ID B7MGE1_ECO45 Unreviewed; 464 AA.
AC B7MGE1;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Cryptic phospho-beta-glucosidase B {ECO:0000313|EMBL:CAR05349.1};
DE EC=3.2.1.86 {ECO:0000313|EMBL:CAR05349.1};
GN Name=bglB {ECO:0000313|EMBL:CAR05349.1};
GN OrderedLocusNames=ECS88_4143 {ECO:0000313|EMBL:CAR05349.1};
OS Escherichia coli O45:K1 (strain S88 / ExPEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585035 {ECO:0000313|EMBL:CAR05349.1, ECO:0000313|Proteomes:UP000000747};
RN [1] {ECO:0000313|Proteomes:UP000000747}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S88 / ExPEC {ECO:0000313|Proteomes:UP000000747};
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC {ECO:0000256|ARBA:ARBA00010838, ECO:0000256|RuleBase:RU003690}.
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DR EMBL; CU928161; CAR05349.1; -; Genomic_DNA.
DR RefSeq; WP_000643257.1; NC_011742.1.
DR AlphaFoldDB; B7MGE1; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR KEGG; ecz:ECS88_4143; -.
DR HOGENOM; CLU_001859_0_2_6; -.
DR Proteomes; UP000000747; Chromosome.
DR GO; GO:0008706; F:6-phospho-beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0103047; F:methyl beta-D-glucoside 6-phosphate glucohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001360; Glyco_hydro_1.
DR InterPro; IPR018120; Glyco_hydro_1_AS.
DR InterPro; IPR033132; Glyco_hydro_1_N_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR10353:SF348; 6-PHOSPHO-BETA-GLUCOSIDASE ASCB-RELATED; 1.
DR PANTHER; PTHR10353; GLYCOSYL HYDROLASE; 1.
DR Pfam; PF00232; Glyco_hydro_1; 1.
DR PRINTS; PR00131; GLHYDRLASE1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR PROSITE; PS00572; GLYCOSYL_HYDROL_F1_1; 1.
DR PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU004468, ECO:0000313|EMBL:CAR05349.1};
KW Hydrolase {ECO:0000256|RuleBase:RU004468, ECO:0000313|EMBL:CAR05349.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000747}.
FT ACT_SITE 361
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ SEQUENCE 464 AA; 52580 MW; 089CDD101305A92C CRC64;
MKAFPETFLW GGATAANQVE GAWQEDGKGI TTSDLQPHGV MGKMEPRILG KENIKDVAID
FYHRYPEDIA LFAEMGFTCL RISIAWARIF PQGDEAEPNE AGLAFYERLF DEMAQAGIKP
LVTLSHYEMP YGLVKNYGGW ANRAVIDHFE HYARTVFTRY QHKVALWLTF NEINMSLHAP
FTGVGLAEES GEAEVYQAIH HQLVASARAV KACHSLIPEA KIGNMLLGGL VYPLTCQPQD
MLQAMEENRR WMFFGDVQAR GQYPGYMQRF FRDHNITIEM TESDAEDLKH TVDFISFSYY
MTGCVSHDES INKNAQGNIL NMIPNPHLKS SEWGWQIDPV GLRILLNTLW DRYQKPLFIV
ENGLGAKDSV EVDGSIQDDY RIAYLNDHLV QVNEAIADGV DIMGYTSWGP IDLVSASHSQ
MSKRYGFIYV DRDDNGEGSL TRTRKKSFGW YAEVIKTRGL SLKK
//
