Beta-lactamase type II
Details
- Name
- Beta-lactamase type II
- Synonyms
- 3.5.2.6
- Cephalosporinase
- cfiA
- Imipenem-cefoxitin hydrolyzing enzyme
- Penicillinase
- Gene Name
- ccrA
- Organism
- Bacteroides fragilis
- Amino acid sequence
>lcl|BSEQ0010843|Beta-lactamase type II MKTVFILISMLFPVAVMAQKSVKISDDISITQLSDKVYTYVSLAEIEGWGMVPSNGMIVI NNHQAALLDTPINDAQTEMLVNWVTDSLHAKVTTFIPNHWHGDCIGGLGYLQRKGVQSYA NQMTIDLAKEKGLPVPEHGFTDSLTVSLDGMPLQCYYLGGGHATDNIVVWLPTENILFGG CMLKDNQATSIGNISDADVTAWPKTLDKVKAKFPSARYVVPGHGDYGGTELIEHTKQIVN QYIESTSKP
- Number of residues
- 249
- Molecular Weight
- 27257.06
- Theoretical pI
- 5.5
- GO Classification
- Functionsbeta-lactamase activity / zinc ion bindingProcessesantibiotic catabolic process / response to antibiotic
- General Function
- Zinc ion binding
- Specific Function
- Can hydrolyze carbapenem compounds.
- Pfam Domain Function
- Lactamase_B (PF00753)
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasmic
- Gene sequence
>lcl|BSEQ0002412|750 bp ATGAAAACAGTATTTATCCTTATCTCCATGCTTTTCCCTGTCGCAGTTATGGCACAGAAA AGCGTAAAAATATCCGATGACATCAGTATCACCCAACTCTCGGACAAAGTGTACACTTAT GTATCCCTCGCCGAAATCGAAGGATGGGGTATGGTACCTTCCAACGGGATGATTGTTATC AACAACCACCAGGCAGCGTTGCTGGACACACCGATCAATGACGCACAAACGGAAATGCTG GTCAACTGGGTGACAGACTCTTTGCATGCCAAAGTCACCACGTTTATCCCGAACCACTGG CACGGCGATTGTATTGGCGGACTGGGTTACCTGCAAAGGAAAGGTGTCCAATCATACGCG AACCAGATGACGATAGACCTCGCCAAGGAAAAAGGGTTGCCCGTACCGGAACATGGATTC ACCGATTCACTGACCGTCAGCTTGGACGGCATGCCTCTCCAATGTTATTATTTAGGAGGC GGACATGCGACCGACAATATCGTGGTTTGGCTGCCGACAGAGAATATCCTTTTTGGCGGA TGTATGCTTAAAGACAACCAGGCGACAAGCATCGGCAACATCTCGGACGCGGACGTGACG GCATGGCCGAAAACTCTCGATAAGGTAAAAGCCAAGTTCCCCTCGGCCCGTTACGTCGTG CCCGGACATGGCGACTATGGCGGAACCGAACTGATAGAGCATACCAAGCAGATCGTGAAC CAATATATAGAAAGCACTTCAAAGCCATAG
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P25910 UniProtKB Entry Name BLAB_BACFG GenBank Protein ID 143932 GenBank Gene ID M63556 - General References
- Rasmussen BA, Gluzman Y, Tally FP: Cloning and sequencing of the class B beta-lactamase gene (ccrA) from Bacteroides fragilis TAL3636. Antimicrob Agents Chemother. 1990 Aug;34(8):1590-2. [Article]
- Rasmussen BA, Gluzman Y, Tally FP: Escherichia coli chromosomal mutations that permit direct cloning of the Bacteroides fragilis metallo-beta-lactamase gene, ccrA. Mol Microbiol. 1991 May;5(5):1211-9. [Article]
- Thompson JS, Malamy MH: Sequencing the gene for an imipenem-cefoxitin-hydrolyzing enzyme (CfiA) from Bacteroides fragilis TAL2480 reveals strong similarity between CfiA and Bacillus cereus beta-lactamase II. J Bacteriol. 1990 May;172(5):2584-93. [Article]
- Concha NO, Rasmussen BA, Bush K, Herzberg O: Crystal structure of the wide-spectrum binuclear zinc beta-lactamase from Bacteroides fragilis. Structure. 1996 Jul 15;4(7):823-36. [Article]
- Concha NO, Rasmussen BA, Bush K, Herzberg O: Crystal structures of the cadmium- and mercury-substituted metallo-beta-lactamase from Bacteroides fragilis. Protein Sci. 1997 Dec;6(12):2671-6. [Article]
- Carfi A, Duee E, Paul-Soto R, Galleni M, Frere JM, Dideberg O: X-ray structure of the ZnII beta-lactamase from Bacteroides fragilis in an orthorhombic crystal form. Acta Crystallogr D Biol Crystallogr. 1998 Jan 1;54(Pt 1):45-57. [Article]
- Fitzgerald PM, Wu JK, Toney JH: Unanticipated inhibition of the metallo-beta-lactamase from Bacteroides fragilis by 4-morpholineethanesulfonic acid (MES): a crystallographic study at 1.85-A resolution. Biochemistry. 1998 May 12;37(19):6791-800. [Article]
- Li Z, Rasmussen BA, Herzberg O: Structural consequences of the active site substitution Cys181 ==> Ser in metallo-beta-lactamase from Bacteroides fragilis. Protein Sci. 1999 Jan;8(1):249-52. [Article]