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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

    GO - Biological processi

    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

    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.Bsubs1_010100003978.

    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:January 1, 1998 - 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.
    WP_003242572.1. NZ_JNCM01000032.1.

    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.
    WP_003242572.1. NZ_JNCM01000032.1.

    3D structure databases

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

    Protein-protein interaction databases

    STRINGi224308.Bsubs1_010100003978.

    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(1997) [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(2006) [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(2007) [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(2007) [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 24, 2009
    Last sequence update: January 1, 1998
    Last modified: June 24, 2015
    This is version 83 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.