Reviewed,
UniProtKB/Swiss-Prot P30897 (BLAC_PROMI)
Last modified
June 16, 2009.
Version 49.
History...
Clusters with 100%,
90%,
50% identity |
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: Beta-lactamase EC=3.5.2.6 Alternative name(s): Carbenicillinase | ||
| Gene names |
| ||
| Organism | Proteus mirabilis | ||
| Taxonomic identifier | 584 [NCBI] | ||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Proteus |
Protein attributes
| Sequence length | 298 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 carbenicillin. |
| Catalytic activity | A beta-lactam + H2O = a substituted beta-amino acid. |
| Sequence similarities | Belongs to the class-A beta-lactamase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Antibiotic resistance |
| Domain | Signal |
| Molecular function | Hydrolase |
| PTM | Disulfide bond |
| 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)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 28 | 28 | Potential | ||||||||
| Chain | 29 – 298 | 270 | Beta-lactamase | PRO_0000017007 | |||||||
Regions | |||||||||||
| Region | 237 – 239 | 3 | Substrate binding By similarity | ||||||||
Sites | |||||||||||
| Active site | 72 | 1 | Acyl-ester intermediate By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 79 ↔ 126 | By similarity | |||||||||
Sequences
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References
| [1] | "Nucleotide sequence and characterization of a carbenicillin-hydrolyzing penicillinase gene from Proteus mirabilis." Sakurai Y., Tsukamoto K., Sawai T. J. Bacteriol. 173:7038-7041(1991) [PubMed: 1840585] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 29-37. Strain: GN79. |
Cross-references
Sequence databases | |
|---|---|
| D13209 Genomic DNA. Translation: BAA02496.1. | |
| PIR | A41381. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1JTG based on UniProtKB P00810. |
| ModBase | Search... |
Enzyme and pathway databases | |
| BRENDA | 3.5.2.6. 639. |
Family and domain databases | |
| InterPro | IPR001466. Beta_lactamase-related. IPR000871. Beta_lactamase_A/D. [Graphical view] |
| Pfam | PF00144. Beta-lactamase. 1 hit. [Graphical view] |
| PRINTS | PR00118. BLACTAMASEA. |
| PROSITE | PS00146. BETA_LACTAMASE_A. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | BLAC_PROMI | ||||||||
| Accession | Primary (citable) accession number: P30897 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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