NameBeta-lactamase OXA-2
Synonyms
  • 3.5.2.6
  • oxa2
  • Penicillinase
Gene Namebla
OrganismSalmonella typhimurium
Amino acid sequence
>lcl|BSEQ0022472|Beta-lactamase OXA-2
MAIRIFAILFSIFSLATFAHAQEGTLERSDWRKFFSEFQAKGTIVVADERQADRAMLVFD
PVRSKKRYSPASTFKIPHTLFALDAGAVRDEFQIFRWDGVNRGFAGHNQDQDLRSAMRNS
TVWVYELFAKEIGDDKARRYLKKIDYGNADPSTSNGDYWIEGSLAISAQEQIAFLRKLYR
NELPFRVEHQRLVKDLMIVEAGRNWILRAKTGWEGRMGWWVGWVEWPTGSVFFALNIDTP
NRMDDLFKREAIVRAILRSIEALPPNPAVNSDAAR
Number of residues275
Molecular Weight31685.78
Theoretical pI9.77
GO Classification
Functions
  • penicillin binding
  • beta-lactamase activity
Processes
  • response to antibiotic
  • antibiotic catabolic process
General FunctionPenicillin binding
Specific FunctionThis is an oxacillin-hydrolyzing beta-lactamase.
Pfam Domain Function
Transmembrane RegionsNot Available
GenBank Protein ID154222
UniProtKB IDP0A1V8
UniProtKB Entry NameBLO2_SALTM
Cellular LocationCytoplasmic
Gene sequence
>lcl|BSEQ0003524|828 bp
ATGGCAATCCGAATCTTCGCGATACTTTTCTCCATTTTTTCTCTTGCCACTTTCGCGCAT
GCGCAAGAAGGCACGCTAGAACGTTCTGACTGGAGGAAGTTTTTCAGCGAATTTCAAGCC
AAAGGCACGATAGTTGTGGCAGACGAACGCCAAGCGGATCGTGCCATGTTGGTTTTTGAT
CCTGTGCGATCGAAGAAACGCTACTCGCCTGCATCGACATTCAAGATACCTCATACACTT
TTTGCACTTGATGCAGGCGCTGTTCGTGATGAGTTCCAGATTTTTCGATGGGACGGCGTT
AACAGGGGCTTTGCAGGCCACAATCAAGACCAAGATTTGCGATCAGCAATGCGGAATTCT
ACTGTTTGGGTGTATGAGCTATTTGCAAAGGAAATTGGTGATGACAAAGCTCGGCGCTAT
TTGAAGAAAATCGACTATGGCAACGCCGATCCTTCGACAAGTAATGGCGATTACTGGATA
GAAGGCAGCCTTGCAATCTCGGCGCAGGAGCAAATTGCATTTCTCAGGAAGCTCTATCGT
AACGAGCTGCCCTTTCGGGTAGAACATCAGCGCTTGGTCAAGGATCTCATGATTGTGGAA
GCCGGTCGCAACTGGATACTGCGTGCAAAGACGGGCTGGGAAGGCCGTATGGGTTGGTGG
GTAGGATGGGTTGAGTGGCCGACTGGCTCCGTATTCTTCGCACTGAATATTGATACGCCA
AACAGAATGGATGATCTTTTCAAGAGGGAGGCAATCGTGCGGGCAATCCTTCGCTCTATT
GAAGCGTTACCGCCCAACCCGGCAGTCAACTCGGACGCTGCGCGATAA
GenBank Gene IDM25261
GeneCard IDNot Available
GenAtlas IDNot Available
HGNC IDNot Available
Chromosome LocationNot Available
LocusNot Available
References
  1. 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. 3876949
  2. 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. 2538329
  3. Holland S, Dale JW: Improved purification and characterization of the OXA-2 beta-lactamase. Biochem J. 1984 Dec 15;224(3):1009-13. 6335398
  4. 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. 2689593
  5. Ledent P, Frere JM: Substrate-induced inactivation of the OXA2 beta-lactamase. Biochem J. 1993 Nov 1;295 ( Pt 3):871-8. 8240304