ID   BGAL_STAXY              Reviewed;         994 AA.
AC   O33815;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Beta-galactosidase;
DE            Short=Beta-gal;
DE            EC=3.2.1.23;
DE   AltName: Full=Lactase;
GN   Name=lacZ; Synonyms=lacH;
OS   Staphylococcus xylosus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1288;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 20267 / Isolate C2A;
RX   PubMed=9573174; DOI=10.1128/jb.180.9.2273-2279.1998;
RA   Bassias J., Brueckner R.;
RT   "Regulation of lactose utilization genes in Staphylococcus xylosus.";
RL   J. Bacteriol. 180:2273-2279(1998).
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   -!- 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; Y14599; CAA74937.1; -; Genomic_DNA.
DR   RefSeq; WP_047171676.1; NZ_LN554884.1.
DR   AlphaFoldDB; O33815; -.
DR   SMR; O33815; -.
DR   STRING; 1288.SXYLSMQ121_0084; -.
DR   CAZy; GH2; Glycoside Hydrolase Family 2.
DR   KEGG; sxo:SXYL_00084; -.
DR   eggNOG; COG3250; Bacteria.
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:0016052; P:carbohydrate catabolic process; IEA:UniProt.
DR   Gene3D; 2.60.40.10; -; 1.
DR   Gene3D; 2.70.98.10; -; 1.
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   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   PRINTS; PR00132; GLHYDRLASE2.
DR   SMART; SM01038; Bgal_small_N; 1.
DR   SUPFAM; SSF49303; SSF49303; 1.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   SUPFAM; SSF74650; SSF74650; 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..994
FT                   /note="Beta-galactosidase"
FT                   /id="PRO_0000057675"
FT   ACT_SITE        437
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        510
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   994 AA;  115234 MW;  78B2B43EB3EE0B1B CRC64;
     MLKQQFHENL EVQHVNLLPR RAFYIPYQQG EADYHFETRY NTRNATLLNG EWYFQYFESL
     EAYLNHSNKQ ESKTLTVPSV WNLYGYDQIQ YLNTQYPIPF NPPYVPKDNP CGHYTRKFTI
     DEYDQQYDYH LNFEGVDSAF YVWINNEFIG YSQISHAISE FDISNFVKQG ENNIEVLVLK
     YSDGTYLEDQ DMFRHSGIFR DVYILKRATE RVDDFKVETN LSDDLNAAQI DVKIERAHNL
     KSVEFQLYNP KGEEVASISG VNEHQFDVHN PHLWSTENPV LYTLYILTDQ EVITQKVGIR
     EVAIQNNQFY INGQSIKIRG TNYHDSHPET GYVMTESHFK KDLELMKQGN FNAIRTAHYP
     KSPLFYEMTD QYGFYVMSEA DIETHGVVRL YGEDNNEDFN IIADDSKFET AIIERIEASI
     MPLKNYSSIV SWSLGNESGF GKNMVKGAAR AKSLDNTRPI HYEGTLYRDK QQHYDLSNID
     MISRMYPSPE EIEETYLSNP DLDKPFILCE YAHAMGNSPG DLHAYQTLVE QYDSFIGGFV
     WEWCDHAIQT GMKDGNPIFR YGGDFGEKLH DGNFCVDGIV FPNRVPHEGY YEFKQEHRPL
     NLVSQEDFKI VLRNQLDFIP AEKYMFVEAT VTNLNGGKTI SEIPLSNFLP HTAQTIDLSD
     YINIQHISDV ILRYKLKYDD IFRHENFELG HDQIVYQRRT LKEQNEQSDE TEILVTQTDK
     LIKVSVGKSE TYVFNKDNAS LESVLKHNHI VISQNTTNNI WRAPTDNDTN IKNDWAYSGY
     KDITTRVHDY QIVENETEVS LIFNIAMVND AVPPVLFGTV TWHVQRNGTL NVTYDLERDM
     KAPYLPRFGL GLTLPKAFEQ VKYYGKGPFS SYQDKGVANY LDDFGTTVTD NGEIHIRPQE
     TGSHNETTFV EISDGCKKVI VTSDNTFSFN TTHYSLKQLT ETTHKDALEP EDQTYLYIDY
     AQSGIGSNSC GPELNEAYRL NNRHIEFSFN LKFV