ID   BGAL_PRIM3              Reviewed;        1034 AA.
AC   O52847; D5DFH9;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Beta-galactosidase;
DE            Short=Beta-gal;
DE            EC=3.2.1.23;
DE   AltName: Full=Lactase;
GN   Name=bgaM; OrderedLocusNames=BMD_2126;
OS   Priestia megaterium (strain DSM 319 / IMG 1521) (Bacillus megaterium).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Priestia.
OX   NCBI_TaxID=592022;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Strey J.;
RL   Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 319 / IMG 1521;
RX   PubMed=21705586; DOI=10.1128/jb.00449-11;
RA   Eppinger M., Bunk B., Johns M.A., Edirisinghe J.N., Kutumbaka K.K.,
RA   Koenig S.S., Creasy H.H., Rosovitz M.J., Riley D.R., Daugherty S.,
RA   Martin M., Elbourne L.D., Paulsen I., Biedendieck R., Braun C.,
RA   Grayburn S., Dhingra S., Lukyanchuk V., Ball B., Ul-Qamar R., Seibel J.,
RA   Bremer E., Jahn D., Ravel J., Vary P.S.;
RT   "Genome sequences of the biotechnologically important Bacillus megaterium
RT   strains QM B1551 and DSM319.";
RL   J. Bacteriol. 193:4199-4213(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal non-reducing beta-D-galactose residues
CC         in beta-D-galactosides.; EC=3.2.1.23;
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family. {ECO:0000305}.
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DR   EMBL; AJ000733; CAA04267.1; -; Genomic_DNA.
DR   EMBL; CP001982; ADF38979.1; -; Genomic_DNA.
DR   PIR; T30574; T30574.
DR   RefSeq; WP_013082993.1; NC_014103.1.
DR   AlphaFoldDB; O52847; -.
DR   SMR; O52847; -.
DR   CAZy; GH2; Glycoside Hydrolase Family 2.
DR   PRIDE; O52847; -.
DR   EnsemblBacteria; ADF38979; ADF38979; BMD_2126.
DR   KEGG; bmd:BMD_2126; -.
DR   PATRIC; fig|592022.4.peg.2076; -.
DR   HOGENOM; CLU_002346_0_2_9; -.
DR   OMA; DYPQYTN; -.
DR   Proteomes; UP000002365; Chromosome.
DR   GO; GO:0009341; C:beta-galactosidase complex; IEA:InterPro.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0016052; P:carbohydrate catabolic process; IEA:UniProt.
DR   Gene3D; 2.60.40.10; -; 2.
DR   Gene3D; 2.70.98.10; -; 1.
DR   InterPro; IPR004199; B-gal_small/dom_5.
DR   InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR014718; GH-type_carb-bd.
DR   InterPro; IPR006101; Glyco_hydro_2.
DR   InterPro; IPR023232; Glyco_hydro_2_AS.
DR   InterPro; IPR006103; Glyco_hydro_2_cat.
DR   InterPro; IPR023230; Glyco_hydro_2_CS.
DR   InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR   InterPro; IPR006104; Glyco_hydro_2_N.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR032312; LacZ_4.
DR   Pfam; PF02929; Bgal_small_N; 1.
DR   Pfam; PF16353; DUF4981; 1.
DR   Pfam; PF00703; Glyco_hydro_2; 1.
DR   Pfam; PF02836; Glyco_hydro_2_C; 1.
DR   Pfam; PF02837; Glyco_hydro_2_N; 1.
DR   PRINTS; PR00132; GLHYDRLASE2.
DR   SMART; SM01038; Bgal_small_N; 1.
DR   SUPFAM; SSF49303; SSF49303; 2.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   SUPFAM; SSF74650; SSF74650; 1.
DR   PROSITE; PS00719; GLYCOSYL_HYDROL_F2_1; 1.
DR   PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
PE   3: Inferred from homology;
KW   Glycosidase; Hydrolase.
FT   CHAIN           1..1034
FT                   /note="Beta-galactosidase"
FT                   /id="PRO_0000057659"
FT   ACT_SITE        481
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        547
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1034 AA;  118674 MW;  38644C9A649415E9 CRC64;
     MLKTGKKFHY TAPANGYPEW NNNPEIFQLN RSKAHALLMP YQTVEEALKN DRKSSVYYQS
     LNGSWYFHFA ENADGRVKNF FAPEFSYEKW DSISVPSHWQ LQGYDYPQYT NVTYPWVENE
     ELEPPFAPTK YNPVGQYVRT FTPKSEWKDQ PVYISFQGVE SAFYVWINGE FVGYSEDSFT
     PAEFDITSYL QEGENTIAVE VYRWSDASWL EDQDFWRMSG IFRDVYLYST PQVHIYDFSV
     RSSLDNNYED GELSVSADIL NYFEHDTQDL TFEVMLYDAN AQEVLQAPLQ TNLSVSDQRT
     VSLRTHIKSP AKWSAESPNL YTLVLSLKNA AGSIIETESC KVGFRTFEIK NGLMTINGKR
     IVLRGVNRHE FDSVKGRAGI TREDMIHDIL LMKQHNINAV RTSHYPNDSV WYELCNEYGL
     YVIDETNLET HGTWTYLQEG EQKAVPGSKP EWKENVLDRC RSMYERDKNH PSIIIWSLGN
     ESFGGENFQH MYTFFKEKDS TRLVHYEGIF HHRDYDASDI ESTMYVKPAD VERYALMNPK
     KPYILCEYSH AMGNSCGNLY KYWELFDQYP ILQGGFIWDW KDQALQATAE DGTSYLAYGG
     DFGDTPNDGN FCGNGLIFAD GTASPKIAEV KKCYQPVKWT AVDPAKGKFA VQNKHLFTNL
     NAYDFVWTVE KNGELVEKHA SLLNVAPDGT DELTLSYPLY EQENETDEFV LTLSLRLSKD
     TAWASAGYEV AYEQFVLPAK AAMPSVKAAH PALTVDQNEQ TLTVTGTNFT AIFDKRKGQF
     ISYNYERTEL LASGFRPNFW RAVTDNDLGN KLHERCQTWR QASLEQHVKK VTVQPQVDFV
     IISVELALDN SLASCYVTYT LYNDGEMKIE QSLAPSETMP EIPEIGMLFT MNAAFDSLTW
     YGRGPHENYW DRKTGAKLAL HKGSVKEQVT PYLRPQECGN KTDVRWATIT NDQGRGFLIK
     GLPTVELNAL PYSPFELEAY DHFYKLPASD SVTVRVNYKQ MGVGGDDSWQ AKTHPNYTLY
     ANRSYTNTFT LKPL