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P22498

- BGAL_SULSO

UniProt

P22498 - BGAL_SULSO

Protein

Beta-galactosidase

Gene

lacS

Organism
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 117 (01 Oct 2014)
      Sequence version 2 (20 Jun 2001)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei76 – 761Not N6-methylated
    Sitei102 – 1021Not N6-methylated
    Sitei124 – 1241Not N6-methylated
    Sitei138 – 1381Not N6-methylated
    Active sitei206 – 2061Proton donorSequence Analysis
    Active sitei387 – 3871NucleophilePROSITE-ProRule annotation

    GO - Molecular functioni

    1. beta-galactosidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Enzyme and pathway databases

    BioCyciSSOL273057:GCH2-2809-MONOMER.
    BRENDAi3.2.1.23. 6163.
    SABIO-RKP22498.

    Protein family/group databases

    CAZyiGH1. Glycoside Hydrolase Family 1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-galactosidase (EC:3.2.1.23)
    Short name:
    Lactase
    Gene namesi
    Name:lacS
    Ordered Locus Names:SSO3019
    OrganismiSulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
    Taxonomic identifieri273057 [NCBI]
    Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus
    ProteomesiUP000001974: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 489489Beta-galactosidasePRO_0000063867Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei116 – 1161N6-methyllysine; partial1 Publication
    Modified residuei135 – 1351N6-methyllysine1 Publication
    Modified residuei273 – 2731N6-methyllysine; partial1 Publication
    Modified residuei311 – 3111N6-methyllysine; partial1 Publication
    Modified residuei332 – 3321N6-methyllysine1 Publication

    Keywords - PTMi

    Methylation

    Interactioni

    Subunit structurei

    Homotetramer.

    Protein-protein interaction databases

    STRINGi273057.SSO3019.

    Structurei

    Secondary structure

    1
    489
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi9 – 135
    Helixi16 – 194
    Helixi32 – 387
    Helixi40 – 445
    Helixi53 – 553
    Helixi59 – 7214
    Beta strandi77 – 815
    Helixi84 – 874
    Helixi112 – 12110
    Helixi124 – 13916
    Beta strandi143 – 1486
    Helixi155 – 1573
    Helixi160 – 1645
    Helixi173 – 1753
    Helixi177 – 19418
    Turni195 – 1973
    Beta strandi199 – 2057
    Helixi207 – 2159
    Helixi218 – 2203
    Helixi229 – 25123
    Beta strandi258 – 27114
    Helixi272 – 2743
    Helixi275 – 28511
    Helixi287 – 2959
    Beta strandi297 – 2993
    Beta strandi304 – 3063
    Turni308 – 3125
    Beta strandi317 – 33014
    Beta strandi333 – 3364
    Beta strandi338 – 3403
    Beta strandi346 – 3494
    Helixi366 – 37914
    Beta strandi383 – 3875
    Helixi398 – 41417
    Beta strandi419 – 4257
    Helixi433 – 4353
    Beta strandi443 – 4464
    Turni448 – 4503
    Beta strandi453 – 4553
    Helixi457 – 46812
    Helixi473 – 4786
    Beta strandi484 – 4874

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GOWX-ray2.60A/B1-489[»]
    1UWIX-ray2.55A/B/C/D1-489[»]
    1UWQX-ray2.02A/B1-489[»]
    1UWRX-ray2.14A/B1-489[»]
    1UWSX-ray1.95A/B1-489[»]
    1UWTX-ray1.95A/B1-489[»]
    1UWUX-ray1.95A/B1-489[»]
    2CEQX-ray2.14A/B1-489[»]
    2CERX-ray2.29A/B1-489[»]
    4EAMX-ray1.70A/B1-489[»]
    4EANX-ray1.75A/B1-489[»]
    ProteinModelPortaliP22498.
    SMRiP22498. Positions 1-489.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP22498.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 1 family.Curated

    Phylogenomic databases

    eggNOGiCOG2723.
    HOGENOMiHOG000088630.
    KOiK01190.
    OMAiGEYTEMG.

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR001360. Glyco_hydro_1.
    IPR018120. Glyco_hydro_1_AS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PANTHERiPTHR10353. PTHR10353. 1 hit.
    PfamiPF00232. Glyco_hydro_1. 2 hits.
    [Graphical view]
    PRINTSiPR00131. GLHYDRLASE1.
    SUPFAMiSSF51445. SSF51445. 1 hit.
    PROSITEiPS00572. GLYCOSYL_HYDROL_F1_1. 1 hit.
    PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P22498-1 [UniParc]FASTAAdd to Basket

    « Hide

    MYSFPNSFRF GWSQAGFQSE MGTPGSEDPN TDWYKWVHDP ENMAAGLVSG    50
    DLPENGPGYW GNYKTFHDNA QKMGLKIARL NVEWSRIFPN PLPRPQNFDE 100
    SKQDVTEVEI NENELKRLDE YANKDALNHY REIFKDLKSR GLYFILNMYH 150
    WPLPLWLHDP IRVRRGDFTG PSGWLSTRTV YEFARFSAYI AWKFDDLVDE 200
    YSTMNEPNVV GGLGYVGVKS GFPPGYLSFE LSRRAMYNII QAHARAYDGI 250
    KSVSKKPVGI IYANSSFQPL TDKDMEAVEM AENDNRWWFF DAIIRGEITR 300
    GNEKIVRDDL KGRLDWIGVN YYTRTVVKRT EKGYVSLGGY GHGCERNSVS 350
    LAGLPTSDFG WEFFPEGLYD VLTKYWNRYH LYMYVTENGI ADDADYQRPY 400
    YLVSHVYQVH RAINSGADVR GYLHWSLADN YEWASGFSMR FGLLKVDYNT 450
    KRLYWRPSAL VYREIATNGA ITDEIEHLNS VPPVKPLRH 489
    Length:489
    Mass (Da):56,692
    Last modified:June 20, 2001 - v2
    Checksum:iB56F6CE8EE4A429D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti235 – 2351A → H in AAA72843. (PubMed:2121622)Curated

