVLFGDYN PSGKLPISFP RSVGQIPVYY
     SHLNTGRPYN PEKPNKYTSR YFDEANGPLY PFGYGLSYTT FTVSDVTLSS PTMQRDGKVT
     ASVEVTNTGK REGATVIQMY LQDVTASMSR PVKQLKGFEK ITLKPGERKT VSFPIDIEAL
     KFWNQQMKYD AEPGKFNVFI GVDSARVKQG SFELL
//
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