ID   B0SK30_LEPBP            Unreviewed;       660 AA.
AC   B0SK30;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 80.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|PIRNR:PIRNR001084};
DE            Short=Beta-gal {ECO:0000256|PIRNR:PIRNR001084};
DE            EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|PIRNR:PIRNR001084};
GN   OrderedLocusNames=LEPBI_I0024 {ECO:0000313|EMBL:ABZ96171.1};
OS   Leptospira biflexa serovar Patoc (strain Patoc 1 / ATCC 23582 / Paris).
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Leptospira.
OX   NCBI_TaxID=456481 {ECO:0000313|EMBL:ABZ96171.1, ECO:0000313|Proteomes:UP000001847};
RN   [1] {ECO:0000313|EMBL:ABZ96171.1, ECO:0000313|Proteomes:UP000001847}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Patoc 1 / ATCC 23582 / Paris
RC   {ECO:0000313|Proteomes:UP000001847};
RX   PubMed=18270594; DOI=10.1371/journal.pone.0001607;
RA   Picardeau M., Bulach D.M., Bouchier C., Zuerner R.L., Zidane N.,
RA   Wilson P.J., Creno S., Kuczek E.S., Bommezzadri S., Davis J.C., McGrath A.,
RA   Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z., Coppel R.L.,
RA   Rood J.I., Lajus A., Davies J.K., Medigue C., Adler B.;
RT   "Genome sequence of the saprophyte Leptospira biflexa provides insights
RT   into the evolution of Leptospira and the pathogenesis of leptospirosis.";
RL   PLoS ONE 3:E1607-E1607(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|PIRNR:PIRNR001084};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 42 family.
CC       {ECO:0000256|ARBA:ARBA00005940, ECO:0000256|PIRNR:PIRNR001084}.
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DR   EMBL; CP000786; ABZ96171.1; -; Genomic_DNA.
DR   RefSeq; WP_012387062.1; NC_010602.1.
DR   AlphaFoldDB; B0SK30; -.
DR   STRING; 456481.LEPBI_I0024; -.
DR   CAZy; GH42; Glycoside Hydrolase Family 42.
DR   KEGG; lbi:LEPBI_I0024; -.
DR   HOGENOM; CLU_012430_1_0_12; -.
DR   OrthoDB; 9800974at2; -.
DR   BioCyc; LBIF456481:LEPBI_RS00135-MONOMER; -.
DR   Proteomes; UP000001847; Chromosome I.
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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd03143; A4_beta-galactosidase_middle_domain; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
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; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR36447; BETA-GALACTOSIDASE GANA; 1.
DR   PANTHER; PTHR36447:SF2; BETA-GALACTOSIDASE YESZ; 1.
DR   Pfam; PF02449; Glyco_hydro_42; 1.
DR   Pfam; PF08532; Glyco_hydro_42M; 1.
DR   PIRSF; PIRSF001084; B-galactosidase; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|PIRNR:PIRNR001084, ECO:0000313|EMBL:ABZ96171.1};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR001084, ECO:0000313|EMBL:ABZ96171.1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001084-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001847};
KW   Zinc {ECO:0000256|PIRSR:PIRSR001084-3}.
FT   DOMAIN          6..381
FT                   /note="Glycoside hydrolase family 42 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02449"
FT   DOMAIN          393..609
FT                   /note="Beta-galactosidase trimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF08532"
FT   ACT_SITE        142
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT   ACT_SITE        304
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT   BINDING         103
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT   BINDING         107
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT   BINDING         141
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ   SEQUENCE   660 AA;  75646 MW;  8619CAC0AAA94AA8 CRC64;
     MIFGACYYPE QWNPKDWDED LKMMKEMGLS SVRLAEFAWG IMEPKEGKFD FSLFDAILEK
     IQKQGMTAIL GTPTATFPPW LYQKFPEIVQ ISKEGIIRGI GTRRQACFSS PAYKKATERI
     VTAMAKHFGN HPAVVGWQID NEPGHEGSDV DYSPLAEKNF RIWLKTKYKT LDSLNKRWGN
     VFWGVIYSDW NQIPLPGAHV ASNFNPAMIQ DYYRFQSDEL VSYIHFQAEI LRKYSKGKPL
     TTNLYPSPFL PVTDMYEMFK KLDYVSWDNY PVWGNQQEPY PHPLVTATQQ YSRGLKDKPY
     TVMEQFSGVQ GHDTLGYLPP PGQIGLWLTQ AIVNGANQIY FFRYRTARFG QEQLCYGILD
     HGKRKTSKYF ELKKTIEEIK EFAEDIAASP YPAKVAILHD IENSRNYKHQ PLSDGLKFSP
     VPFAQVGYDI ELATWFAGTN VLNVNTHSLP IQREQDWSNY KVLTLPLYTM FGPEIVEKLK
     AYVQEGGTLV LGYRSGIKDK DHWMVEEPVP GVFSEMAGVE VFQFEAPATD KVGIKMGIWP
     LKGSKFCEIL EPTSAKVIAR YRDKKKFYSG KPAITVNSFG KGKVYYVGTS LTPESFVLLY
     RKILKGAGIP FGFLGATIER HFREGKKYNY EITMNHSNQY KLAGFSVLKP FGYQIKRIQK
//