    Mass spectrometryi

    Molecular mass is 56754.8±4.9 Da from positions 1 - 489. Determined by ESI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M34696 Genomic DNA. Translation: AAA72843.1.
    AF133096 Genomic DNA. Translation: AAD21094.1.
    AE006641 Genomic DNA. Translation: AAK43121.1.
    PIRiB90483.
    JQ0767.
    RefSeqiNP_344331.1. NC_002754.1.
    WP_009992676.1. NC_002754.1.

    Genome annotation databases

    EnsemblBacteriaiAAK43121; AAK43121; SSO3019.
    GeneIDi1453040.
    KEGGisso:SSO3019.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M34696 Genomic DNA. Translation: AAA72843.1 .
    AF133096 Genomic DNA. Translation: AAD21094.1 .
    AE006641 Genomic DNA. Translation: AAK43121.1 .
    PIRi B90483.
    JQ0767.
    RefSeqi NP_344331.1. NC_002754.1.
    WP_009992676.1. NC_002754.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GOW X-ray 2.60 A/B 1-489 [» ]
    1UWI X-ray 2.55 A/B/C/D 1-489 [» ]
    1UWQ X-ray 2.02 A/B 1-489 [» ]
    1UWR X-ray 2.14 A/B 1-489 [» ]
    1UWS X-ray 1.95 A/B 1-489 [» ]
    1UWT X-ray 1.95 A/B 1-489 [» ]
    1UWU X-ray 1.95 A/B 1-489 [» ]
    2CEQ X-ray 2.14 A/B 1-489 [» ]
    2CER X-ray 2.29 A/B 1-489 [» ]
    4EAM X-ray 1.70 A/B 1-489 [» ]
    4EAN X-ray 1.75 A/B 1-489 [» ]
    ProteinModelPortali P22498.
    SMRi P22498. Positions 1-489.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 273057.SSO3019.

    Protein family/group databases

    CAZyi GH1. Glycoside Hydrolase Family 1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAK43121 ; AAK43121 ; SSO3019 .
    GeneIDi 1453040.
    KEGGi sso:SSO3019.

    Phylogenomic databases

    eggNOGi COG2723.
    HOGENOMi HOG000088630.
    KOi K01190.
    OMAi GEYTEMG.

    Enzyme and pathway databases

    BioCyci SSOL273057:GCH2-2809-MONOMER.
    BRENDAi 3.2.1.23. 6163.
    SABIO-RK P22498.

    Miscellaneous databases

    EvolutionaryTracei P22498.

    Family and domain databases

    Gene3Di 3.20.20.80. 1 hit.
    InterProi IPR001360. Glyco_hydro_1.
    IPR018120. Glyco_hydro_1_AS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    PANTHERi PTHR10353. PTHR10353. 1 hit.
    Pfami PF00232. Glyco_hydro_1. 2 hits.
    [Graphical view ]
    PRINTSi PR00131. GLHYDRLASE1.
    SUPFAMi SSF51445. SSF51445. 1 hit.
    PROSITEi PS00572. GLYCOSYL_HYDROL_F1_1. 1 hit.
    PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and sequencing of a new beta-galactosidase-encoding archaebacterial gene."
      Cubellis M.V., Rozzo C., Montecucchi P., Rossi M.
      Gene 94:89-94(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-33.
      Strain: DSM 5833 / MT-4.
    2. "Coordinate transcriptional control in the hyperthermophilic archaeon Sulfolobus solfataricus."
      Haseltine C., Montalvo-Rodriguez R., Bini E., Carl A., Blum P.
      J. Bacteriol. 181:3920-3927(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 98/2.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
    4. "Thermal stability and aggregation of Sulfolobus solfataricus beta-glycosidase are dependent upon the N-epsilon-methylation of specific lysyl residues: critical role of in vivo post-translational modifications."
      Febbraio F., Andolfo A., Tanfani F., Briante R., Gentile F., Formisano S., Vaccaro C., Scire A., Bertoli E., Pucci P., Nucci R.
      J. Biol. Chem. 279:10185-10194(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT LYS-116; LYS-135; LYS-273; LYS-311 AND LYS-332, MASS SPECTROMETRY.
    5. "Crystal structure of the beta-glycosidase from the hyperthermophilic archeon Sulfolobus solfataricus: resilience as a key factor in thermostability."
      Aguilar C.F., Sanderson I., Moracci M., Ciaramella M., Nucci R., Rossi M., Pearl L.H.
      J. Mol. Biol. 271:789-802(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
      Strain: DSM 5833 / MT-4.

    Entry informationi

    Entry nameiBGAL_SULSO
    AccessioniPrimary (citable) accession number: P22498
    Secondary accession number(s): Q9V2Z5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1991
    Last sequence update: June 20, 2001
    Last modified: October 1, 2014
    This is version 117 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Caution

    The DNA coding for this protein is not found in the complete genome of strain 98/2. Sequence in PubMed:10383958 could have originated from another strain.Curated

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3