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Database: UniProt
Entry: A0A1C0ZT02_9BACL
LinkDB: A0A1C0ZT02_9BACL
Original site: A0A1C0ZT02_9BACL 
ID   A0A1C0ZT02_9BACL        Unreviewed;      1048 AA.
AC   A0A1C0ZT02;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
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=A8709_05920 {ECO:0000313|EMBL:OCT11215.1};
OS   Paenibacillus pectinilyticus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=512399 {ECO:0000313|EMBL:OCT11215.1, ECO:0000313|Proteomes:UP000093309};
RN   [1] {ECO:0000313|Proteomes:UP000093309}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC13222 {ECO:0000313|Proteomes:UP000093309};
RA   Zhang J., Zhang X.;
RT   "Paenibacillus oryzae. sp. nov., isolated from the rice root.";
RL   Submitted (MAY-2016) 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}.
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:OCT11215.1}.
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DR   EMBL; LYPC01000028; OCT11215.1; -; Genomic_DNA.
DR   RefSeq; WP_065858041.1; NZ_LYPC01000028.1.
DR   AlphaFoldDB; A0A1C0ZT02; -.
DR   STRING; 512399.A8709_05920; -.
DR   OrthoDB; 9762066at2; -.
DR   Proteomes; UP000093309; 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   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:UP000093309}.
FT   DOMAIN          744..1015
FT                   /note="Beta galactosidase small chain/"
FT                   /evidence="ECO:0000259|SMART:SM01038"
FT   REGION          1022..1048
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1029..1048
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1048 AA;  118555 MW;  31557C22022055BB CRC64;
     MSNNNVARDW DNLAVLERNR TKSRAYFIPH WDIAGALSYD RGSSPWFKSL NGNWKFHYAK
     GPEWAQDDFY TADYDLSGWD EIQVPSHWQL KGYGHPHYTD LYYPFPVDPP HVPNDNPTGS
     YVREFELPKL WDGRKLCVKF DGVDSAFHVW VNGNFVGYSQ GSRLTSEFDL TPYVKEGINR
     MAVRVYQWSD GSYLEDQDMW YMSGIFRDVY LISEPSSLRM VDYRIVTELD AAYRDATLHV
     EIELQGDAGG GEVQLQLLDY KGHSVISAKR QITLAGTDEA IVAFTIPVSK PSLWSAEAPT
     LYHLTIGIVD QNVTVVETVA QRVGFRKIEV KDGQFLVNGK AILLKGVNRH DHHPDSGRTV
     TVSTMIQDVK MMKQHNINAV RTAHYPNDPR FYDICDEYGL YVMEETDLET HGFEPLGNIS
     RLSDDPAWQE AYVDRVRRMV DRDKNHPSVL FWSLGNESGF GCNFRAMSAW CKGADPTRLI
     HYEEDREAEV CDIVSTMYSS VEKMVGFGQL VDHPKPHILC EFAHAMGNGP GGLKPYFDTF
     DAYRRLQGGF VWEWIDHGIR RKTADGKDDY AYGGDYGDVP NNSNFVIDGL VQPDRTPSPG
     LIEYKKIIEP VRVSYIEEGR IRIMNRYDFV TLEHLQAHWS VTVDGRTVQS GVLELPQIRP
     GESAEVHVPL GEDMQLAVLA QEAERWLNVG FTLAVDCLWG EQGHEVAWAQ MTMEARANNS
     SFAAIAARPP IQSLACTEEG RQLVLANDAF RIAFDTRQAG ISSLRMNGHE LVNTGPRLNF
     WRAPIDNDMY VLPDWYKAHL NRLSERIDSC RWEQLSEGTV RITYTSRIAP PVFDWGFRCE
     TTYTITGSGL IVMDVHGVPE GKTPAMLPKI GLQMEIPGDM DAVRWYGRGP GENYSDSKEA
     GRFGVYSQSV DELLTPYIYP QENGNRTDVR WVSVTDGAGI GLLAVGAPTL EFSARRYTDA
     DIEAAKHASD LVPRDFVTLN LDYRQNGLGS NSCGPAQSPE NTVTSEAFRF RIMLKPYLSE
     DASPERLSHQ MRSEVQMNHH QQEGTNHA
//
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