ID   BGAL1_BACSU             Reviewed;         663 AA.
AC   O31529;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   27-MAR-2024, entry version 115.
DE   RecName: Full=Beta-galactosidase YesZ;
DE            Short=Beta-gal;
DE            EC=3.2.1.23;
DE   AltName: Full=Probable rhamnogalacturonan beta-galactosidase;
GN   Name=yesZ; OrderedLocusNames=BSU07080;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [2]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=17056685; DOI=10.1128/aem.01306-06;
RA   Shipkowski S., Brenchley J.E.;
RT   "Bioinformatic, genetic, and biochemical evidence that some glycoside
RT   hydrolase family 42 beta-galactosidases are arabinogalactan type I oligomer
RT   hydrolases.";
RL   Appl. Environ. Microbiol. 72:7730-7738(2006).
RN   [3]
RP   FUNCTION IN DEGRADATION OF TYPE I RHAMNOGALACTURONAN, AND INDUCTION.
RC   STRAIN=168;
RX   PubMed=17449691; DOI=10.1128/aem.00147-07;
RA   Ochiai A., Itoh T., Kawamata A., Hashimoto W., Murata K.;
RT   "Plant cell wall degradation by saprophytic Bacillus subtilis strains: gene
RT   clusters responsible for rhamnogalacturonan depolymerization.";
RL   Appl. Environ. Microbiol. 73:3803-3813(2007).
RN   [4]
RP   BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE, AND MUTAGENESIS OF GLU-145.
RX   PubMed=17485082; DOI=10.1016/j.febslet.2007.04.053;
RA   Shaikh F.A., Muellegger J., He S., Withers S.G.;
RT   "Identification of the catalytic nucleophile in family 42 beta-
RT   galactosidases by intermediate trapping and peptide mapping: YesZ from
RT   Bacillus subtilis.";
RL   FEBS Lett. 581:2441-2446(2007).
CC   -!- FUNCTION: May play a role in the degradation of rhamnogalacturonan
CC       derived from plant cell walls. {ECO:0000269|PubMed:17449691}.
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=3 mM for p-nitrophenyl beta-D-galactopyranoside (at pH 7.0 and 37
CC         degrees Celsius) {ECO:0000269|PubMed:17485082};
CC   -!- SUBUNIT: Homotrimer. {ECO:0000250}.
CC   -!- INDUCTION: Up-regulated by growth on type I rhamnogalacturonan.
CC       {ECO:0000269|PubMed:17449691}.
CC   -!- DISRUPTION PHENOTYPE: No chromogen 5-bromo-4-chloro-3-indolyl-beta-D-
CC       galactopyranoside (X-Gal) hydrolyzation. {ECO:0000269|PubMed:17056685}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 42 family. {ECO:0000305}.
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DR   EMBL; AL009126; CAB12527.1; -; Genomic_DNA.
DR   PIR; A69798; A69798.
DR   RefSeq; NP_388589.1; NC_000964.3.
DR   RefSeq; WP_003242572.1; NZ_JNCM01000032.1.
DR   AlphaFoldDB; O31529; -.
DR   SMR; O31529; -.
DR   STRING; 224308.BSU07080; -.
DR   CAZy; GH42; Glycoside Hydrolase Family 42.
DR   PaxDb; 224308-BSU07080; -.
DR   EnsemblBacteria; CAB12527; CAB12527; BSU_07080.
DR   GeneID; 936080; -.
DR   KEGG; bsu:BSU07080; -.
DR   PATRIC; fig|224308.179.peg.768; -.
DR   eggNOG; COG1874; Bacteria.
DR   InParanoid; O31529; -.
DR   OrthoDB; 9800974at2; -.
DR   PhylomeDB; O31529; -.
DR   BioCyc; BSUB:BSU07080-MONOMER; -.
DR   SABIO-RK; O31529; -.
DR   Proteomes; UP000001570; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006012; P:galactose metabolic process; IEA:InterPro.
DR   CDD; cd03143; A4_beta-galactosidase_middle_domain; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR013739; Beta_galactosidase_C.
DR   InterPro; IPR013738; Beta_galactosidase_Trimer.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR003476; Glyco_hydro_42.
DR   InterPro; IPR013529; Glyco_hydro_42_N.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR36447; BETA-GALACTOSIDASE GANA; 1.
DR   PANTHER; PTHR36447:SF2; BETA-GALACTOSIDASE YESZ; 1.
DR   Pfam; PF02449; Glyco_hydro_42; 1.
DR   Pfam; PF08533; Glyco_hydro_42C; 1.
DR   Pfam; PF08532; Glyco_hydro_42M; 1.
DR   PIRSF; PIRSF001084; B-galactosidase; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
PE   1: Evidence at protein level;
KW   Glycosidase; Hydrolase; Metal-binding; Reference proteome; Zinc.
FT   CHAIN           1..663
FT                   /note="Beta-galactosidase YesZ"
FT                   /id="PRO_0000367024"
FT   ACT_SITE        145
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000305|PubMed:17485082"
FT   ACT_SITE        296
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000305|PubMed:17485082"
FT   BINDING         106
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         110
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         144
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         153
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         155
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         158
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         345..348
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         145
FT                   /note="E->A: Hydrolysis of the covalent glycosyl-enzyme
FT                   intermediate is slowed."
FT                   /evidence="ECO:0000269|PubMed:17485082"
SQ   SEQUENCE   663 AA;  74099 MW;  7E5799B02C0C5238 CRC64;
     MRKLYHGACY YPELWDEETI QQDIDIMREV GVNVVRIGEF AWSVMEPEEG KIDVGFFKEI
     IARLYDSGIE TIMCTPTPTP PIWFSHGRPE RMHANEKREI MGHGSRQHAC TNNPYFRKKA
     AIITTAIAKE LGRLPGLIGW QLDNEFKCHV AECMCETCLR LWHDWLKNRY GVIERLNEAW
     GTDVWSETYQ TFEQVPQPGP APFLHHASLR TMYQLFSMEM IASFADEQAK IIRCYSDAPI
     THNGSVMFSV DNERMFQNLD FASYDTYASQ ENASAFLLNC DLWRNLKQGR PFWILETSPS
     YAASLESSAY PHADGYLQAE AVSSYALGSQ GFCYWLWRQQ RSGSEISHGS VLSAWGEPTI
     GYQNVLAVER ARKEIEPIIL STEPVQAEAA MTYSDRAKAF IKTEPHRGLR HRSLVTHFYE
     RILNTGIHRD LIPEGAPLDG YRLLFTPFVP YLSSEFIKKA SAFAEAGGIW ITGPLTGGRT
     CEHTIHTDCG LGELEKTSGI KTLFTFPMNE NVNTGKAFGI TAPLGLWSAV FDTESGNTLG
     TVEAGPGAGH AFLTERNYGE GKIVMLGSLP SGKEGDAMLE ALVRHYAEEA VISSRSDVTP
     GTIVAPRIGE NGLVWIVVNM DGKGGSVTLP ESGTDLLTHR LEKAGRLAVG PHEYRVIQFD
     NHS
//