Beta-lactamase OXA-2
Details
- Name
- Beta-lactamase OXA-2
- Synonyms
- 3.5.2.6
- oxa2
- Penicillinase
- Gene Name
- bla
- Organism
- Salmonella typhimurium
- Amino acid sequence
>lcl|BSEQ0022472|Beta-lactamase OXA-2 MAIRIFAILFSIFSLATFAHAQEGTLERSDWRKFFSEFQAKGTIVVADERQADRAMLVFD PVRSKKRYSPASTFKIPHTLFALDAGAVRDEFQIFRWDGVNRGFAGHNQDQDLRSAMRNS TVWVYELFAKEIGDDKARRYLKKIDYGNADPSTSNGDYWIEGSLAISAQEQIAFLRKLYR NELPFRVEHQRLVKDLMIVEAGRNWILRAKTGWEGRMGWWVGWVEWPTGSVFFALNIDTP NRMDDLFKREAIVRAILRSIEALPPNPAVNSDAAR
- Number of residues
- 275
- Molecular Weight
- 31685.78
- Theoretical pI
- 9.77
- GO Classification
- Functionsbeta-lactamase activity / penicillin bindingProcessesantibiotic catabolic process / response to antibiotic
- General Function
- Penicillin binding
- Specific Function
- This is an oxacillin-hydrolyzing beta-lactamase.
- Pfam Domain Function
- Transpeptidase (PF00905)
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasmic
- Gene sequence
>lcl|BSEQ0003524|828 bp ATGGCAATCCGAATCTTCGCGATACTTTTCTCCATTTTTTCTCTTGCCACTTTCGCGCAT GCGCAAGAAGGCACGCTAGAACGTTCTGACTGGAGGAAGTTTTTCAGCGAATTTCAAGCC AAAGGCACGATAGTTGTGGCAGACGAACGCCAAGCGGATCGTGCCATGTTGGTTTTTGAT CCTGTGCGATCGAAGAAACGCTACTCGCCTGCATCGACATTCAAGATACCTCATACACTT TTTGCACTTGATGCAGGCGCTGTTCGTGATGAGTTCCAGATTTTTCGATGGGACGGCGTT AACAGGGGCTTTGCAGGCCACAATCAAGACCAAGATTTGCGATCAGCAATGCGGAATTCT ACTGTTTGGGTGTATGAGCTATTTGCAAAGGAAATTGGTGATGACAAAGCTCGGCGCTAT TTGAAGAAAATCGACTATGGCAACGCCGATCCTTCGACAAGTAATGGCGATTACTGGATA GAAGGCAGCCTTGCAATCTCGGCGCAGGAGCAAATTGCATTTCTCAGGAAGCTCTATCGT AACGAGCTGCCCTTTCGGGTAGAACATCAGCGCTTGGTCAAGGATCTCATGATTGTGGAA GCCGGTCGCAACTGGATACTGCGTGCAAAGACGGGCTGGGAAGGCCGTATGGGTTGGTGG GTAGGATGGGTTGAGTGGCCGACTGGCTCCGTATTCTTCGCACTGAATATTGATACGCCA AACAGAATGGATGATCTTTTCAAGAGGGAGGCAATCGTGCGGGCAATCCTTCGCTCTATT GAAGCGTTACCGCCCAACCCGGCAGTCAACTCGGACGCTGCGCGATAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P0A1V8 UniProtKB Entry Name BLO2_SALTM GenBank Protein ID 154222 GenBank Gene ID M25261 - General References
- Dale JW, Godwin D, Mossakowska D, Stephenson P, Wall S: Sequence of the OXA2 beta-lactamase: comparison with other penicillin-reactive enzymes. FEBS Lett. 1985 Oct 21;191(1):39-44. [Article]
- Mossakowska D, Ali NA, Dale JW: Oxacillin-hydrolysing beta-lactamases. A comparative analysis at nucleotide and amino acid sequence levels. Eur J Biochem. 1989 Mar 15;180(2):309-18. [Article]
- Holland S, Dale JW: Improved purification and characterization of the OXA-2 beta-lactamase. Biochem J. 1984 Dec 15;224(3):1009-13. [Article]
- Nucken EJ, Henschke RB, Schmidt FR: Nucleotide sequence of an OXA-2 beta-lactamase gene from the R-plasmid R1767 derived plasmid pBP11 and comparison to closely related resistance determinants found in R46 and Tn2603. J Gen Microbiol. 1989 Apr;135(4):761-5. [Article]
- Ledent P, Frere JM: Substrate-induced inactivation of the OXA2 beta-lactamase. Biochem J. 1993 Nov 1;295 ( Pt 3):871-8. [Article]