ID   BGLH_BACSU              Reviewed;         469 AA.
AC   P40740; O32287;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=Aryl-phospho-beta-D-glucosidase BglH;
DE            EC=3.2.1.86;
DE   AltName: Full=6-phospho-beta-glucosidase;
GN   Name=bglH; OrderedLocusNames=BSU39260; ORFNames=N17D;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC   3610 / NRRL NRS-744 / VKM B-501;
RX   PubMed=7883710; DOI=10.1128/jb.177.6.1527-1535.1995;
RA   Le Coq D., Lindner C., Krueger S., Steinmetz M., Stuelke J.;
RT   "New beta-glucoside (bgl) genes in Bacillus subtilis: the bglP gene product
RT   has both transport and regulatory functions similar to those of BglF, its
RT   Escherichia coli homolog.";
RL   J. Bacteriol. 177:1527-1535(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / BGSC1A1;
RX   PubMed=7704263; DOI=10.1099/13500872-141-2-337;
RA   Yoshida K., Sano H., Seki S., Oda M., Fujimura M., Fujita Y.;
RT   "Cloning and sequencing of a 29 kb region of the Bacillus subtilis genome
RT   containing the hut and wapA loci.";
RL   Microbiology 141:337-343(1995).
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: Significantly expressed throughout all stages of
CC       growth or development. {ECO:0000269|PubMed:14652714}.
CC   -!- INDUCTION: Highly up-regulated by aryl-beta-D-glucosides such as
CC       salicin or 4-methylumbelliferyl-beta-D-glucopyranoside (MUG).
CC       {ECO:0000269|PubMed:14652714}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; Z34526; CAA84287.1; -; Genomic_DNA.
DR   EMBL; D31856; BAA06653.1; -; Genomic_DNA.
DR   EMBL; D29985; BAA06257.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15962.2; -; Genomic_DNA.
DR   PIR; H69593; H69593.
DR   RefSeq; NP_391805.2; NC_000964.3.
DR   RefSeq; WP_003243232.1; NZ_JNCM01000034.1.
DR   AlphaFoldDB; P40740; -.
DR   SMR; P40740; -.
DR   STRING; 224308.BSU39260; -.
DR   CAZy; GH1; Glycoside Hydrolase Family 1.
DR   jPOST; P40740; -.
DR   PaxDb; P40740; -.
DR   PRIDE; P40740; -.
DR   EnsemblBacteria; CAB15962; CAB15962; BSU_39260.
DR   GeneID; 937512; -.
DR   KEGG; bsu:BSU39260; -.
DR   PATRIC; fig|224308.179.peg.4250; -.
DR   eggNOG; COG2723; Bacteria.
DR   InParanoid; P40740; -.
DR   OMA; YIAINHY; -.
DR   PhylomeDB; P40740; -.
DR   BioCyc; BSUB:BSU39260-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..469
FT                   /note="Aryl-phospho-beta-D-glucosidase BglH"
FT                   /id="PRO_0000063873"
FT   ACT_SITE        175
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        368
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10055"
FT   CONFLICT        402
FT                   /note="A -> R (in Ref. 1; CAA84287)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   469 AA;  53289 MW;  4C0CA25F964C1CC1 CRC64;
     MSSNEKRFPE GFLWGGAVAA NQVEGAYNEG GKGLSTADVS PNGIMSPFDE SMTSLNLYHN
     GIDFYHRYKE DIALFAEMGF KAFRTSIAWT RIFPNGDEEE PNEEGLRFYD DLFDELLKHH
     IEPVVTISHY EMPLGLVKNY GGWKNRKVIE FYERYAKTVF KRYQHKVKYW MTFNEINVVL
     HAPFTGGGLV FEEGENKLNA MYQAAHHQFV ASALAVKAGH DIIPDSKIGC MIAATTTYPM
     TSKPEDVFAA MENERKTLFF SDVQARGAYP GYMKRYLAEN NIEIEMAEGD EELLKEHTVD
     YIGFSYYMSM AASTDPEELA KSGGNLLGGV KNPYLKSSEW GWQIDPKGLR ITLNTLYDRY
     QKPLFIVENG LGAVDKVEED GTIQDDYRIN YLRDHLIEAR EAIADGVELI GYTSWGPIDL
     VSASTAEMKK RYGFIYVDRD NEGNGTFNRI KKKSFNWYQQ VIATNGESL