ID A0A3Q9QSL7_9BACI Unreviewed; 1018 AA.
AC A0A3Q9QSL7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 28-JAN-2026, entry version 25.
DE RecName: Full=Beta-galactosidase {ECO:0000256|ARBA:ARBA00013303, ECO:0000256|RuleBase:RU361154};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|RuleBase:RU361154};
DE AltName: Full=Lactase {ECO:0000256|ARBA:ARBA00032230, ECO:0000256|RuleBase:RU361154};
GN ORFNames=CHR53_03700 {ECO:0000313|EMBL:AZU60441.1};
OS Neobacillus mesonae.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC Neobacillus.
OX NCBI_TaxID=1193713 {ECO:0000313|EMBL:AZU60441.1, ECO:0000313|Proteomes:UP000282892};
RN [1] {ECO:0000313|EMBL:AZU60441.1, ECO:0000313|Proteomes:UP000282892}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H20-5 {ECO:0000313|EMBL:AZU60441.1,
RC ECO:0000313|Proteomes:UP000282892};
RA Kim S.Y., Song H., Sang M.K., Weon H.-Y., Song J.;
RT "The complete genome sequence of Bacillus mesonae strain H20-5, an
RT efficient strain improving plant abiotic stress resistance.";
RL Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU361154};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401, ECO:0000256|RuleBase:RU361154}.
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DR EMBL; CP022572; AZU60441.1; -; Genomic_DNA.
DR RefSeq; WP_127485039.1; NZ_CP022572.1.
DR AlphaFoldDB; A0A3Q9QSL7; -.
DR STRING; 1193713.GCA_001636315_03258; -.
DR KEGG; nmk:CHR53_03700; -.
DR OrthoDB; 9762066at2; -.
DR Proteomes; UP000282892; Chromosome.
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:0005990; P:lactose catabolic process; IEA:TreeGrafter.
DR Gene3D; 2.70.98.10; -; 1.
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; 2.
DR InterPro; IPR004199; B-gal_small/dom_5.
DR InterPro; IPR050347; Bact_Beta-galactosidase.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR017853; GH.
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; IPR006104; Glyco_hydro_2_N.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR006102; Ig-like_GH2.
DR InterPro; IPR032312; LacZ_4.
DR NCBIfam; NF007666; PRK10340.1; 1.
DR PANTHER; PTHR46323; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR46323:SF2; BETA-GALACTOSIDASE; 1.
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 Pfam; PF16353; LacZ_4; 1.
DR PRINTS; PR00132; GLHYDRLASE2.
DR SMART; SM01038; Bgal_small_N; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 2.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 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:UP000282892}.
FT DOMAIN 728..1002
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1018 AA; 117274 MW; A8C92B7DAD253766 CRC64;
MKKFKRWEDI HTDGINRMEP RAHFSSFPSR EAAQSGDAGK SHYYQSLNGT WKFLFLDAPE
YSPEGFYTEE LETTNWDDIT VPGNWQLQGY GKMHYSDLWY NFPIIPPRVP TDNPTGIYRR
EFELDRDLEG EQLILRFNGV DSAYELYVNG EFAGYSKGAR IQAEFDVTNL CRQGRNSLTV
RVFQWSDGTY LEDQDMWWLS GIFRDVDLYT RPAAGLYDYT VNTELDSDNQ NATLSVSVKL
TEQNGQTISY ELIDPNGEQV LNVEKKADEP LGQFVAAPLK WSAEEPNLYH LYMTVKDSDG
KIIEVIRQQV GFRSIVISGE TFLVNGVAIK FKGANRHDYN PKTGRVVTKA EIERDIITMK
QNNINAIRTA HYPNAHYLYD LCDQYGMYVI DETDLECHGF ELTGNYKWIS DDPDWELAYV
SRMERMIERD KNHPCIIMWS LGNESSFGHN FRAMAKRAKE MDSTRLVHYE GDFEAEVTDV
YSTMYTWLER KDDKLKMDKI IEKSKKPHIL CEYAHAMGNG PGNLKEYQDL FYKHDKLQGG
FIWEWFDHGI ETVAEDGSVY YRYGGDFGDD PTNGNFCIDG LIMPDGTPSP SLFEYKKVIE
PVQTECLDIE KGLFRLINRY DFISLDHLEL TCCLFEDEKL LESFTVELPQ LKGRETAKIE
LPVGRELEKL NGAKYYFVFS YTLKEDTAWA SKGHELANAS FELPGKEKLP KVHADGELQV
TKDGALVTVS GVDFTVTFDS VKGSIKEVTR NGKVQIEKGP QFNFWRAPID NDMYYVTDYR
TKYFMHLGHE IVEEVNYELK DGVFEWQADA LYGTTNSSWY YQLQYRYSIY PDGDIECRID
GIASGMKENA PVMIPRLGVN MRLNKEFIDT KWRGRGPGES YVDSKEANHP GVYQKTVDEL
FTNYVKPQEN GNRSDCDWVS LTAGDGNGLI FSADETFDFS ASHYEIGDLE HAKHTIDLKP
RDYVVLNLDY KQNGLGSNSC GQDQLEKYRC KFEDFTLEFR ISSFNTEEIS AVELGRLR
//
