ID   BGAL_LACAC              Reviewed;         628 AA.
AC   O07684; Q5FJ37;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2005, sequence version 2.
DT   27-MAR-2024, entry version 121.
DE   RecName: Full=Beta-galactosidase large subunit {ECO:0000250|UniProtKB:Q02603};
DE            Short=Beta-gal large subunit {ECO:0000250|UniProtKB:Q02603};
DE            EC=3.2.1.23 {ECO:0000250|UniProtKB:Q02603};
GN   Name=lacL; OrderedLocusNames=LBA1467;
OS   Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=272621;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=JCM 1229 / KCTC 3168;
RA   Suzuki M., Saito T., Konno K., Kamio Y., Itoh T.;
RL   Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700396 / NCK56 / N2 / NCFM;
RX   PubMed=15671160; DOI=10.1073/pnas.0409188102;
RA   Altermann E., Russell W.M., Azcarate-Peril M.A., Barrangou R., Buck B.L.,
RA   McAuliffe O., Souther N., Dobson A., Duong T., Callanan M., Lick S.,
RA   Hamrick A., Cano R., Klaenhammer T.R.;
RT   "Complete genome sequence of the probiotic lactic acid bacterium
RT   Lactobacillus acidophilus NCFM.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:3906-3912(2005).
CC   -!- FUNCTION: Component of a beta-galactosidase.
CC       {ECO:0000250|UniProtKB:Q02603}.
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         Evidence={ECO:0000250|UniProtKB:Q02603};
CC   -!- SUBUNIT: Heterodimer of a large (LacL) and a small subunit (LacM).
CC       {ECO:0000250|UniProtKB:Q02603}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family. {ECO:0000305}.
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DR   EMBL; AB004867; BAA20536.1; -; Genomic_DNA.
DR   EMBL; CP000033; AAV43287.1; -; Genomic_DNA.
DR   RefSeq; WP_003548184.1; NC_006814.3.
DR   RefSeq; YP_194318.1; NC_006814.3.
DR   AlphaFoldDB; O07684; -.
DR   SMR; O07684; -.
DR   STRING; 272621.LBA1467; -.
DR   CAZy; GH2; Glycoside Hydrolase Family 2.
DR   GeneID; 56943041; -.
DR   KEGG; lac:LBA1467; -.
DR   PATRIC; fig|272621.13.peg.1388; -.
DR   eggNOG; COG3250; Bacteria.
DR   HOGENOM; CLU_002346_3_2_9; -.
DR   OrthoDB; 9762066at2; -.
DR   BioCyc; LACI272621:G1G49-1436-MONOMER; -.
DR   Proteomes; UP000006381; Chromosome.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 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   PANTHER; PTHR46323; BETA-GALACTOSIDASE; 1.
DR   PANTHER; PTHR46323:SF2; BETA-GALACTOSIDASE; 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   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 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; Reference proteome.
FT   CHAIN           1..628
FT                   /note="Beta-galactosidase large subunit"
FT                   /id="PRO_0000057665"
FT   ACT_SITE        468
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        536
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        302
FT                   /note="H -> N (in Ref. 1; BAA20536)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   628 AA;  73254 MW;  B73F7C691CC6B7E6 CRC64;
     MQANIKWLDD PEIFRVNQLP AHSDHPFFKN YREWQNNHSS FKQSLNGMWQ FKFSKDPQSR
     PVDFYKKDFN TSSFTTIPVP SEIELNNFAQ NQYINTLYPW EGKIFRRPAY ALNKSDAEEG
     SFSEGKDNTV GSYIKHFDLN PELRDHDIHI VFEGAERAMY VWLNGHFIGY AEDSFTPSEF
     DLTKYIKEKD NILAVEVFKH STASWLEDQD MFRFSGLFRS VELLAFPETH LVDLDLKPTV
     CDNYQDGIFN AELKFTGSLN GHVHLSVEDV NGSAILEQDV PLDSEVEFTS STLENIHLWD
     NHHPYLYQLL IEVHDENGHL VELIPYQFGF RRIEINQDKV ILLNGKCLII NGVNRHEWNA
     KTGRSITLND MEKDIDTFKE NNINAVRTCH YPNQIPWYYL CDQNGIYMMA ENNLESHGTW
     QKMGQVEPSD NVPGSVPEWR EAVIDRARNN YETFKNHTSI LFWSLGNESY AGSNIVAMNE
     FYKEHDSSRL VHYEGVVHRP ELKDQISDIE SHMYLPPKEV AEYLRNNPQK PFMECEYMHD
     MGNSDGGMGS YIKLIDEYPQ YVGGFIWDFI DQALLVYDPI SKQNVLRYGG DFDDRHSDYE
     FSGDGLMFAD RTPKPAMQEV RYYYGLHK
//