ID   Q03NB4_LEVBA            Unreviewed;       628 AA.
AC   Q03NB4;
DT   14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT   14-NOV-2006, sequence version 1.
DT   27-MAR-2024, entry version 94.
DE   RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE            EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
GN   OrderedLocusNames=LVIS_2259 {ECO:0000313|EMBL:ABJ65308.1};
OS   Levilactobacillus brevis (strain ATCC 367 / BCRC 12310 / CIP 105137 / JCM
OS   1170 / LMG 11437 / NCIMB 947 / NCTC 947) (Lactobacillus brevis).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Levilactobacillus.
OX   NCBI_TaxID=387344 {ECO:0000313|EMBL:ABJ65308.1, ECO:0000313|Proteomes:UP000001652};
RN   [1] {ECO:0000313|EMBL:ABJ65308.1, ECO:0000313|Proteomes:UP000001652}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 367 / BCRC 12310 / CIP 105137 / JCM 1170 / LMG 11437 /
RC   NCIMB 947 / NCTC 947 {ECO:0000313|Proteomes:UP000001652};
RX   PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA   Makarova K., Slesarev A., Wolf Y., Sorokin A., Mirkin B., Koonin E.,
RA   Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA   Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA   Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA   Baldwin K., Lee J.H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA   Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA   Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J., Hutkins R.,
RA   O'Sullivan D., Steele J., Unlu G., Saier M., Klaenhammer T., Richardson P.,
RA   Kozyavkin S., Weimer B., Mills D.;
RT   "Comparative genomics of the lactic acid bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC       {ECO:0000256|ARBA:ARBA00007401, ECO:0000256|RuleBase:RU361154}.
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DR   EMBL; CP000416; ABJ65308.1; -; Genomic_DNA.
DR   RefSeq; WP_011668828.1; NC_008497.1.
DR   AlphaFoldDB; Q03NB4; -.
DR   SMR; Q03NB4; -.
DR   STRING; 387344.LVIS_2259; -.
DR   KEGG; lbr:LVIS_2259; -.
DR   PATRIC; fig|387344.15.peg.2162; -.
DR   eggNOG; COG3250; Bacteria.
DR   HOGENOM; CLU_002346_3_2_9; -.
DR   Proteomes; UP000001652; 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 {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361154};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361154};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001652}.
FT   DOMAIN          43..227
FT                   /note="Glycosyl hydrolases family 2 sugar binding"
FT                   /evidence="ECO:0000259|Pfam:PF02837"
FT   DOMAIN          230..332
FT                   /note="Glycoside hydrolase family 2 immunoglobulin-like
FT                   beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF00703"
FT   DOMAIN          334..625
FT                   /note="Glycoside hydrolase family 2 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF02836"
SQ   SEQUENCE   628 AA;  71673 MW;  B5C29E4BC805A4C4 CRC64;
     MKADLTWLDD PQTFRINQLP AHSDHRGYAS VEEATAQHSS LVQSLDGTWQ FAFAPDPVHR
     FEGFYQPDYD RSAFDRLTVP GHIELAGYGQ IQYINTAYPW EGHHYRRPAY SMGADQPEKG
     MFSTDPQNTV GAYVKHFTLN PALANQRVSI EFDGVEQAMF LWLNGQFVGY AEDSFSRSEF
     DLTPYLQAGQ NLLAVEVFKH STAAFLEDQD MFRFSGIFRS VRLVAKPELH VEDLTIRAGL
     DDAFQTGDLK VRLQLTAASQ LSGTATAQLL TADGQEVWAT EQPAASTLDL AAAIDHVHLW
     DHHDPYLYQL RITLKDVAGQ VVEVVPYPVG FRRIELKDKV MCLNGQRLIL NGVNRHEWDA
     HRGRAVTMAD MTQDLQTFHD NHINAVRTCH YPDQDAWYYL CDQQGIYMMA ENNLETHGTW
     QKMGAVEPSY NVPGSLPQWQ LAVLDRAKSN YEMFKNHPAV LFWSLGNESY AGDNIAAMDA
     FYHHADPTRL THYEGVCRNR VYEDRISDME SMMYDPPRAI EDYLKNDPQK PFVNCEYMHD
     MGNSLGGMAS YDALIDQYPM YQGGFIWDFI DQALWVKDEV TGQPVLRYGG DFDDRHSDYE
     FSGDGLLFAD RTPKPALQEV DYYYGQHD
//