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Database: UniProt/TrEMBL
Entry: A0A089M2B0_9BACL
LinkDB: A0A089M2B0_9BACL
Original site: A0A089M2B0_9BACL 
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
//
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