ID A0A089M2B0_9BACL Unreviewed; 1036 AA.
AC A0A089M2B0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 39.
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=PSTEL_23565 {ECO:0000313|EMBL:AIQ65643.1};
OS Paenibacillus stellifer.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=169760 {ECO:0000313|EMBL:AIQ65643.1, ECO:0000313|Proteomes:UP000029507};
RN [1] {ECO:0000313|EMBL:AIQ65643.1, ECO:0000313|Proteomes:UP000029507}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14472 {ECO:0000313|EMBL:AIQ65643.1,
RC ECO:0000313|Proteomes:UP000029507};
RA den Bakker H.C., Tsai Y.-C., Martin N., Korlach J., Wiedmann M.;
RT "Comparative genomics of the Paenibacillus odorifer group.";
RL Submitted (AUG-2014) 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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401, ECO:0000256|RuleBase:RU361154}.
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DR EMBL; CP009286; AIQ65643.1; -; Genomic_DNA.
DR RefSeq; WP_038698878.1; NZ_CP009286.1.
DR AlphaFoldDB; A0A089M2B0; -.
DR STRING; 169760.PSTEL_23565; -.
DR KEGG; pste:PSTEL_23565; -.
DR HOGENOM; CLU_002346_0_2_9; -.
DR OrthoDB; 9762066at2; -.
DR Proteomes; UP000029507; 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; 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; LACTASE; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000029507}.
FT DOMAIN 762..1033
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1036 AA; 117585 MW; 693C62BC9B1B135F CRC64;
MRTKLAYTAP ANGYPEWNNN PEIFQLGRLK AHSSMMPFPG VPEALARDAS SSPFYRSLNG
TWKFAFAETP EQRIQSFYEM NYDSSGWSDM PVPSHWQLQG YDYPHYTNVR YPWAESEPDL
KPPYAPTRYN PVGSYIRTFT VPDDWKGRPV FISFQGVESA FYVWVNGELV GYGEDTFTPS
EFDLTPYLRD GENKLAVEVY RWCDASWLED QDFWRLSGIF RDVYLYSPPS VHISDFFVRT
ELDSEYRDAE LQLDVELTNY WDESAHSVTV EAQLYGADGS AVLERPLAAT ASLAGEEDFK
FKLSAEIRNP LKWSAEAPNL YTLVLTLKDR EGGVLEAVSC RTGFRKFELK DGLMKINGKR
IVFKGVNRHE FSADTGRALG KAEMIRDIEL MKSFNVNAVR TSHYPNQSIW YELCDEYGLY
VIDETNLETH GSWKYGQQEL NEFNVPASRP EWLANVLDRC NSMFQRDKNH PSIIIWSLGN
ESFGGDSFIA MHDFLKEADP TRLVHYEGIY HYRPSEAASD IESTMYIKPR EVEKYARSNP
KKPYILCEYA HAMGNSLGGL HLYWELFDRY DILQGAFIWD WVDQAIRTTT PDGVEYLAYG
GDFGESPHDG DFCGNGLIFA DRTISPKLYE VKKCYQDVRF EAADLREGLI TIRNQYLFTD
LGVYELAWKV EHDGTTVQSG TLQIAAAPGE TADVKIPYTT AFETDQEAVL TVSLVTKEDQ
AWAEAGHEVA WEQFILSPRV RRALSAFAEG TAETISSSDE LLIDCGKAAV RFSKITGDLV
SYQWENSELL AGPARPNFWR AMTDNDCGNK LPERSAFWRS APSERRLTGF SQRMEGGTAV
VQADYTWESH PSCTLSLTYR VAADGAIEIR QALNPGTGLA QLPEFGYLFP LKEQLDTVSW
YGRGPHENYW DRQTGARLGS YSGAVRDQFV PYLKPQECGN KTDVRFAEMS QSASGAGLRF
EADVPFELCA LPWSPLELEA HDHAYKLPTS DKTVVRINYK QMGVGGDDSW GAPTHDEFTL
PANRPYLFTF TISPRP
//