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P22498 (BGAL_SULSO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Beta-galactosidase

Short name=Lactase
EC=3.2.1.23
Gene names
Name:lacS
Ordered Locus Names:SSO3019
OrganismSulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) [Reference proteome] [HAMAP]
Taxonomic identifier273057 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus

Protein attributes

Sequence length489 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Subunit structure

Homotetramer.

Sequence similarities

Belongs to the glycosyl hydrolase 1 family.

Caution

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

Mass spectrometry

Molecular mass is 56754.8±4.9 Da from positions 1 - 489. Determined by ESI. Ref.4

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 489489Beta-galactosidase
PRO_0000063867

Sites

Active site2061Proton donor Potential
Active site3871Nucleophile By similarity
Site761Not N6-methylated
Site1021Not N6-methylated
Site1241Not N6-methylated
Site1381Not N6-methylated

Amino acid modifications

Modified residue1161N6-methyllysine; partial Ref.4
Modified residue1351N6-methyllysine Ref.4
Modified residue2731N6-methyllysine; partial Ref.4
Modified residue3111N6-methyllysine; partial Ref.4
Modified residue3321N6-methyllysine Ref.4

Experimental info

Sequence conflict2351A → H in AAA72843. Ref.1

Secondary structure

.................................................................................. 489
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P22498 [UniParc].

Last modified June 20, 2001. Version 2.
Checksum: B56F6CE8EE4A429D

FASTA48956,692
        10         20         30         40         50         60 
MYSFPNSFRF GWSQAGFQSE MGTPGSEDPN TDWYKWVHDP ENMAAGLVSG DLPENGPGYW 

        70         80         90        100        110        120 
GNYKTFHDNA QKMGLKIARL NVEWSRIFPN PLPRPQNFDE SKQDVTEVEI NENELKRLDE 

       130        140        150        160        170        180 
YANKDALNHY REIFKDLKSR GLYFILNMYH WPLPLWLHDP IRVRRGDFTG PSGWLSTRTV 

       190        200        210        220        230        240 
YEFARFSAYI AWKFDDLVDE YSTMNEPNVV GGLGYVGVKS GFPPGYLSFE LSRRAMYNII 

       250        260        270        280        290        300 
QAHARAYDGI KSVSKKPVGI IYANSSFQPL TDKDMEAVEM AENDNRWWFF DAIIRGEITR 

       310        320        330        340        350        360 
GNEKIVRDDL KGRLDWIGVN YYTRTVVKRT EKGYVSLGGY GHGCERNSVS LAGLPTSDFG 

       370        380        390        400        410        420 
WEFFPEGLYD VLTKYWNRYH LYMYVTENGI ADDADYQRPY YLVSHVYQVH RAINSGADVR 

       430        440        450        460        470        480 
GYLHWSLADN YEWASGFSMR FGLLKVDYNT KRLYWRPSAL VYREIATNGA ITDEIEHLNS 


VPPVKPLRH 

« Hide

References

« Hide 'large scale' references
[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]"The complete genome of the crenarchaeon Sulfolobus solfataricus P2."
She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J., Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G., Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J., Medina N., Peng X. expand/collapse author list , Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C., Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T., Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.
Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M34696 Genomic DNA. Translation: AAA72843.1.
AF133096 Genomic DNA. Translation: AAD21094.1.
AE006641 Genomic DNA. Translation: AAK43121.1.
PIRB90483.
JQ0767.
RefSeqNP_344331.1. NC_002754.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP22498.
SMRP22498. Positions 1-489.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING273057.SSO3019.

Protein family/group databases

CAZyGH1. Glycoside Hydrolase Family 1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK43121; AAK43121; SSO3019.
GeneID1453040.
KEGGsso:SSO3019.

Phylogenomic databases

eggNOGCOG2723.
HOGENOMHOG000088630.
KOK01190.
OMAGEYTEMG.

Enzyme and pathway databases

BioCycSSOL273057:GCH2-2809-MONOMER.
BRENDA3.2.1.23. 6163.
SABIO-RKP22498.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR001360. Glyco_hydro_1.
IPR018120. Glyco_hydro_1_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERPTHR10353. PTHR10353. 1 hit.
PfamPF00232. Glyco_hydro_1. 2 hits.
[Graphical view]
PRINTSPR00131. GLHYDRLASE1.
SUPFAMSSF51445. SSF51445. 1 hit.
PROSITEPS00572. GLYCOSYL_HYDROL_F1_1. 1 hit.
PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP22498.

Entry information

Entry nameBGAL_SULSO
AccessionPrimary (citable) accession number: P22498
Secondary accession number(s): Q9V2Z5
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: June 20, 2001
Last modified: May 14, 2014
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries