ID Q5LAU4_BACFN Unreviewed; 1020 AA.
AC Q5LAU4; A0A380YVE1;
DT 21-JUN-2005, integrated into UniProtKB/TrEMBL.
DT 21-JUN-2005, sequence version 1.
DT 27-MAR-2024, entry version 117.
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=BF9343_2998 {ECO:0000313|EMBL:CAH08779.1};
OS Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019
OS / NCTC 9343 / Onslow).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=272559 {ECO:0000313|EMBL:CAH08779.1, ECO:0000313|Proteomes:UP000006731};
RN [1] {ECO:0000313|EMBL:CAH08779.1, ECO:0000313|Proteomes:UP000006731}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019 / NCTC 9343 /
RC Onslow {ECO:0000313|Proteomes:UP000006731};
RX PubMed=15746427; DOI=10.1126/science.1107008;
RA Cerdeno-Tarraga A.-M., Patrick S., Crossman L.C., Blakely G., Abratt V.,
RA Lennard N., Poxton I., Duerden B., Harris B., Quail M.A., Barron A.,
RA Clark L., Corton C., Doggett J., Holden M.T.G., Larke N., Line A., Lord A.,
RA Norbertczak H., Ormond D., Price C., Rabbinowitsch E., Woodward J.,
RA Barrell B.G., Parkhill J.;
RT "Extensive DNA inversions in the B. fragilis genome control variable gene
RT expression.";
RL Science 307:1463-1465(2005).
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}.
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DR EMBL; CR626927; CAH08779.1; -; Genomic_DNA.
DR RefSeq; WP_010993256.1; NZ_UFTH01000001.1.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
DR PaxDb; 272559-BF9343_2998; -.
DR KEGG; bfs:BF9343_2998; -.
DR eggNOG; COG3250; Bacteria.
DR HOGENOM; CLU_002346_0_2_10; -.
DR BioCyc; BFRA272559:G1GHZ-3252-MONOMER; -.
DR Proteomes; UP000006731; 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: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; 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.
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:UP000006731};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1020
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041118684"
FT DOMAIN 748..1017
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1020 AA; 115699 MW; 25592484915B2179 CRC64;
MNKPIKLTFL LILACLMLLP VNAQNTPEWQ SQYAVGLNKL APHTYVWPYA SATDVKKGDY
EQSPYYLNLN GKWKFHWVKN PDLRPKDFYK PSFYTGGWAD INVPGNWERQ GYGTAIYVNE
TYEFDDKMFN FKKNPPLVPY KENEVGSYRR TFTVPAGWKG RRVVLCCEGV ISFYYVWVNG
HFLGYNQGSK TAAEWDITDQ LEEGENTIAL EVYRWSSGSY LECQDMWRLS GIERDVYLYS
TPKQYIADYK VNATLEKERY KDGIFGLDVT VGGPADGVAS VSYTLNDPLG RPVLSGEMPV
KSRGLSNFIT FGEQRLKDVK RWSAEHPNLY TLVLELKNAG GQVTEVTGCE VGFRTSEIKD
GRFCINGVPV LVKGTNRHEH SQLGRTVSKE LMEQDIRLMK LYNINTVRNS HYPTDPYWYR
LCDRYGLYMI DEANIESHGM GYGPASLAKD STWLTAHMDR THRMYERSKN HPAIVIWSLG
NEAGNGINFE RTYDWLKSVE KSRPVQYERA EQNYNTDIYC RMYRSVDEIK AYLAQKDIYR
PFILCEYVHA MGNSVGGLKE YWDVFENNPM AQGGCVWDWV DQSFREIDSN GRWYWSYGGD
YGPKGIPSFG NFCCNGLVSA DRVPHPHLLE VKKIYQNIKC TLINKNNLTV RVKNWFDFSN
LNEYILHWQV VGDNGKLLAE GNKEVNCAPH ATADVTLGKV ALPANVREGY LNLSWTRKEA
SPMVGTDWEV AYDQFVLPGT KGSTAYLPAK AGQTAFTVDK ETGALNSLTL DGQELLATPV
TLSLFRPATD NDNRDRNGAY LWRKAGLNQL TQKVVSLKDG KKAATAKVEI LNAKGMKVGD
ADFAYSLNSA GALKVKVTFR PDTAVVKSMA RLGLTFEMND TYGNVAYLGR GDNETYSDRM
QSGKIALYQT TAERMFHYYV TPQSTGNRTD VRWMKLTDET GQGIFVDSNR PFQFSVIPFA
DDVLEKARHI NDLERNGHVT VHLDAEQAGV GTATCGPGVQ PQYRVPVTEQ SFEFTLRTVK
//
