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Database: UniProt
Entry: A0A243WCW6_9BACT
LinkDB: A0A243WCW6_9BACT
Original site: A0A243WCW6_9BACT 
ID   A0A243WCW6_9BACT        Unreviewed;      1105 AA.
AC   A0A243WCW6;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|ARBA:ARBA00012756, 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=BXP70_13945 {ECO:0000313|EMBL:OUJ73501.1};
OS   Hymenobacter crusticola.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Hymenobacter.
OX   NCBI_TaxID=1770526 {ECO:0000313|EMBL:OUJ73501.1, ECO:0000313|Proteomes:UP000194873};
RN   [1] {ECO:0000313|EMBL:OUJ73501.1, ECO:0000313|Proteomes:UP000194873}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIMBbqt21 {ECO:0000313|EMBL:OUJ73501.1};
RA   Liang Y., Feng F.;
RT   "A new Hymenobacter.";
RL   Submitted (JAN-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   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
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:OUJ73501.1}.
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DR   EMBL; MTSE01000006; OUJ73501.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A243WCW6; -.
DR   Proteomes; UP000194873; 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   Calcium {ECO:0000256|ARBA:ARBA00022837};
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:UP000194873};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..1105
FT                   /note="Beta-galactosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012331515"
FT   DOMAIN          806..1076
FT                   /note="Beta galactosidase small chain/"
FT                   /evidence="ECO:0000259|SMART:SM01038"
SQ   SEQUENCE   1105 AA;  124368 MW;  9342DCD5FCC2392E CRC64;
     MRRPIWTALL LLLASVAASA QEASVYYFPG VSNPPKIYNG EGWDNPLVSE LNRDPARATA
     YSFTNEKDAL AGDRAKSRLL SLNGNWDFNF VSKPADAPQD FYKSRVQGWK QLEVPSNWEM
     KGYDLPIYKS AKYPFRPVNP PFVPQDYNGV GSYQRTFTVP ANWKDLNVTL HFGGVSSAFK
     VWVNGRFLGY GEDSCLPSEF NVTPYLQAGE NTVSVQVIRW SDGSYLEDQD HWRLSGIYRE
     VLLLGEPKMR LADFHWQAKL DKQYRDAVLS IRPRLENLTG NDDLKGYLLK AQLYNKNGQP
     VFAKPLERTG DAIINEKYPR LDNRKFGLLE TTVANPAKWS DEQPNLYTLV LTLEKDGNVL
     EAKSCKLGFR AIEFSKTDGK LLINGKVTYL YGVNRHDHHP TKGMAVSRED IRQDVRTLKQ
     FNFNCIRTSH YPNDPYFYDL CDEYGILVMD EANLETHGLG SKLSNDPSWT QAYVSRSTRM
     ALRDKNHPSV VFWSLGNESG RGPNHAAMAA WLHDFDITRP VHYEPAQGDP HLDGYIDPSD
     PNYPKNHAKR IQVPRDQAYV DMVSRMYPTL TTGALLANQQ NGDNRPIFFC EYSHSMGNAT
     GNMKEFWDGW RATKRVIGGC IWEFKDQGLL KRDSLGTPFY AYGGDFQEKY YDDFTIKGIV
     ASDGKPHAAL YECKRVYQPA ECVLTDAAKA LIKVTNRHAT ESLNSYNVSL VVREDGKVVA
     IKALPHLRLA AGKDTTISLK SYLPKLKAGS EYLADIHFTL AQPTLWADMG HEVASNQFEL
     TSLAKPTSKP QQYVALTTRE DASAYTLSGK GFQATFDKTS GALTSYRWNN QEQILAPLLP
     HFTRPLTDND RRGWKADKKS KEWFEPSLKL KTITLDQAQK GVATIKSDYT LIDGKAAVQV
     VYTLNGAGVL KVDYKLSPQA SLPNMIKVGM QCGIANDYRQ ISWYGRGPWE NYIDRSYAAD
     AGIYSQGLQD FMESYVVPQE NSNRTDVRWM LLSSAQKGGL LVVADSLLSM SAWPYTEANI
     AKARHTNKLQ EAGFLTLNID LKQIGVGGNT SWDDDAQPVE QYRMPAKPYA YSFYLLPTNS
     KKEAASALAK SIKFQSKFSS SVGVK
//
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