ID F7QW76_9LACO Unreviewed; 1007 AA.
AC F7QW76;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
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=LSGJ_01567 {ECO:0000313|EMBL:EGM50021.1};
OS Ligilactobacillus salivarius GJ-24.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Ligilactobacillus.
OX NCBI_TaxID=1041521 {ECO:0000313|EMBL:EGM50021.1, ECO:0000313|Proteomes:UP000003074};
RN [1] {ECO:0000313|EMBL:EGM50021.1, ECO:0000313|Proteomes:UP000003074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GJ-24 {ECO:0000313|EMBL:EGM50021.1,
RC ECO:0000313|Proteomes:UP000003074};
RX PubMed=21742893; DOI=10.1128/JB.05616-11;
RA Cho Y.J., Choi J.K., Kim J.H., Lim Y.S., Ham J.S., Kang D.K., Chun J.,
RA Paik H.D., Kim G.B.;
RT "Genome Sequence of Lactobacillus salivarius GJ-24, a Probiotic Strain
RT Isolated from Healthy Adult Intestine.";
RL J. Bacteriol. 193:5021-5022(2011).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGM50021.1}.
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DR EMBL; AFOI01000005; EGM50021.1; -; Genomic_DNA.
DR RefSeq; WP_003705753.1; NZ_AFOI01000005.1.
DR AlphaFoldDB; F7QW76; -.
DR PATRIC; fig|1041521.3.peg.1577; -.
DR Proteomes; UP000003074; Unassembled WGS sequence.
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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:1901575; P:organic substance catabolic process; IEA:UniProt.
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; 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 InterPro; IPR032312; LacZ_4.
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}.
FT DOMAIN 733..1004
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1007 AA; 116522 MW; BA8AB32E39FE681E CRC64;
MENTKAKLNW LEKPDIFAIN RLEAHSSHKF YASQEEYQNK ETSLKQSLNG LWKFSYAQNP
DLRVKKFYKE DFNDSGFDTI KVPGHIQTQG YDHLQYINTQ YPWDGLDELR PPYISRKYNP
VGSYVKTFTV DKSLKNKRIF ISFQGVETAM YLWLNGKFIG YSEDSFTPHD FELTDFIRED
SENRLAVEVY KRSSASWIED QDMFRFSGIF RDVFLYAIPE VHVRDIFAKT TLDDSYKDGI
LLLNTKLEGN LENTEINVEL YDKDQVVWSR KEKAREKTFM DIKLENIKKW SAETPYLYDL
KITLVKNREV IEVATQKIGF RRFEMKDGIM LINGKRIVFK GVNRHEFDYL HGRAISEDVM
LHDIKFFKQN NINAVRTSHY PNQTRWYELC DEYGIYVIDE TNLESHGSWQ KLGECEPSWN
VPGSKEEWLD NVLDRANSMF QRDKNHASVI IWSCGNESYA GDDIVKMHDF FHKVDDSRLV
HYEGVTWNRD FEEATDMESR MYAKPQEIEE YLQGNPSKPY ISCEYMHSMG NSTGGMKLYT
DLEDKYPQYQ GGFIWDYVDQ AMLKTDDFGE KVLGYGGDFD ERATDYEFSG DGIVFADRTP
SPKAAEVKQL YANVKVKVTE EGVIIKNDNL FIDTSAYIFE TIVKRDGQKI WQKDYSFNVL
PQTKQEEVID WPNIEKIPGE YIFEVNVCLK ESVAWANERH ELSFGQLVTK VSSKDNEIVS
GKLNVVHGDV NIGINGDGFS VLLSRAEGGI VSLAYNGKEY ITRTPKTTFW RAMTDNDRGV
KHGFDRGVWL QAGLYQKLVD VNVKEELSEI TVSFKWNLPL AKEVYNVISY TVTPDGKVKV
TAKYFGVDGL PSLPAYGYEL KLKRKYNQYK FYGLGPDENY IDRDNGVKLG IYEGDADTNL
APYLVPQETG NHRGTRWLEV TDVYGEGLRF VANGDTFESS VLPYSEYEIE QAMHQEELSN
PHYTWVRLLA AQMGVGGDDS WGAPVQKQFW IPSNKDLTVS FTIEPTI
//
