P52699 · BLAB_SERMA
- ProteinMetallo-beta-lactamase type 2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids246 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Confers resistance to the different beta-lactams antibiotics (penicillin, cephalosporin and carbapenem) via the hydrolysis of the beta-lactam ring.
Catalytic activity
- a beta-lactam + H2O = a substituted beta-amino acid
Cofactor
Note: Binds 2 Zn2+ ions per subunit.
Activity regulation
Inhibited by captopril stereoisomers, Hg2+, Fe2+, Cu2+ and by chelating agents such as EDTA (PubMed:26482303, PubMed:8141584).
This enzyme is not susceptible to inactivation by the beta-lactamase-blocking agents clavulanic acid or cloxacillin (PubMed:8141584).
This enzyme is not susceptible to inactivation by the beta-lactamase-blocking agents clavulanic acid or cloxacillin (PubMed:8141584).
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
0.74 μM | meropenem | |||||
1.24 μM | ceftazidime | |||||
2.07 μM | ceftizoxime and panipenem | |||||
2.13 μM | cefoperazone | |||||
2.15 μM | ampicillin | |||||
3.97 μM | aztreonam | |||||
7.33 μM | imipenem | |||||
7.55 μM | moxalactam | |||||
7.74 μM | cephaloridine |
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 95 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 97 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 99 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 157 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 176 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 179 | substrate | ||||
Sequence: K | ||||||
Binding site | 185 | substrate | ||||
Sequence: N | ||||||
Binding site | 215 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | periplasmic space | |
Molecular Function | beta-lactamase activity | |
Molecular Function | zinc ion binding | |
Biological Process | antibiotic catabolic process | |
Biological Process | response to antibiotic |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMetallo-beta-lactamase type 2
- EC number
- Alternative names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Yersiniaceae > Serratia
Accessions
- Primary accessionP52699
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-18 | |||||
Sequence: MSKLSVFFIFLFCSIATA | ||||||
Chain | PRO_0000016946 | 19-246 | Metallo-beta-lactamase type 2 | |||
Sequence: AESLPDLKIEKLDEGVYVHTSFEEVNGWGVVPKHGLVVLVNAEAYLIDTPFTAKDTEKLVTWFVERGYKIKGSISSHFHSDSTGGIEWLNSRSIPTYASELTNELLKKDGKVQATNSFSGVNYWLVKNKIEVFYPGPGHTPDNVVVWLPERKILFGGCFIKPYGLGNLGDANIEAWPKSAKLLKSKYGKAKLVVPSHSEVGDASLLKLTLEQAVKGLNESKKPSKPSN |
Interaction
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length246
- Mass (Da)27,120
- Last updated1996-10-01 v1
- Checksum9B2599E8F1B22D36
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
S71932 EMBL· GenBank· DDBJ | AAB30289.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
D50438 EMBL· GenBank· DDBJ | BAA08930.1 EMBL· GenBank· DDBJ | Genomic DNA |