ID   D2BM26_LACLK            Unreviewed;       998 AA.
AC   D2BM26;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|ARBA:ARBA00013303, ECO:0000256|RuleBase:RU361154};
DE            EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|RuleBase:RU361154};
DE   AltName: Full=Lactase {ECO:0000256|ARBA:ARBA00032230, ECO:0000256|RuleBase:RU361154};
GN   Name=lacZ {ECO:0000313|EMBL:ADA65738.1};
GN   OrderedLocusNames=LLKF_2164 {ECO:0000313|EMBL:ADA65738.1};
OS   Lactococcus lactis subsp. lactis (strain KF147).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=684738 {ECO:0000313|EMBL:ADA65738.1, ECO:0000313|Proteomes:UP000001886};
RN   [1] {ECO:0000313|EMBL:ADA65738.1, ECO:0000313|Proteomes:UP000001886}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KF147 {ECO:0000313|EMBL:ADA65738.1,
RC   ECO:0000313|Proteomes:UP000001886};
RX   PubMed=18039825; DOI=10.1128/AEM.01850-07;
RA   Siezen R.J., Starrenburg M.J., Boekhorst J., Renckens B., Molenaar D.,
RA   van Hylckama Vlieg J.E.;
RT   "Genome-scale genotype-phenotype matching of two Lactococcus lactis
RT   isolates from plants identifies mechanisms of adaptation to the plant
RT   niche.";
RL   Appl. Environ. Microbiol. 74:424-436(2008).
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:0000256|ARBA:ARBA00001412,
CC         ECO:0000256|RuleBase:RU361154};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC       {ECO:0000256|ARBA:ARBA00007401, ECO:0000256|RuleBase:RU361154}.
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DR   EMBL; CP001834; ADA65738.1; -; Genomic_DNA.
DR   AlphaFoldDB; D2BM26; -.
DR   CAZy; GH2; Glycoside Hydrolase Family 2.
DR   KEGG; llk:LLKF_2164; -.
DR   HOGENOM; CLU_002346_0_2_9; -.
DR   Proteomes; UP000001886; 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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:1901575; P:organic substance catabolic process; IEA:UniProt.
DR   Gene3D; 2.70.98.10; -; 1.
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; 2.
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   PANTHER; PTHR46323; BETA-GALACTOSIDASE; 1.
DR   PANTHER; PTHR46323:SF2; BETA-GALACTOSIDASE; 1.
DR   Pfam; PF02929; Bgal_small_N; 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   Pfam; PF16353; LacZ_4; 1.
DR   PRINTS; PR00132; GLHYDRLASE2.
DR   SMART; SM01038; Bgal_small_N; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 2.
DR   SUPFAM; SSF74650; Galactose mutarotase-like; 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 {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361154};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361154}.
FT   DOMAIN          719..996
FT                   /note="Beta galactosidase small chain/"
FT                   /evidence="ECO:0000259|SMART:SM01038"
SQ   SEQUENCE   998 AA;  115349 MW;  220BFF8A1FBC50EE CRC64;
     MAMMTMIDVL ERKDWENPVV SNWNRLPMHT PMDFLEKQSL NGLWNFDHFS RISDVPKNWL
     ELTESKTEII VPSNWQIEFK DKSDVPIYTN VTYPIPIQPP YVPEANPVGA YSRYFDITKE
     WLESGHVHLT FEGVGSAFHF WLNGEYGGYS EDSRLSAEFD ISNLAKEGQN CLKVLVFRWS
     KGTYFEDQDM WRMSGIFRSV NLQWLPDNYL LDFSIKTDLD EDLDFANVKL QAYAKNMDDA
     CLEFKLYDDE QLIGECHGFD AEIGVVNPKL WSDEIPYLYR LELTLMDRSG AVFHKETKKI
     GIRKIAIEKG QLKINGKALL VRGVNKHEFT PEHGYVVSEE VMIKDIKLMK EHNFNAVRCS
     HYPNDSRWYE LCDEYGLYVM DEANIETHGM TPMNRLTNDP TYLPLMSERV TRMVMRDRNH
     PSIIIWSLGN ESGYGSNHQA LYDWCKSFDS SRPVHYEGGD DASRGATDAT DIICPMYARV
     DSPSINAPYS LKTWMGVAGE NRPLILCEYA HDMGNSLGGF GKYWQAFREI DRLQGGFIWD
     WVDQGLLKDG NYAYGGDFGD KPNDRQFSLN GLVFPNRQAK PALREAKYWQ QYYQFELEKT
     PLGQVFAFTV TNEYLFRSTD NEKLCYQLTN GLEVLWENEL ILNMPAGGSM RIDLSELPID
     GTDNLFLNIQ VKTIEKCNLL ESDFEVAHQQ FVLQEKINFT DRIDSNEEIT LLEDEELLTV
     RSAKQKFIFN KSNGNLSRWL DEKGNEKLLH ELSEQFTRAP LDNDIGVSEV EHIDPNAWLE
     RWKAVGFYEL KTLLKNMIIQ ATENEVIISV QTDYEAKGKI AFSTIREYHI FRNGELLLKV
     DFKRNIEFPE PARIGLSLQL AEKAENVTYF GLGPDENYPD RRGASLFGQW NLRITDMTTP
     YIFPSENGLR METRELNYGR LKVRAMGQSF AFNLSPYSQN QLAKKGHWHL LEEEAGTWLN
     IDGFHMGVGG DDSWSPSVAQ EYLLTKGNYH YEVSFKLT
//