Beta-lactamase 2

Details

Name
Beta-lactamase 2
Kind
protein
Synonyms
  • 3.5.2.6
  • Beta-lactamase II
  • Cephalosporinase
  • Penicillinase
Gene Name
blm
UniProtKB Entry
P04190Swiss-Prot
Organism
Bacillus cereus
NCBI Taxonomy ID
1396
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
Confers resistance to the different beta-lactams antibiotics (penicillin, cephalosporin and carbapenem) via the hydrolysis of the beta-lactam ring. Active on cephalosporin and penicillin.
Specific Function
beta-lactamase activity
Pfam Domain Function
Signal Regions
1-30
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
PDB ID(s)1BC2, 1BMC, 1BVT, 1DXK, 1MQO, 2BC2, 2BFK, 2BFL, 2BFZ, 2BG2, 2BG6, 2BG7, 2BG8, 2BGA, 2M5C, 2M5D, 2NXA, 2NYP, 2NZE, 2NZF, 2UYX, 3BC2, 3FCZ, 3I0V, 3I11, 3I13, 3I14, 3I15, 3KNR, 3KNS, 4C09, 4C1C, 4C1H, 4NQ4, 4NQ5, 4NQ6, 4NQ7, 4TYT
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]

Associated Data

Drug Relations
DrugDrug groupPharmacological action?TypeActionsDetails
3-sulfino-L-alanineexperimentalunknowntargetDetails
Chlorophyll AexperimentalunknowntargetDetails
Citric acidapproved, nutraceutical, vet_approvedunknowntargetDetails
Amoxicillinapproved, vet_approvedunknownenzymesubstrateDetails