Q51574 (BLO15_PSEAI) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 60.
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 OXA-15 EC=3.5.2.6 | ||||
| Gene names |
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| Encoded on | Plasmid pMLH54 | ||||
| Organism | Pseudomonas aeruginosa | ||||
| Taxonomic identifier | 287 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas › ![]() |
Protein attributes
| Sequence length | 275 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Hydrolyzes oxacillin, first-generation cephalosporins and ceftazidime. Does not hydrolyze cefotaxime or carbapenems. |
| Catalytic activity | A beta-lactam + H2O = a substituted beta-amino acid. |
| Sequence similarities | Belongs to the class-D beta-lactamase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Antibiotic resistance |
| Domain | Signal |
| Molecular function | Hydrolase |
| Technical term | Plasmid |
| Gene Ontology (GO) | |
| Biological_process | antibiotic catabolic process Inferred from electronic annotation. Source: InterPro peptidoglycan-based cell wall biogenesisInferred 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 penicillin bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 21 | 21 | By similarity | ||||||
| Chain | 22 – 275 | 254 | Beta-lactamase OXA-15 | PRO_0000017032 | |||||
Regions | |||||||||
| Region | 210 – 212 | 3 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Active site | 72 | 1 | Acyl-ester intermediate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 75 | 1 | N6-carboxylysine By similarity | ||||||
Sequences
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References
| [1] | "OXA-15, an extended-spectrum variant of OXA-2 beta-lactamase, isolated from a Pseudomonas aeruginosa strain." Danel F., Hall L.M.C., Gur D., Livermore D.M. Antimicrob. Agents Chemother. 41:785-790(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION. Strain: AH. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | U63835 Genomic DNA. Translation: AAB05874.1. |
3D structure databases | |
| ProteinModelPortal | Q51574. |
| SMR | Q51574. Positions 25-265. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| Gene3D | 3.40.710.10. 1 hit. |
| InterPro | IPR012338. Beta-lactam/transpept-like. IPR002137. Beta-lactam_class-D_AS. IPR001460. PCN-bd_Tpept. [Graphical view] |
| Pfam | PF00905. Transpeptidase. 1 hit. [Graphical view] |
| SUPFAM | SSF56601. PBP_transp_fold. 1 hit. |
| PROSITE | PS00337. BETA_LACTAMASE_D. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | BLO15_PSEAI | ||||||||
| Accession | Primary (citable) accession number: Q51574 | ||||||||
| 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
