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Database: UniProt
Entry: I8YFA9_9BACE
LinkDB: I8YFA9_9BACE
Original site: I8YFA9_9BACE 
ID   I8YFA9_9BACE            Unreviewed;      1075 AA.
AC   I8YFA9;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 54.
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=HMPREF1071_02938 {ECO:0000313|EMBL:EIY61067.1};
OS   Bacteroides salyersiae CL02T12C01.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=997887 {ECO:0000313|EMBL:EIY61067.1, ECO:0000313|Proteomes:UP000005150};
RN   [1] {ECO:0000313|EMBL:EIY61067.1, ECO:0000313|Proteomes:UP000005150}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CL02T12C01 {ECO:0000313|EMBL:EIY61067.1,
RC   ECO:0000313|Proteomes:UP000005150};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Zitomersky N.L., Coyne M.J.,
RA   Comstock L.E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B.,
RA   Gearin G., Goldberg J., Griggs A., Gujja S., Hansen M., Heiman D.,
RA   Howarth C., Larimer J., Lui A., MacDonald P.J.P., McCowen C.,
RA   Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA   Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Bacteroides salyersiae CL02T12C01.";
RL   Submitted (FEB-2012) 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:EIY61067.1}.
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DR   EMBL; AGXV01000035; EIY61067.1; -; Genomic_DNA.
DR   RefSeq; WP_007480870.1; NZ_JH724308.1.
DR   AlphaFoldDB; I8YFA9; -.
DR   PATRIC; fig|997887.3.peg.3039; -.
DR   HOGENOM; CLU_002346_0_2_10; -.
DR   OrthoDB; 9801077at2; -.
DR   Proteomes; UP000005150; 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   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..1075
FT                   /note="Beta-galactosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003717176"
FT   DOMAIN          774..1060
FT                   /note="Beta galactosidase small chain/"
FT                   /evidence="ECO:0000259|SMART:SM01038"
FT   REGION          987..1010
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        996..1010
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1075 AA;  122715 MW;  9D55917742F35DF4 CRC64;
     MKNLLTVACL VILPLTSIAQ GERYKQITDP QLTSIRKEAP RSSFTSYTNE KDAAVNNRKD
     GTFRLSLNGK WKFNYVDSFS TRPTDFMLPE KNVSDWADIQ VPGNWERQGF GIPIYVNTSY
     EFCSPGYAPY WDRPNPPYVP EEWNPTGTYR RDFTLPADWN GKEIFLSADG TKGAAFFYLN
     GQFAGMSKDA KTPARFNITQ FVKPGKNVIA VQVHRFSDAN YLECQDFWRL SGFERDVYLY
     AQPKLRMADF KVESPLDADY KDGILKLKVK VADSGKPVST SYVLSYKLLD KDGKQVATSD
     YAVEAMPVSA PSQSTNEFIF DDNIIRNPKQ WTAETPYLYT LIISLREPEN GEVLEATSVK
     VGFRTVEMKN HQLCVNGKPI LVKGVNVHEH NEYTGHYVTE ELMLKDFELW KKYNVNTVRT
     CHYPQQERFY ELCDEYGMYV IDEANIESHG MGYNREVGGT LANNPLFMDA HVARTVNMYE
     RDKNHPSVIV WSLGNEAGNG VNFYKTYSLL KELDSRPVQY EQAHLEWNTD ICCPMYSRPA
     DIEKYAKNPK HTRPLILCEY AHAMGNSLGN FQEYWDIIEK YPLLQGGCIW DWVDQGFAEK
     TADGRKYWAY GGDYGATGTP SDGDFCINGV VYPDRSVKPQ TTEMGKVYQN IKFVNFKKEA
     GTVDVRNDFS FTNLDKYDYH YIIRDHGKEI YTDKFRASGA PGETVTVQLK GIPQEQTNTG
     DVRIEFYATV RTPEPFLPAG TVIAREQNYI YTFHKDNAAL QAAAPVKETE TQAIYSGKNF
     KAVFDKKSGM LVSYKYNGME YILNGQGLHP NFWRAPIDND YGAGLPHKLG VWKEVSYGEV
     TAAVFNARNG EVTCSYKFPK ADASWDITYK IYADGVIKVN NRFVAANEKT PMIPRIGLRM
     QMPETFTTLT YYGRGPEENY RDRRTSQFFG EYSLPIKDMY EPYIRPQENN HRTDIYWCAF
     TNKSGAGLLL VADRTFELNA SNHPLETLDS GDDLHNAAPR TAETDHRHLT DPKPEKVVDV
     FVDYRMMGIG GDNSWGALPH EPYLIRTGSG NAIEYGFTLV PFGRKVDFRN LIYQY
//
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