ID   BGAL_LATSK              Reviewed;         625 AA.
AC   Q48846;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 83.
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   Latilactobacillus sakei (Lactobacillus sakei).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Latilactobacillus.
OX   NCBI_TaxID=1599;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 15521 / DSM 20017 / JCM 1157 / CCUG 30501 / CIP 103139 / KCTC
RC   3603 / NBRC 15893 / NCIMB 13090 / T.S;
RX   PubMed=8574399; DOI=10.1099/13500872-141-12-3059;
RA   Obst M., Meding E.R., Vogel R.F., Hammes W.P.;
RT   "Two genes encoding the beta-galactosidase of Lactobacillus sake.";
RL   Microbiology 141:3059-3066(1995).
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.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 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; X82287; CAA57730.1; -; Genomic_DNA.
DR   RefSeq; WP_025015980.1; NZ_CP048116.1.
DR   AlphaFoldDB; Q48846; -.
DR   SMR; Q48846; -.
DR   CAZy; GH2; Glycoside Hydrolase Family 2.
DR   GeneID; 57132632; -.
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   3: Inferred from homology;
KW   Glycosidase; Hydrolase.
FT   CHAIN           1..625
FT                   /note="Beta-galactosidase large subunit"
FT                   /id="PRO_0000057670"
FT   ACT_SITE        465
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        533
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   625 AA;  72457 MW;  C658A3C46136B886 CRC64;
     MQPNIQWLDT PAVFRVGQLP AHSDHRYYAT LAEMAQQQSS FEQSLNGTWQ FHYSVNAASR
     PKSFYELAFD AQDFEPITVP QHIELAGYEQ LHYINTMYPW EGHYYRRPAF STSDDKQHLG
     MFSEADYNPV GSYLHHFDLT PALRNQRVII RFEGVEQAMY VWLNGQFIGY AEDSFTPSEF
     DLTPYLKETD NCLAVEVHKR SSAAFIEDQD FFRFFGIFRD VKLLAKPRTH LEDLWVIPEY
     DVVQQTGQVK LRLQFSGDEN RVHLRIRDQH QIILTADLTS GAQVNDLYKM PELVQAWSNQ
     TPNLYTLELE VVDQAGETIE ISQQPFGFRK IEIKDKVMLL NGKRLVINGV NRHEWHPETG
     RTITAEDEAW DIACMQRNHI NAVRTSHYPD RLSFYNGCDQ AGIYMMAETN LESHGSWQKM
     GAVEPSWNVP GSYDEWEAAT LDRARTNFET FKNHVSILFW SLGNESYAGS VLEKMNAYYK
     QQDPTRLVHY EGVFRAPEYK ATISDVESRM YATPAEIKAY LDNAPQKPFI LCEYMHDMGN
     SLGGMQSYID LLSQYDMYQG GFIWDFIDQA LLVTDPVTGQ RELRYGGDFD DRPSDYEFSG
     DGLVFATRDE KPAMQEVRYY YGEHK