ID K8Y5A2_9LEPT Unreviewed; 658 AA.
AC K8Y5A2;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 24-JAN-2024, entry version 45.
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 ORFNames=LSS_15226 {ECO:0000313|EMBL:EKT85862.1};
OS Leptospira santarosai serovar Shermani str. LT 821.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=758847 {ECO:0000313|EMBL:EKT85862.1, ECO:0000313|Proteomes:UP000035800};
RN [1] {ECO:0000313|EMBL:EKT85862.1, ECO:0000313|Proteomes:UP000035800}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT 821 {ECO:0000313|EMBL:EKT85862.1};
RX PubMed=23041083; DOI=10.1016/j.gene.2012.09.074;
RA Chou L.F., Chen Y.T., Lu C.W., Ko Y.C., Tang C.Y., Pan M.J., Tian Y.C.,
RA Chiu C.H., Hung C.C., Yang C.W.;
RT "Sequence of Leptospira santarosai serovar Shermani genome and prediction
RT of virulence-associated genes.";
RL Gene 511:364-370(2012).
RN [2] {ECO:0000313|Proteomes:UP000035800}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT821 {ECO:0000313|Proteomes:UP000035800};
RA Chou L.-F., Chen T.-W., Ko Y.-C., Pan M.-J., Tian Y.-C., Chiu C.-H.,
RA Tang P., Hung C.-C., Yang C.-W.;
RT "Potential impact on kidney infection: a whole-genome analysis of
RT Leptospira santarosai serovar Shermani.";
RL Emerg. Microbes Infect. 3:e82-e82(2014).
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; CP006694; EKT85862.1; -; Genomic_DNA.
DR RefSeq; WP_004461748.1; NZ_CP006694.1.
DR AlphaFoldDB; K8Y5A2; -.
DR STRING; 758847.LSS_15226; -.
DR GeneID; 29742220; -.
DR KEGG; lst:LSS_15226; -.
DR PATRIC; fig|758847.3.peg.3184; -.
DR Proteomes; UP000035800; 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:0006012; P:galactose 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; 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; 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; PF08533; Glyco_hydro_42C; 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};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR001084};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001084-3};
KW Zinc {ECO:0000256|PIRSR:PIRSR001084-3}.
FT DOMAIN 6..380
FT /note="Glycoside hydrolase family 42 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02449"
FT DOMAIN 392..607
FT /note="Beta-galactosidase trimerisation"
FT /evidence="ECO:0000259|Pfam:PF08532"
FT DOMAIN 615..655
FT /note="Beta-galactosidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08533"
FT ACT_SITE 141
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT ACT_SITE 303
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT BINDING 102
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 140
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ SEQUENCE 658 AA; 76274 MW; 64B35F472390FD4D CRC64;
MIFGVDYYPE QWTPKDWEED ISIMKEMGLS SVRLAEFAWA LMEPKEGKYD FSFFDHILDL
IQKNGMTAIL GTPTATFPPW LAKKFPDIIQ ERDGIQRTIG TRRQACFSSP NYKKAVVKIV
TAMAKHFGNH PAVIGWQIDN EIGHEGSDID HSQTSLKAFR VWLKNKYKTI HALNESWGNV
FWGMLYNSFD EIPIPGRHVA SNFHPSMIQD FHRFHSDTIV EFVKLQAQIL RKFSVGRPLT
TNLYPSPFLS IIDMAELSAY LDYISWDNYP TWGEQEAPFP HPFLSAMQQY NRGLKNLPFT
VMEQISGFQG HDLLGYLPAP GQTKLWMKHS IIHGSNSIYF FRYRTARFGQ EQLCYGILDH
DKEKTERYYE LQKGIQEIKE HAEDFTEELF PAQVAVVHDI ENARNWKHQP ISTGLKFSPV
PWSQLGYDIE MATWFSGMNV LNVNTHFRPA SKIDFKNYKI IILPMYTMVD DSVFKRLEQF
VREGGTLVLG FRTGAKNQNG WMYDSPIPGP FAEMAGIKVR KFEAVGNQKV KFRFRYFPGS
CSKICEILEP TTAKVWARYT DRKKFYKGSP VITANYYHKG KVVYVGSSLE PSSFVLLYRR
ILKESKIPFI FYGPNIEKIF RIGRKQNYEI FINHSGKKSL AGLKILDPYE VRILPKRK
//
