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P52664 (BLAB_PROVU) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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-lactamase

EC=3.5.2.6
Alternative name(s):
Cefuroximase
Gene names
Name:blaB
Synonyms:cumA
OrganismProteus vulgaris
Taxonomic identifier585 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeProteus

Protein attributes

Sequence length300 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hydrolyzes broad-spectrum beta-lactam antibiotics. Active against cephalosporins such as cefuroxime and cefotaxime.

Catalytic activity

A beta-lactam + H2O = a substituted beta-amino acid.

Subunit structure

Monomer By similarity.

Sequence similarities

Belongs to the class-A beta-lactamase family.

Ontologies

Keywords
   Biological processAntibiotic resistance
   DomainSignal
   Molecular functionHydrolase
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processbeta-lactam antibiotic catabolic process

Inferred from electronic annotation. Source: InterPro

response to antibiotic

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionbeta-lactamase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2929 Potential
Chain30 – 300271Beta-lactamase
PRO_0000017008

Regions

Region239 – 2413Substrate binding By similarity

Sites

Active site751Acyl-ester intermediate By similarity

Natural variations

Natural variant131T → A in strain: 5E78-1.
Natural variant231V → A in strain: 5E78-1.
Natural variant30 – 312NT → DN in strain: 5E78-1.
Natural variant401S → N in strain: 5E78-1.
Natural variant581E → K in strain: 5E78-1.
Natural variant881E → A in strain: 5E78-1.
Natural variant1191V → T in strain: 5E78-1.
Natural variant1231S → T in strain: 5E78-1.
Natural variant1261Q → E in strain: 5E78-1.
Natural variant2241H → N in strain: 5E78-1.
Natural variant2351I → V in strain: 5E78-1.
Natural variant2571K → E in strain: 5E78-1.
Natural variant2831V → A in strain: 5E78-1.
Natural variant2861T → A in strain: 5E78-1.

Secondary structure

........................................... 300
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P52664 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 2719AF2464F1CD77

FASTA30032,992
        10         20         30         40         50         60 
MTMFKTTFRQ TATIAVSLIS LLVSPMLWAN TNNTIEEQLS TLEKYSQGRL GVALINTEDN 

        70         80         90        100        110        120 
SQITYRGEER FAMASTSKVM AVAAVLKESE KQAGLLDKNI TIKKSDLVAY SPITEKHLVT 

       130        140        150        160        170        180 
GMSLAQLSAA TLQYSDNTAM NKILDYLGGP AKVTQFARSI NDVTYRLDRK EPELNTAIHG 

       190        200        210        220        230        240 
DPRDTTSPIA MAKSLQALTL GDALGQSQRQ QLVTWLKGNT TGDHSIKAGL PKHWIVGDKT 

       250        260        270        280        290        300 
GSGDYGTTND IAVIWPKNHA PLILVVYFTQ QEQDAKYRKD IIVKATEIVT KEISNSPQTK 

« Hide

References

[1]"A common system controls the induction of very different genes. The class-A beta-lactamase of Proteus vulgaris and the enterobacterial class-C beta-lactamase."
Datz M., Joris B., Azab E.A., Galleni M., van Beeumen J., Frere J.-M., Martin H.H.
Eur. J. Biochem. 226:149-157(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: B317.
[2]Okuguchi M., Komai T., Makajima N., Eguchi H., Kuboki A., Ito T., Meguro M., Nakata T., Sugimoto K.
Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 5E78-1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X80128 Genomic DNA. Translation: CAA56427.1.
D37831 Genomic DNA. Translation: BAA07084.1.
PIRS51044.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1HZOX-ray1.75A/B32-300[»]
ProteinModelPortalP52664.
SMRP52664. Positions 33-296.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.40.710.10. 1 hit.
InterProIPR012338. Beta-lactam/transpept-like.
IPR000871. Beta-lactam_class-A/D.
IPR023650. Beta-lactam_class-A_AS.
[Graphical view]
PRINTSPR00118. BLACTAMASEA.
SUPFAMSSF56601. SSF56601. 1 hit.
PROSITEPS00146. BETA_LACTAMASE_A. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP52664.

Entry information

Entry nameBLAB_PROVU
AccessionPrimary (citable) accession number: P52664
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: October 16, 2013
This is version 68 of the entry and version 1 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