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
- 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|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
Resource Link UniProtKB ID P04190 UniProtKB Entry Name BLA2_BACCE GenBank Protein ID 142604 GenBank Gene ID M11189 - General References
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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 ID Name Drug group Pharmacological action? Actions Details DB02153 3-sulfino-L-alanine experimental unknown Details DB02133 Chlorophyll A experimental unknown Details DB04272 Citric acid approved, nutraceutical, vet_approved unknown Details DB01060 Amoxicillin approved, vet_approved unknown substrate Details