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Protein

Beta-galactosidase YesZ

Gene

yesZ

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

May play a role in the degradation of rhamnogalacturonan derived from plant cell walls.1 Publication

Catalytic activityi

Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.

Kineticsi

  1. KM=3.0 mM for p-nitrophenyl beta-D-galactopyranoside (at pH 7.0 and 37 degrees Celsius)1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei106 – 1061SubstrateBy similarity
Metal bindingi110 – 1101ZincBy similarity
Binding sitei144 – 1441SubstrateBy similarity
Active sitei145 – 1451Proton donor1 Publication
Metal bindingi153 – 1531ZincBy similarity
Metal bindingi155 – 1551ZincBy similarity
Metal bindingi158 – 1581ZincBy similarity
Active sitei296 – 2961Nucleophile1 Publication

GO - Molecular functioni

  1. beta-galactosidase activity Source: UniProtKB-EC
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. galactose metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciBSUB:BSU07080-MONOMER.
SABIO-RKO31529.

Protein family/group databases

CAZyiGH42. Glycoside Hydrolase Family 42.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-galactosidase YesZ (EC:3.2.1.23)
Short name:
Beta-gal
Alternative name(s):
Probable rhamnogalacturonan beta-galactosidase
Gene namesi
Name:yesZ
Ordered Locus Names:BSU07080
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570 Componenti: Chromosome

Organism-specific databases

GenoListiBSU07080.

Subcellular locationi

GO - Cellular componenti

  1. beta-galactosidase complex Source: InterPro
Complete GO annotation...

Pathology & Biotechi

Disruption phenotypei

No chromogen 5-bromo-4-chloro-3-indolyl-beta-D-galactopyranoside (X-Gal) hydrolyzation.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi145 – 1451E → A: Hydrolysis of the covalent glycosyl-enzyme intermediate is slowed. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 663663Beta-galactosidase YesZPRO_0000367024Add
BLAST

Proteomic databases

PaxDbiO31529.

Expressioni

Inductioni

Up-regulated by growth on type I rhamnogalacturonan.1 Publication

Interactioni

Subunit structurei

Homotrimer.By similarity

Protein-protein interaction databases

STRINGi224308.BSU07080.

Structurei

3D structure databases

ProteinModelPortaliO31529.
SMRiO31529. Positions 17-149.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni345 – 3484Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the glycosyl hydrolase 42 family.Curated

Phylogenomic databases

eggNOGiCOG1874.
HOGENOMiHOG000095202.
InParanoidiO31529.
KOiK01190.
OMAiFYERILN.
OrthoDBiEOG6HMX9F.
PhylomeDBiO31529.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
3.40.50.880. 1 hit.
InterProiIPR013739. Beta_galactosidase_C.
IPR013738. Beta_galactosidase_Trimer.
IPR029062. Class_I_gatase-like.
IPR003476. Glyco_hydro_42.
IPR013529. Glyco_hydro_42_N.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF02449. Glyco_hydro_42. 1 hit.
PF08533. Glyco_hydro_42C. 1 hit.
PF08532. Glyco_hydro_42M. 1 hit.
[Graphical view]
PIRSFiPIRSF001084. B-galactosidase. 1 hit.
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF52317. SSF52317. 1 hit.

Sequencei

Sequence statusi: Complete.

