Beta-lactamase 2

Details

Name
Beta-lactamase 2
Synonyms
  • 3.5.2.6
  • Beta-lactamase II
  • Cephalosporinase
  • Penicillinase
Gene Name
blm
Organism
Bacillus cereus
Amino acid sequence
>lcl|BSEQ0011000|Beta-lactamase 2
MKKNTLLKVGLCVGLLGTIQFVSTISSVQASQKVEKTVIKNETGTISISQLNKNVWVHTE
LGSFNGEAVPSNGLVLNTSKGLVLVDSSWDDKLTKELIEMVEKKFQKRVTDVIITHAHAD
RIGGIKTLKERGIKAHSTALTAELAKKNGYEEPLGDLQTVTNLKFGNMKVETFYPGKGHT
EDNIVVWLPQYNILVGGCLVKSTSAKDLGNVADAYVNEWSTSIENVLKRYRNINAVVPGH
GEVGDKGLLLHTLDLLK
Number of residues
257
Molecular Weight
28092.24
Theoretical pI
9.29
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|BSEQ0002830|774 bp
ATGAAAAAGAATACGTTGTTAAAAGTAGGATTATGTGTAGGTTTACTAGGAACAATTCAA
TTTGTTAGCACAATTTCTTCTGTACAAGCATCACAAAAGGTAGAGAAAACAGTAATAAAA
AATGAGACGGGAACCATTTCAATATCTCAGTTAAACAAGAATGTATGGGTTCATACGGAG
TTAGGTTCTTTTAATGGAGAAGCAGTTCCTTCGAACGGTCTAGTTCTTAATACTTCTAAA
GGGTTAGTACTTGTGGATTCTTCTTGGGATGACAAATTAACGAAGGAACTAATAGAAATG
GTAGAAAAGAAATTTCAGAAGCGCGTAACGGATGTCATTATTACACATGCGCACGCTGAT
CGAATTGGCGGAATAAAAACGTTGAAAGAAAGAGGCATTAAAGCGCATAGTACAGCATTA
ACTGCAGAACTAGCAAAGAAAAATGGATATGAAGAACCGCTTGGAGATTTACAAACCGTT
ACAAATTTGAAGTTTGGAAATATGAAAGTAGAAACATTTTATCCAGGGAAAGGGCATACA
GAAGATAATATTGTCGTATGGTTACCGCAATACAATATTTTAGTTGGAGGCTGTTTAGTG
AAATCTACGTCCGCGAAAGATTTAGGAAACGTTGCGGATGCTTATGTAAATGAATGGTCT
ACATCGATTGAGAATGTGCTGAAGCGATATAGAAATATAAATGCAGTAGTGCCTGGTCAT
GGGGAAGTAGGGGACAAAGGATTACTTTTACATACATTGGATTTATTAAAATAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP04190
UniProtKB Entry NameBLA2_BACCE
GenBank Protein ID142604
GenBank Gene IDM11189
General 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. [Article]
  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. [Article]
  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. [Article]
  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. [Article]
  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. [Article]
  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. [Article]
  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. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB021533-sulfino-L-alanineexperimentalunknownDetails
DB02133Chlorophyll AexperimentalunknownDetails
DB04272Citric acidapproved, nutraceutical, vet_approvedunknownDetails
DB01060Amoxicillinapproved, vet_approvedunknownsubstrateDetails