ID A0A108T711_BACSE Unreviewed; 1071 AA.
AC A0A108T711;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
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};
DE Flags: Precursor;
GN Name=lacZ_5 {ECO:0000313|EMBL:KWR54543.1};
GN ORFNames=AA415_02077 {ECO:0000313|EMBL:KWR54543.1};
OS Bacteroides stercoris.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=46506 {ECO:0000313|EMBL:KWR54543.1, ECO:0000313|Proteomes:UP000056419};
RN [1] {ECO:0000313|EMBL:KWR54543.1, ECO:0000313|Proteomes:UP000056419}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL09T03C01 {ECO:0000313|EMBL:KWR54543.1,
RC ECO:0000313|Proteomes:UP000056419};
RX PubMed=26768901; DOI=10.1186/s12864-016-2377-z;
RA Coyne M.J., Roelofs K.G., Comstock L.E.;
RT "Type VI secretion systems of human gut Bacteroidales segregate into three
RT genetic architectures, two of which are contained on mobile genetic
RT elements.";
RL BMC Genomics 17:58-58(2016).
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:KWR54543.1}.
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DR EMBL; LRGC01000008; KWR54543.1; -; Genomic_DNA.
DR RefSeq; WP_060385988.1; NZ_LRGC01000008.1.
DR AlphaFoldDB; A0A108T711; -.
DR STRING; 46506.AA415_02077; -.
DR PATRIC; fig|46506.5.peg.2223; -.
DR Proteomes; UP000056419; 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; 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:UP000056419};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..1071
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007130826"
FT DOMAIN 766..1056
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
FT REGION 983..1008
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1071 AA; 122994 MW; 50E83200B97AFC4E CRC64;
MKIHGLLLAA AFLPVALAAQ EDRYAQITNP KLTSINKEPP RSTFTSYTNE ADAVVNDRKN
GTFRISLNGK WKFNYVENFA DRPTDFMDIH ADVSKWPDID VPGNWELQGF GTPVYVNQSY
EFCSPGYAPY WDKPNPPYVP KEWNPTGTYR RTFTLPADWD NKEIFLSADG VRGAAFYYLN
GKFAGMSKDS KTPARFNVTS LARRGENVIA IQVHRFSDGN YLECQDFWRI SGIERDIYMY
AQPQIHLTDF KAETPLDGDY RNGILKLKVK FANETGKETP FLVSYRLLDS KDKLIAQSST
RVSYGQTEVE FTPKTIKEPL QWTAETPNLY TLVISLKHTN GDIIEATGCK VGFRTVEIKD
KQLMVNGKPI LVKGVNYHEH NEYTGHYVPE ELMLKDFELW KRYNINTIRT CHYPQQERFY
ELCDQYGFYV IDEANIESHG MGYNLNVGGT LGNNPLFTKA HIDRTMNMYE RDKNHPCIIT
WSLGNEAGNG LNFYVTYNTL KALDSRPVQY ERALLEWNTD IFCPMYHSPA RIEKYAQDPE
MTRPLILCEY AHAMGNSLGN FQDYWNIIEK YPILQGGCIW DWVDQGLAAK TADGRKYWAY
GGDYGEYGTP SDGDFCINGI VYPDRSVKPQ TEEMGKVYQN IKFFDFDPAA SVVKIRNDFS
FTNLDKYDFH YIVRHHGKEI YKGRIKDIKA EPGQTVTSPF LNGIPATNSS TGDVRIEFYA
AIRTPEPFLP AGTVIAREQT YVHTFHKEDA PKQAFAGSEE DDRQVVFSGP HFKATFDKQS
GLLVSYRYKK QEYIHNGQGP RPFFWRAPTD NDYGAKLPVR LKAWKEASYQ EPKAESFNVV
RDKDTTAIKV TYRFPQTDAR WDITYKVYGN GVIKVDNHFV AENAQTPMIP RVGLRMQLPA
RITSLTYYGR GPEENYRDRR TSQFIGEYTS GIQDMYEPYV RPQENNHRTD IYWCTLTSKA
KEGLLFVADR TFEMNVSNYP LESLDSGESI ENGSPRTEKT NHRHLTDPQP EPSVDLFIDY
RMMGVGGDDS WGALAHEPYL IRPGRQNAIS YGFAIVPFDK GTDFKSLIYR Y
//
