ID   BGAL_WEICA              Reviewed;         665 AA.
AC   D5JGG0;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 1.
DT   03-AUG-2022, entry version 39.
DE   RecName: Full=Beta-galactosidase LacZ;
DE            Short=Beta-gal {ECO:0000250|UniProtKB:P19668};
DE            EC=3.2.1.23;
GN   Name=lacZ {ECO:0000312|EMBL:ADF47156.1};
OS   Weizmannia coagulans (Bacillus coagulans).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Weizmannia.
OX   NCBI_TaxID=1398;
RN   [1] {ECO:0000312|EMBL:ADF47156.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 7050 / DSM 1 / JCM 2257 / CCUG 7417 / NBRC 12583 / NCIMB 9365 /
RC   NCTC 10334 / NRS 609 {ECO:0000312|EMBL:ADF47156.1};
RX   PubMed=20400555; DOI=10.1128/aem.03060-09;
RA   Kovacs A.T., van Hartskamp M., Kuipers O.P., van Kranenburg R.;
RT   "Genetic tool development for a new host for biotechnology, the
RT   thermotolerant bacterium Bacillus coagulans.";
RL   Appl. Environ. Microbiol. 76:4085-4088(2010).
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:P19668};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 42 family. {ECO:0000255}.
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DR   EMBL; GU323918; ADF47156.1; -; Genomic_DNA.
DR   RefSeq; WP_029142380.1; NZ_CP051674.1.
DR   AlphaFoldDB; D5JGG0; -.
DR   SMR; D5JGG0; -.
DR   STRING; 1398.AB434_1803; -.
DR   CAZy; GH42; Glycoside Hydrolase Family 42.
DR   GeneID; 29812235; -.
DR   GO; GO:0009341; C:beta-galactosidase complex; IEA:InterPro.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006012; P:galactose metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.40.1180; -; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   InterPro; IPR013739; Beta_galactosidase_C.
DR   InterPro; IPR013738; Beta_galactosidase_Trimer.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR003476; Glyco_hydro_42.
DR   InterPro; IPR013529; Glyco_hydro_42_N.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR36447; PTHR36447; 1.
DR   Pfam; PF02449; Glyco_hydro_42; 1.
DR   Pfam; PF08533; Glyco_hydro_42C; 1.
DR   Pfam; PF08532; Glyco_hydro_42M; 1.
DR   PIRSF; PIRSF001084; B-galactosidase; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
PE   3: Inferred from homology;
KW   Glycosidase; Hydrolase; Metal-binding; Zinc.
FT   CHAIN           1..665
FT                   /note="Beta-galactosidase LacZ"
FT                   /id="PRO_0000407682"
FT   ACT_SITE        149
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:O69315"
FT   ACT_SITE        303
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:O69315"
FT   BINDING         110
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O69315"
FT   BINDING         114
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:O69315"
FT   BINDING         148
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O69315"
FT   BINDING         157
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:O69315"
FT   BINDING         159
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:O69315"
FT   BINDING         162
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:O69315"
FT   BINDING         311
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O69315"
FT   BINDING         351..354
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O69315"
SQ   SEQUENCE   665 AA;  76013 MW;  E1DBF3B4E13FFAB4 CRC64;
     MLKKHEKFYY GGDYNPEQWD ESVWKEDMRL MKKAGVNYVS INIFSWARLQ PDEETYDFST
     LDKIMDMLAE NGIGADLATA TAAPPAWLSR KYPDSLPVDK DGSRFLPGSR QHYCPNSKDY
     ARLAAKLVRK IAERYKSHPA LVMWHVNNEY GCHISECYCD NCKKGFQTWL KEKYGTIENL
     NKSWSTDFWS QRYYEWEEIC LPGKTPTFAN PMQQLDYKAF MDDSLLALYK MERDILKTYT
     PDVPVMTNLM GLHKPVDGFH WAKEMDLVTW DAYPDPFEDI PYAQFMAHDL TRSLKKQPFL
     LMEQAAGAVN WRAQNAVKAP GVMRLWSYEA AAHGADGIMF FQWRASQGGA EKFHSGMVPH
     SGDEESRNFR EVVQLGNELK NLEKVTGSAY ASDVAIVFDW KNWWALELDS KPSSLVTYIK
     QLLPFYRVLH TQNIGVDFIH PDEAMDRYKV VFAPASYRVT KTFADKVKAY VENGGYFATN
     FFSGIADENE RVYLGGYPGA YRDILGIYVE EFAPMKKGAV HQIRTGYGDA AIRVWEEKIH
     LKGAEALAWF KDGYLAGSPA VTAHHCGKGK AYYIGTQPDE QYLSSLLKEI LKEADVRPAL
     DAPRGVEVAV RKNGHEKFLF LLNHTDQVQF VDAGGTYPEL IYGRTEAETV RLSPRDVKIL
     QVIEK