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
Functions
beta-lactamase activity / zinc ion binding
Processes
antibiotic catabolic process / response to antibiotic
General Function
Zinc ion binding
Specific Function
Can hydrolyze carbapenem compounds.
Pfam Domain Function
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
ResourceLink
UniProtKB IDP25910
UniProtKB Entry NameBLAB_BACFG
GenBank Protein ID143932
GenBank Gene IDM63556
General References
  1. 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]
  2. 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]
  3. 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]
  4. 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]
  5. 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]
  6. 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]
  7. 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]
  8. 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]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB025937,8-Dihydroxy-1-Methoxy-3-Methyl-10-Oxo-4,10-Dihydro-1h,3h-Pyrano[4,3-B]Chromene-9-Carboxylic AcidexperimentalunknownDetails