ID   BGAL_LACHE              Reviewed;         628 AA.
AC   Q7WTB4;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Beta-galactosidase large subunit;
DE            Short=Beta-gal large subunit;
DE            EC=3.2.1.23;
DE   AltName: Full=Lactase large subunit;
GN   Name=lacL;
OS   Lactobacillus helveticus (Lactobacillus suntoryeus).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=1587;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TRANSCRIPTIONAL REGULATION.
RC   STRAIN=ATCC 15009 / DSM 20075 / BCRC 12936 / JCM 1120 / NBRC 15019 / NCIMB
RC   11971 / NRRL B-4526 / Lh12;
RX   PubMed=12788721; DOI=10.1128/aem.69.6.3238-3243.2003;
RA   Fortina M.G., Ricci G., Mora D., Guglielmetti S., Manachini P.L.;
RT   "Unusual organization for lactose and galactose gene clusters in
RT   Lactobacillus helveticus.";
RL   Appl. Environ. Microbiol. 69:3238-3243(2003).
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   -!- SUBUNIT: Heterodimer of a large and a small subunit. {ECO:0000250}.
CC   -!- INDUCTION: By lactose. {ECO:0000269|PubMed:12788721}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family. {ECO:0000305}.
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DR   EMBL; AJ512877; CAD55499.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7WTB4; -.
DR   SMR; Q7WTB4; -.
DR   STRING; 326425.lhe_1442; -.
DR   CAZy; GH2; Glycoside Hydrolase Family 2.
DR   eggNOG; COG3250; Bacteria.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016052; P:carbohydrate catabolic process; IEA:UniProt.
DR   Gene3D; 2.60.40.10; -; 1.
DR   InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
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   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   SUPFAM; SSF49303; SSF49303; 1.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS00719; GLYCOSYL_HYDROL_F2_1; 1.
DR   PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
PE   2: Evidence at transcript level;
KW   Glycosidase; Hydrolase.
FT   CHAIN           1..628
FT                   /note="Beta-galactosidase large subunit"
FT                   /id="PRO_0000057667"
FT   ACT_SITE        468
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        536
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   628 AA;  73479 MW;  A4BBC9B78A84517A CRC64;
     MQANINWLDN PEVFRVNQLP AHSDHPFFRD YREWQKQHSS YQQSLNGKWK FHFSANPMDR
     PQDFYQRDFD SSNFDSIPVP SEIELSNYTQ NQYINVLFPW EGKIFRRPAY ALDPNDHEEG
     SFSKGADNTV GSYLKRFDLS SALIGKDVHI KFEGVEQAMY VWLNGHFVGY AEDSFTPSEF
     DLTPYIQDKD NLLAVEVFKH STASWLEDQD MFRFSGIFRS VELLGIPATH LMDMDLKPRV
     ADNYQDGIFN LKLHFIGKKA GSFHLLVKDI KGHTLLEKNE DIKENVQINN EKFENVHLWN
     NHDPYLYQLL IEVYDEQQNL LELIPFQFGF RRIEISPEKV VLLNGKRLII NGVNRHEWDA
     KRGRSITMSD MTTDINTFKE NNINAVRTCH YPNQIPWYYL CDQNGIYVMA ENNLESHGTW
     QKMGEIEPSD NVPGSIPQWK EAVIDRARIN YETFKNHTSI LFWSLGNESY AGDNIIAMNE
     FYKSHDDTRL VHYEGVVHRP ELKDKISDVE SCMYLPPKKV EEYLQNDPPK PFMECEYMHD
     MGNSDGGMGS YIKLLDKYPQ YFGGFIWDFI DQALLVHDEI SGHDVLRYGG DFDDRHSDYE
     FSGDGLMFAD RTPKPAMQEV RYYYGLHK