O31529-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRKLYHGACY YPELWDEETI QQDIDIMREV GVNVVRIGEF AWSVMEPEEG
60 70 80 90 100
KIDVGFFKEI IARLYDSGIE TIMCTPTPTP PIWFSHGRPE RMHANEKREI
110 120 130 140 150
MGHGSRQHAC TNNPYFRKKA AIITTAIAKE LGRLPGLIGW QLDNEFKCHV
160 170 180 190 200
AECMCETCLR LWHDWLKNRY GVIERLNEAW GTDVWSETYQ TFEQVPQPGP
210 220 230 240 250
APFLHHASLR TMYQLFSMEM IASFADEQAK IIRCYSDAPI THNGSVMFSV
260 270 280 290 300
DNERMFQNLD FASYDTYASQ ENASAFLLNC DLWRNLKQGR PFWILETSPS
310 320 330 340 350
YAASLESSAY PHADGYLQAE AVSSYALGSQ GFCYWLWRQQ RSGSEISHGS
360 370 380 390 400
VLSAWGEPTI GYQNVLAVER ARKEIEPIIL STEPVQAEAA MTYSDRAKAF
410 420 430 440 450
IKTEPHRGLR HRSLVTHFYE RILNTGIHRD LIPEGAPLDG YRLLFTPFVP
460 470 480 490 500
YLSSEFIKKA SAFAEAGGIW ITGPLTGGRT CEHTIHTDCG LGELEKTSGI
510 520 530 540 550
KTLFTFPMNE NVNTGKAFGI TAPLGLWSAV FDTESGNTLG TVEAGPGAGH
560 570 580 590 600
AFLTERNYGE GKIVMLGSLP SGKEGDAMLE ALVRHYAEEA VISSRSDVTP
610 620 630 640 650
GTIVAPRIGE NGLVWIVVNM DGKGGSVTLP ESGTDLLTHR LEKAGRLAVG
660
PHEYRVIQFD NHS
Length:663
Mass (Da):74,099
Last modified:December 31, 1997 - v1
Checksum:i7E5799B02C0C5238
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB12527.1.
PIRiA69798.
RefSeqiNP_388589.1. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB12527; CAB12527; BSU07080.
GeneIDi936080.
KEGGibsu:BSU07080.
PATRICi18973064. VBIBacSub10457_0746.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB12527.1.
PIRiA69798.
RefSeqiNP_388589.1. NC_000964.3.

3D structure databases

ProteinModelPortaliO31529.
SMRiO31529. Positions 17-149.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.BSU07080.

Protein family/group databases

CAZyiGH42. Glycoside Hydrolase Family 42.

Proteomic databases

PaxDbiO31529.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB12527; CAB12527; BSU07080.
GeneIDi936080.
KEGGibsu:BSU07080.
PATRICi18973064. VBIBacSub10457_0746.

Organism-specific databases

GenoListiBSU07080.

Phylogenomic databases

eggNOGiCOG1874.
HOGENOMiHOG000095202.
InParanoidiO31529.
KOiK01190.
OMAiFYERILN.
OrthoDBiEOG6HMX9F.
PhylomeDBiO31529.

Enzyme and pathway databases

BioCyciBSUB:BSU07080-MONOMER.
SABIO-RKO31529.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
3.40.50.880. 1 hit.
InterProiIPR013739. Beta_galactosidase_C.
IPR013738. Beta_galactosidase_Trimer.
IPR029062. Class_I_gatase-like.
IPR003476. Glyco_hydro_42.
IPR013529. Glyco_hydro_42_N.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF02449. Glyco_hydro_42. 1 hit.
PF08533. Glyco_hydro_42C. 1 hit.
PF08532. Glyco_hydro_42M. 1 hit.
[Graphical view]
PIRSFiPIRSF001084. B-galactosidase. 1 hit.
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF52317. SSF52317. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  2. "Bioinformatic, genetic, and biochemical evidence that some glycoside hydrolase family 42 beta-galactosidases are arabinogalactan type I oligomer hydrolases."
    Shipkowski S., Brenchley J.E.
    Appl. Environ. Microbiol. 72:7730-7738(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  3. "Plant cell wall degradation by saprophytic Bacillus subtilis strains: gene clusters responsible for rhamnogalacturonan depolymerization."
    Ochiai A., Itoh T., Kawamata A., Hashimoto W., Murata K.
    Appl. Environ. Microbiol. 73:3803-3813(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DEGRADATION OF TYPE I RHAMNOGALACTURONAN, INDUCTION.
    Strain: 168.
  4. "Identification of the catalytic nucleophile in family 42 beta-galactosidases by intermediate trapping and peptide mapping: YesZ from Bacillus subtilis."
    Shaikh F.A., Muellegger J., He S., Withers S.G.
    FEBS Lett. 581:2441-2446(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE, MUTAGENESIS OF GLU-145.

Entry informationi

Entry nameiBGAL1_BACSU
AccessioniPrimary (citable) accession number: O31529
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 23, 2009
Last sequence update: December 31, 1997
Last modified: January 6, 2015
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.