Beta-lactamase 2

NameBeta-lactamase 2
Synonyms
  • 3.5.2.6
  • Beta-lactamase II
  • Cephalosporinase
  • Penicillinase
Gene Nameblm
OrganismBacillus cereus
Amino acid sequence
>lcl|BSEQ0011000|Beta-lactamase 2
MKKNTLLKVGLCVGLLGTIQFVSTISSVQASQKVEKTVIKNETGTISISQLNKNVWVHTE
LGSFNGEAVPSNGLVLNTSKGLVLVDSSWDDKLTKELIEMVEKKFQKRVTDVIITHAHAD
RIGGIKTLKERGIKAHSTALTAELAKKNGYEEPLGDLQTVTNLKFGNMKVETFYPGKGHT
EDNIVVWLPQYNILVGGCLVKSTSAKDLGNVADAYVNEWSTSIENVLKRYRNINAVVPGH
GEVGDKGLLLHTLDLLK
Number of residues257
Molecular Weight28092.24
Theoretical pI9.29
GO Classification
Functions
  • zinc ion binding
  • beta-lactamase activity
Processes
  • response to antibiotic
  • antibiotic catabolic process
General FunctionZinc ion binding
Specific FunctionCan hydrolyze carbapenem compounds.
Pfam Domain Function
Transmembrane RegionsNot Available
GenBank Protein ID142604
UniProtKB IDP04190
UniProtKB Entry NameBLA2_BACCE
Cellular LocationCytoplasmic
Gene sequence
>lcl|BSEQ0002830|774 bp
ATGAAAAAGAATACGTTGTTAAAAGTAGGATTATGTGTAGGTTTACTAGGAACAATTCAA
TTTGTTAGCACAATTTCTTCTGTACAAGCATCACAAAAGGTAGAGAAAACAGTAATAAAA
AATGAGACGGGAACCATTTCAATATCTCAGTTAAACAAGAATGTATGGGTTCATACGGAG
TTAGGTTCTTTTAATGGAGAAGCAGTTCCTTCGAACGGTCTAGTTCTTAATACTTCTAAA
GGGTTAGTACTTGTGGATTCTTCTTGGGATGACAAATTAACGAAGGAACTAATAGAAATG
GTAGAAAAGAAATTTCAGAAGCGCGTAACGGATGTCATTATTACACATGCGCACGCTGAT
CGAATTGGCGGAATAAAAACGTTGAAAGAAAGAGGCATTAAAGCGCATAGTACAGCATTA
ACTGCAGAACTAGCAAAGAAAAATGGATATGAAGAACCGCTTGGAGATTTACAAACCGTT
ACAAATTTGAAGTTTGGAAATATGAAAGTAGAAACATTTTATCCAGGGAAAGGGCATACA
GAAGATAATATTGTCGTATGGTTACCGCAATACAATATTTTAGTTGGAGGCTGTTTAGTG
AAATCTACGTCCGCGAAAGATTTAGGAAACGTTGCGGATGCTTATGTAAATGAATGGTCT
ACATCGATTGAGAATGTGCTGAAGCGATATAGAAATATAAATGCAGTAGTGCCTGGTCAT
GGGGAAGTAGGGGACAAAGGATTACTTTTACATACATTGGATTTATTAAAATAA
GenBank Gene IDM11189
GeneCard IDNot Available
GenAtlas IDNot Available
HGNC IDNot Available
Chromosome LocationNot Available
LocusNot Available
References
  1. Hussain M, Carlino A, Madonna MJ, Lampen JO: Cloning and sequencing of the metallothioprotein beta-lactamase II gene of Bacillus cereus 569/H in Escherichia coli. J Bacteriol. 1985 Oct;164(1):223-9. 3930467
  2. Ambler RP, Daniel M, Fleming J, Hermoso JM, Pang C, Waley SG: The amino acid sequence of the zinc-requiring beta-lactamase II from the bacterium Bacillus cereus 569. FEBS Lett. 1985 Sep 23;189(2):207-11. 3930290
  3. Sutton BJ, Artymiuk PJ, Cordero-Borboa AE, Little C, Phillips DC, Waley SG: An X-ray-crystallographic study of beta-lactamase II from Bacillus cereus at 0.35 nm resolution. Biochem J. 1987 Nov 15;248(1):181-8. 3124808
  4. Carfi A, Pares S, Duee E, Galleni M, Duez C, Frere JM, Dideberg O: The 3-D structure of a zinc metallo-beta-lactamase from Bacillus cereus reveals a new type of protein fold. EMBO J. 1995 Oct 16;14(20):4914-21. 7588620
  5. Carfi A, Duee E, Galleni M, Frere JM, Dideberg O: 1.85 A resolution structure of the zinc (II) beta-lactamase from Bacillus cereus. Acta Crystallogr D Biol Crystallogr. 1998 May 1;54(Pt 3):313-23. 9761898
  6. Fabiane SM, Sohi MK, Wan T, Payne DJ, Bateson JH, Mitchell T, Sutton BJ: Crystal structure of the zinc-dependent beta-lactamase from Bacillus cereus at 1.9 A resolution: binuclear active site with features of a mononuclear enzyme. Biochemistry. 1998 Sep 8;37(36):12404-11. 9730812
  7. Chantalat L, Duee E, Galleni M, Frere JM, Dideberg O: Structural effects of the active site mutation cysteine to serine in Bacillus cereus zinc-beta-lactamase. Protein Sci. 2000 Jul;9(7):1402-6. 10933508