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Database: UniProt/TrEMBL
Entry: A9QSQ8_LACLK
LinkDB: A9QSQ8_LACLK
Original site: A9QSQ8_LACLK 
ID   A9QSQ8_LACLK            Unreviewed;       483 AA.
AC   A9QSQ8;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   24-JAN-2024, entry version 82.
DE   SubName: Full=6-phospho-beta-glucosidase {ECO:0000313|EMBL:ABX75744.1};
DE            EC=3.2.1.86 {ECO:0000313|EMBL:ABX75744.1};
GN   Name=pbg {ECO:0000313|EMBL:ABX75744.1};
GN   OrderedLocusNames=LLKF_0673 {ECO:0000313|EMBL:ABX75744.1};
OS   Lactococcus lactis subsp. lactis (strain KF147).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=684738 {ECO:0000313|EMBL:ABX75744.1, ECO:0000313|Proteomes:UP000001886};
RN   [1] {ECO:0000313|EMBL:ABX75744.1, ECO:0000313|Proteomes:UP000001886}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KF147 {ECO:0000313|EMBL:ABX75744.1,
RC   ECO:0000313|Proteomes:UP000001886};
RX   PubMed=18039825; DOI=10.1128/AEM.01850-07;
RA   Siezen R.J., Starrenburg M.J., Boekhorst J., Renckens B., Molenaar D.,
RA   van Hylckama Vlieg J.E.;
RT   "Genome-scale genotype-phenotype matching of two Lactococcus lactis
RT   isolates from plants identifies mechanisms of adaptation to the plant
RT   niche.";
RL   Appl. Environ. Microbiol. 74:424-436(2008).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC       {ECO:0000256|ARBA:ARBA00010838, ECO:0000256|RuleBase:RU003690}.
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DR   EMBL; CP001834; ABX75744.1; -; Genomic_DNA.
DR   RefSeq; WP_012897375.1; NC_013656.1.
DR   AlphaFoldDB; A9QSQ8; -.
DR   CAZy; GH1; Glycoside Hydrolase Family 1.
DR   KEGG; llk:LLKF_0673; -.
DR   HOGENOM; CLU_001859_0_1_9; -.
DR   OMA; ICTINEP; -.
DR   Proteomes; UP000001886; 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:SF122; 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|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU004468};
KW   Hydrolase {ECO:0000256|RuleBase:RU004468, ECO:0000313|EMBL:ABX75744.1}.
FT   ACT_SITE        380
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ   SEQUENCE   483 AA;  55659 MW;  E5D13E27F6F6D83B CRC64;
     MTFKPDFLWG GATAANQFEG AFLEDGRGWS TADTAKYYPH SDKTSMDSLM DPMTTSKIEF
     AKKDLEGIYP KRYGIDFYHH FKEDIALFAE MGFKTFRMSI SWSRIFPNGD ELEPNETGLK
     FYDQVFDELL KYHIEPLVTM SHYEFPLGLA LKQNGWESRE TVDHFEKYAR VILNRYKDKV
     KYWLTFNEIN IIGITGYLSG GLLADKTQNM LQSQFQAAHH QFLASALAVK ACHEIIPEAK
     IGCMLARMET YPETCNPLDV MATIDSDHAN LFYSDVQVRG YYPTYMKKVF KDHHLKIIKE
     SGDDQLLKEG KVDFMSFSYY MSSISSSSEE GEVIGGNFTQ TKKNPYLKSS DWGWQIDPVG
     LRITLHKLYD RYQVPLFVVE NGLGAHDTLE EDGTIHDNYR IDYLREHIKQ MGIAIDEGVD
     LMGYTPWGCI DLVSASTSEM SKRYGFIYVD QDNEGEGSLK RFKKDSFYWY KSVIQSNGET
     LYK
//
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