Reviewed,
UniProtKB/Swiss-Prot P0A9Z7 (BLA2_ECOLX)
Last modified
June 16, 2009.
Version 22.
History...
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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 SHV-2 EC=3.5.2.6 Alternative name(s): SHV-2A | ||||
| Gene names |
| ||||
| Encoded on | Plasmid pBWH77 Ref.2 | ||||
| Organism | Escherichia coli | ||||
| Taxonomic identifier | 562 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 286 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 | This enzyme hydrolyzes cefotaxime, ceftazidime and other broad spectrum cephalosporins. |
| 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 Plasmid |
| 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 – 21 | 21 | Ref.2 | ||||||||
| Chain | 22 – 286 | 265 | Beta-lactamase SHV-2 | PRO_0000016981 | |||||||
Regions | |||||||||||
| Region | 230 – 232 | 3 | Substrate binding By similarity | ||||||||
Sites | |||||||||||
| Active site | 66 | 1 | Acyl-ester intermediate By similarity | ||||||||
| Active site | 164 | 1 | Proton acceptor By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 73 ↔ 119 | By similarity | |||||||||
Sequences
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References
| [1] | "Automated thermal cycling is superior to traditional methods for nucleotide sequencing of bla(SHV) genes." Bradford P.A. Antimicrob. Agents Chemother. 43:2960-2963(1999) [PubMed: 10582889] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC BAA-204 / JC2926 pBP60-1. |
| [2] | "Single amino acid substitution between SHV-1 beta-lactamase and cefotaxime-hydrolyzing SHV-2 enzyme." Barthelemy M., Peduzzi J., Yaghlane H.B., Labia R. FEBS Lett. 231:217-220(1988) [PubMed: 3129309] [Abstract] Cited for: PROTEIN SEQUENCE OF 22-286. Strain: A2302. |
Cross-references
Sequence databases | |
|---|---|
| AF148851 Genomic DNA. Translation: AAD37413.1. | |
| PIR | S02434. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1N9B based on UniProtKB P30896. |
| SMR | P0A9Z7. Positions 22-286. |
| ModBase | Search... |
Enzyme and pathway databases | |
| BRENDA | 3.5.2.6. 246. |
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 | BLA2_ECOLX | ||||||||
| Accession | Primary (citable) accession number: P0A9Z7 Secondary accession number(s): P14558 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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