ID   BGLC_BACSU              Reviewed;         477 AA.
AC   P42403;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   27-MAR-2024, entry version 136.
DE   RecName: Full=Aryl-phospho-beta-D-glucosidase BglC;
DE            EC=3.2.1.86;
DE   AltName: Full=6-phospho-beta-glucosidase;
GN   Name=bglC; Synonyms=yckE; OrderedLocusNames=BSU03410;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=7704255; DOI=10.1099/13500872-141-2-277;
RA   Fujishima Y., Yamane K.;
RT   "A 10 kb nucleotide sequence at the 5' flanking region (32 degrees) of
RT   srfAA of the Bacillus subtilis chromosome.";
RL   Microbiology 141:277-279(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=8969502; DOI=10.1099/13500872-142-11-3047;
RA   Yamane K., Kumano M., Kurita K.;
RT   "The 25 degrees-36 degrees region of the Bacillus subtilis chromosome:
RT   determination of the sequence of a 146 kb segment and identification of 113
RT   genes.";
RL   Microbiology 142:3047-3056(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 461-477.
RX   PubMed=2841296; DOI=10.1128/jb.170.8.3703-3710.1988;
RA   Vosman B., Kuiken G., Kooistra J., Venema G.;
RT   "Transformation in Bacillus subtilis: involvement of the 17-kilodalton DNA-
RT   entry nuclease and the competence-specific 18-kilodalton protein.";
RL   J. Bacteriol. 170:3703-3710(1988).
RN   [5]
RP   FUNCTION AS AN ARYL-PHOSPHO-BETA-D-GLUCOSIDASE, DEVELOPMENTAL STAGE,
RP   INDUCTION, AND GENE NAME.
RC   STRAIN=168 / PS832;
RX   PubMed=14652714; DOI=10.1007/s00203-003-0628-2;
RA   Setlow B., Cabrera-Hernandez A., Cabrera-Martinez R.M., Setlow P.;
RT   "Identification of aryl-phospho-beta-D-glucosidases in Bacillus subtilis.";
RL   Arch. Microbiol. 181:60-67(2004).
CC   -!- FUNCTION: Is able to catalyze the hydrolysis of aryl-phospho-beta-D-
CC       glucosides such as 4-methylumbelliferyl-phospho-beta-D-glucopyranoside
CC       (MUG-P), phosphoarbutin and phosphosalicin. Is not essential for growth
CC       on arbutin and salicin as the sole carbon source.
CC       {ECO:0000269|PubMed:14652714}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=6-phospho-beta-D-glucosyl-(1->4)-D-glucose + H2O = D-glucose +
CC         D-glucose 6-phosphate; Xref=Rhea:RHEA:10772, ChEBI:CHEBI:4167,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:58312, ChEBI:CHEBI:61548; EC=3.2.1.86;
CC   -!- DEVELOPMENTAL STAGE: Expressed at a low and constant level during
CC       growth, sporulation, and spore germination.
CC       {ECO:0000269|PubMed:14652714}.
CC   -!- INDUCTION: Is not induced by aryl-beta-D-glucosides such as arbutin,
CC       salicin or 4-methylumbelliferyl-beta-D-glucopyranoside (MUG). Is not
CC       repressed by glucose. {ECO:0000269|PubMed:14652714}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
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DR   EMBL; D30762; BAA06429.1; -; Genomic_DNA.
DR   EMBL; D50453; BAA08975.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12135.1; -; Genomic_DNA.
DR   EMBL; M21672; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; G69760; G69760.
DR   RefSeq; NP_388223.1; NC_000964.3.
DR   RefSeq; WP_003246242.1; NZ_JNCM01000030.1.
DR   AlphaFoldDB; P42403; -.
DR   SMR; P42403; -.
DR   STRING; 224308.BSU03410; -.
DR   CAZy; GH1; Glycoside Hydrolase Family 1.
DR   PaxDb; 224308-BSU03410; -.
DR   EnsemblBacteria; CAB12135; CAB12135; BSU_03410.
DR   GeneID; 938317; -.
DR   KEGG; bsu:BSU03410; -.
DR   PATRIC; fig|224308.179.peg.358; -.
DR   eggNOG; COG2723; Bacteria.
DR   InParanoid; P42403; -.
DR   OrthoDB; 9765195at2; -.
DR   PhylomeDB; P42403; -.
DR   BioCyc; BSUB:BSU03410-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0008706; F:6-phospho-beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008422; F:beta-glucosidase activity; IBA:GO_Central.
DR   GO; GO:0103047; F:methyl beta-D-glucoside 6-phosphate glucohydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016052; P:carbohydrate catabolic process; IBA:GO_Central.
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:SF136; ARYL-PHOSPHO-BETA-D-GLUCOSIDASE BGLC; 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   1: Evidence at protein level;
KW   Carbohydrate metabolism; Glycosidase; Hydrolase; Reference proteome.
FT   CHAIN           1..477
FT                   /note="Aryl-phospho-beta-D-glucosidase BglC"
FT                   /id="PRO_0000063874"
FT   ACT_SITE        170
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        378
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10055"
SQ   SEQUENCE   477 AA;  55140 MW;  64045E7E4C1A10E4 CRC64;
     MIHQHPESFP KHFLWGSASA AYQIEGAWNE DGKGPSVWDV FTKIPGKTFK GTNGEIAVDH
     YHRFKEDVAL MAEMGLKAYR FSVSWPRVFP KGKGEINEAG LAFYDSLIDE LLSHHIEPVL
     TLYHWDLPQA LMDEYGGFES RNIIEDFNHY CITLYKRFGD RVKYWVTLNE QNYNFNHGFI
     TAMHPPGVKD RKRFYEANHI AFLANAKAIE SFREYVPEGK IGPSFAYSPA YPLSSHPEDI
     LAFENAEEFT NNWWLDMYCW GTYPQIPFRC LEKQGWAPTI EAGDMDLLAK GKPDFVGVNY
     YQTITYERNP LDGVSEGKMN TTGQKGTNQE TGIPGVFKTK KNPHLTTSNW DWTIDPIGLR
     IGLRRITSRY QLPVFITENG LGEFDKVEDG TVQDDYRIDY LRSHLEQCRQ AISDGVDLIG
     YCSWSFTDLL SWLNGYQKRY GFVYVNRDEE STSDLKRLKK KSFYWYQDVI KTNGESL
//