P80298 (BLAC_PROVU) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 56.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Beta-lactamase EC=3.5.2.6 Alternative name(s): Penicillinase |
| Organism | Proteus vulgaris |
| Taxonomic identifier | 585 [NCBI] |
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Proteus![]() |
Protein attributes
| Sequence length | 271 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Hydrolyzes broad-spectrum beta-lactam antibiotics. Active against cephalosporins. |
| Catalytic activity | A beta-lactam + H2O = a substituted beta-amino acid. |
| Subunit structure | Monomer. |
| Sequence similarities | Belongs to the class-A beta-lactamase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Antibiotic resistance |
| Molecular function | Hydrolase |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological_process | beta-lactam antibiotic catabolic process Inferred from electronic annotation. Source: InterPro response to antibioticInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular_function | beta-lactamase activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| [1] | "Chromosomally encoded cephalosporin-hydrolyzing beta-lactamase of Proteus vulgaris RO104 belongs to Ambler's class A." Peduzzi J., Reynaud A., Barthelemy M., Baron P., Labia R. Biochim. Biophys. Acta 1207:31-39(1994) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE. Strain: RO104. |
Cross-references
Sequence databases | |
|---|---|
| PIR | S47620. |
3D structure databases | |
| ProteinModelPortal | P80298. |
| SMR | P80298. Positions 4-267. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| Gene3D | 3.40.710.10. 1 hit. |
| InterPro | IPR001466. Beta-lactam-related. IPR012338. Beta-lactam/transpept-like. IPR000871. Beta-lactam_class-A/D. IPR023650. Beta-lactam_class-A_AS. [Graphical view] |
| Pfam | PF00144. Beta-lactamase. 1 hit. [Graphical view] |
| PRINTS | PR00118. BLACTAMASEA. |
| SUPFAM | SSF56601. PBP_transp_fold. 1 hit. |
| PROSITE | PS00146. BETA_LACTAMASE_A. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| ChEMBL | CHEMBL4782. |
Entry information
| Entry name | BLAC_PROVU | ||||||||
| Accession | Primary (citable) accession number: P80298 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
