ID   BGLA_BACSU              Reviewed;         479 AA.
AC   P42973;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Aryl-phospho-beta-D-glucosidase BglA;
DE            EC=3.2.1.86;
DE   AltName: Full=6-phospho-beta-glucosidase;
GN   Name=bglA; OrderedLocusNames=BSU40110;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC   STRAIN=168 / JH642;
RX   PubMed=8125345; DOI=10.1016/0378-1119(94)90735-8;
RA   Zhang J., Aronson A.I.;
RT   "A Bacillus subtilis bglA gene encoding phospho-beta-glucosidase is
RT   inducible and closely linked to a NADH dehydrogenase-encoding gene.";
RL   Gene 140:85-90(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9205843; DOI=10.1093/dnares/4.2.155;
RA   Kasahara Y., Nakai S., Ogasawara N.;
RT   "Sequence analysis of the 36-kb region between gntZ and trnY genes of
RT   Bacillus subtilis genome.";
RL   DNA Res. 4:155-159(1997).
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   FUNCTION AS AN ARYL-PHOSPHO-BETA-D-GLUCOSIDASE, DEVELOPMENTAL STAGE, AND
RP   INDUCTION.
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: Catalyzes the hydrolysis of aryl-phospho-beta-D-glucosides
CC       such as 4-methylumbelliferyl-phospho-beta-D-glucopyranoside (MUG-P),
CC       phosphoarbutin and phosphosalicin. Plays a major role in the
CC       utilization of arbutin or salicin as the sole carbon source. BglA and
CC       BglH are the major proteins contributing to hydrolysis of MUG-P by
CC       extracts of late-exponential-phase or stationary-phase B.subtilis
CC       cells. {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 during stationary-phase and exponential-
CC       phase of growth. {ECO:0000269|PubMed:14652714}.
CC   -!- INDUCTION: Up-regulated by the aryl-beta-D-glucoside salicin.
CC       {ECO:0000269|PubMed:14652714, ECO:0000269|PubMed:8125345}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
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DR   EMBL; L19710; AAA22660.1; -; Genomic_DNA.
DR   EMBL; D78193; BAA11270.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB16048.1; -; Genomic_DNA.
DR   PIR; I39953; I39953.
DR   RefSeq; NP_391891.1; NC_000964.3.
DR   RefSeq; WP_003226994.1; NZ_JNCM01000034.1.
DR   AlphaFoldDB; P42973; -.
DR   SMR; P42973; -.
DR   STRING; 224308.BSU40110; -.
DR   CAZy; GH1; Glycoside Hydrolase Family 1.
DR   jPOST; P42973; -.
DR   PaxDb; P42973; -.
DR   PRIDE; P42973; -.
DR   EnsemblBacteria; CAB16048; CAB16048; BSU_40110.
DR   GeneID; 937718; -.
DR   KEGG; bsu:BSU40110; -.
DR   PATRIC; fig|224308.179.peg.4338; -.
DR   eggNOG; COG2723; Bacteria.
DR   InParanoid; P42973; -.
DR   OMA; NPLFLWT; -.
DR   PhylomeDB; P42973; -.
DR   BioCyc; BSUB:BSU40110-MON; -.
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   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; PTHR10353; 1.
DR   Pfam; PF00232; Glyco_hydro_1; 1.
DR   PRINTS; PR00131; GLHYDRLASE1.
DR   SUPFAM; SSF51445; SSF51445; 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..479
FT                   /note="Aryl-phospho-beta-D-glucosidase BglA"
FT                   /id="PRO_0000063896"
FT   ACT_SITE        176
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        377
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10055"
SQ   SEQUENCE   479 AA;  54841 MW;  FC9FA6131A14257A CRC64;
     MGNMPKDFLW GGALAAHQFE GGWNQGGKGP SVVDVMTAGA HGVPRKITDT IEENEFYPNH
     EAIDFYHRYK EDIALFAEMG LKCLRTSIGW SRIFPKGDEA EPNEAGLQFY DDVFDELLKH
     GIEPVITLSH FEMPLHLARE YGGFRNRKVV DFFVNFAEAC FTRYKDKVKY WMTFNEINNQ
     MDVNNPLFLW TNSGVVVGEN ENAKEVMYQT AHHELVASAL AVAKGKDINP EFQIGAMVSH
     VPIYPFSSNP EDVMLAEEEM RQRYFFPDVQ VRGYYPSYAL KEFEREGYNI TFEDGDDEIL
     RNGTVDYLGF SYYMSTTVKS DVKNDNTGDI VNGGLPNGVE NPYITSSDWG WAIDPTGLRY
     TLNRFYDRYQ IPLFIVENGF GAVDTLEEDG KVHDPERIQY LKSHIEALKK AVTYDGVDLI
     GYTPWGIIDI VSFTTGEMKK RYGMIYVDRD NEGNGSMKRY KKDSFEWYKN VIQTNGEEL