ID   F0RBZ1_CELLC            Unreviewed;      1076 AA.
AC   F0RBZ1;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   02-SEP-2026, entry version 76.
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   OrderedLocusNames=Celly_1802 {ECO:0000313|EMBL:ADY29625.1};
OS   Cellulophaga lytica (strain ATCC 23178 / DSM 7489 / JCM 8516 / NBRC 14961 /
OS   NCIMB 1423 / VKM B-1433 / Cy l20).
OC   Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Cellulophaga.
OX   NCBI_TaxID=867900 {ECO:0000313|EMBL:ADY29625.1, ECO:0000313|Proteomes:UP000007487};
RN   [1] {ECO:0000313|EMBL:ADY29625.1, ECO:0000313|Proteomes:UP000007487}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23178 / DSM 7489 / JCM 8516 / NBRC 14961 / NCIMB 1423 /
RC   VKM B-1433 / Cy l20 {ECO:0000313|Proteomes:UP000007487};
RX   PubMed=21677859; DOI=10.4056/sigs.1774329;
RA   Pati A., Abt B., Teshima H., Nolan M., Lapidus A., Lucas S., Hammon N.,
RA   Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S.,
RA   Liolios K., Pagani I., Mavromatis K., Ovchinikova G., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Jeffries C.D., Detter J.C.,
RA   Brambilla E.M., Kannan K.P., Rohde M., Spring S., Goker M., Woyke T.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P., Ivanova N.;
RT   "Complete genome sequence of Cellulophaga lytica type strain (LIM- 21).";
RL   Stand. Genomic Sci. 4:221-232(2011).
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   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC       {ECO:0000256|ARBA:ARBA00007401, ECO:0000256|RuleBase:RU361154}.
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DR   EMBL; CP002534; ADY29625.1; -; Genomic_DNA.
DR   RefSeq; WP_013621370.1; NC_015167.1.
DR   AlphaFoldDB; F0RBZ1; -.
DR   STRING; 867900.Celly_1802; -.
DR   GeneID; 308207625; -.
DR   KEGG; cly:Celly_1802; -.
DR   eggNOG; COG3250; Bacteria.
DR   HOGENOM; CLU_002346_0_2_10; -.
DR   OrthoDB; 9801077at2; -.
DR   Proteomes; UP000007487; 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:0005990; P:lactose catabolic process; IEA:TreeGrafter.
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; IPR050347; Bact_Beta-galactosidase.
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; IPR017853; GH_hydrolase_sf.
DR   InterPro; IPR006101; Glyco_hydro_2.
DR   InterPro; IPR006103; Glyco_hydro_2_cat.
DR   InterPro; IPR023230; Glyco_hydro_2_CS.
DR   InterPro; IPR006104; Glyco_hydro_2_N.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR006102; Ig-like_GH2.
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:UP000007487};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..1076
FT                   /note="Beta-galactosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003255088"
FT   DOMAIN          804..1073
FT                   /note="Beta galactosidase small chain/"
FT                   /evidence="ECO:0000259|SMART:SM01038"
SQ   SEQUENCE   1076 AA;  122674 MW;  4CC3FA34A1C6C215 CRC64;
     MRHGLTIALL FFIVAQSVTA QNDWENEHIF GINKMEARVA SYSYKNSTDA LEGDRNKARV
     KSLNGIWKFK YTAKSTDRPT DFYAANFKGE DFANIPVPSN WELQGHGQPI YTNITYPFTP
     NIQDPNLKYG WRGPQPPIPP KIYRDNPVGS YYRDFKIPEE WKNQSVILHF GGISSAFYVW
     VNGKKVGYSQ DSRLAAEFDI SAYINPNTTN RVAVQVFRWS DGSYLENQDM WRLSGIHREV
     LLLAQPKIAI NDFYIKTKFD ANIEDAKLQI RPKVWIKENK TNLQNWTITA MLFNADKKEV
     LDKEISVPVS TVFNERWPAR DITKFGLLEA NIRMPNKWSA ENPYLYTVVL NVKDPNGKIV
     ESRSQKIGFR KVEFSKKNEL LINGKVVKLM GVNRHDHHPT RGKALTREDL RKDVALIKQY
     NFNAVRTSHY PNDPYFIELC NEYGIYVMSE ANIETHHLGS YIPQTPSWTA PILSRVYRMV
     ERDKNNPSII SWSLGNESGT GPAFAAAAAW IKDYDSSRFI HYEGAQGAPN NPAYIENAGF
     TSNNWPSMAN PTDPAYVDVI SRMYPDHEQL INLANSPHIN RPIVMCEYMH AMGNSMGGLG
     EFWDIIRAKP NLIGGFIWDM VDQGLEKKDP NGNIFYAYGG DFGDVPNDHN FCINGVFASD
     RTPNPHAWEA KYVFQPVAFE AVDLANKKVR IINRFTTTNL DKYTIKWSVF ENGKELESGE
     LDSQDIAASS SAIVTIPFKS NNLKSNSDYW LRLSAHEKTD RLWAKKGYLI AKEQLNIKTK
     KATSTYTSSS NNHITTLETD KTITVKGTKF SVSISKENGQ LASYKTEGKE QVISPLKPNF
     YRPPVDNDIR GASNKVLKKG RQFWKNIIDS VKTTKVTISK KHEKFIEITS EQYISKKLSF
     KTSFTVYNDA TVLISFSTQA SKSLPAPIRI GLTMGVSKQL KNTSYYGNGP YENYSDRKRN
     SEIGEYHTKT DAMFTNYVMP QENGNRTETR WLKLTNNKKS GIAIIAMSEF SFSVWPYSSE
     NIEQAKHPYE LTPQNYYTLN IDYAQTGLGG TLSHLLPKYT LKSGEYNFQF LIQPLQ
//