Beta-lactamase

NameBeta-lactamase
Synonyms
  • 3.5.2.6
  • blaCTX-M-9
  • blaCTX-M-9b
Gene NameblaCTX-M-9a
OrganismEscherichia coli
Amino acid sequence
>lcl|BSEQ0022432|Beta-lactamase
MVTKRVQRMMFAAAACIPLLLGSAPLYAQTSAVQQKLAALEKSSGGRLGVALIDTADNTQ
VLYRGDERFPMCSTSKVMAAAAVLKQSETQKQLLNQPVEIKPADLVNYNPIAEKHVNGTM
TLAELSAAALQYSDNTAMNKLIAQLGGPGGVTAFARAIGDETFRLDRTEPTLNTAIPGDP
RDTTTPRAMAQTLRQLTLGHALGETQRAQLVTWLKGNTTGAASIRAGLPTSWTAGDKTGS
GDYGTTNDIAVIWPQGRAPLVLVTYFTQPQQNAESRRDVLASAARIIAEGL
Number of residuesNone
Molecular Weight30951.03
Theoretical pI9.38
GO Classification
Functions
  • beta-lactamase activity
Processes
  • response to antibiotic
  • beta-lactam antibiotic catabolic process
Components
General FunctionBeta-lactamase activity
Specific FunctionNone
Transmembrane Regions
GenBank Protein ID
UniProtKB IDQ9L5C8
UniProtKB Entry Name
Cellular LocationCytoplasmic
Gene sequence
>lcl|BSEQ0005330|876 bp
ATGGTGACAAAGAGAGTGCAACGGATGATGTTCGCGGCGGCGGCGTGCATTCCGCTGCTG
CTGGGCAGCGCGCCGCTTTATGCGCAGACGAGTGCGGTGCAGCAAAAGCTGGCGGCGCTG
GAGAAAAGCAGCGGAGGGCGGCTGGGCGTCGCGCTCATCGATACCGCAGATAATACGCAG
GTGCTTTATCGCGGTGATGAACGCTTTCCAATGTGCAGTACCAGTAAAGTTATGGCGGCC
GCGGCGGTGCTTAAGCAGAGTGAAACGCAAAAGCAGCTGCTTAATCAGCCTGTCGAGATC
AAGCCTGCCGATCTGGTTAACTACAATCCGATTGCCGAAAAACACGTCAACGGCACAATG
ACGCTGGCAGAGCTGAGCGCGGCCGCGTTGCAGTACAGCGACAATACCGCCATGAACAAA
TTGATTGCCCAGCTCGGTGGCCCGGGAGGCGTGACGGCTTTTGCCCGCGCGATCGGCGAT
GAGACGTTTCGTCTGGATCGCACTGAACCTACGCTGAATACCGCCATTCCCGGCGACCCG
AGAGACACCACCACGCCGCGGGCGATGGCACAGACGTTGCGTCAGCTTACGCTGGGTCAT
GCGCTGGGCGAAACCCAGCGGGCGCAGTTGGTGACGTGGCTCAAAGGCAATACGACCGGC
GCAGCCAGCATTCGGGCCGGCTTACCGACGTCGTGGACTGCAGGTGATAAGACCGGCAGC
GGCGACTACGGCACCACCAATGATATTGCGGTGATCTGGCCGCAGGGTCGTGCGCCGCTG
GTTCTGGTGACCTATTTTACCCAGCCGCAACAGAACGCAGAGAGCCGCCGCGATGTGCTG
GCTTCAGCGGCGAGAATCATCGCCGAAGGGCTGTAA
GenBank Gene ID
GeneCard IDNone
GenAtlas ID
HGNC ID
Chromosome LocationNone
LocusNone
References
  1. Chen Y, Shoichet B, Bonnet R: Structure, function, and inhibition along the reaction coordinate of CTX-M beta-lactamases. J Am Chem Soc. 2005 Apr 20;127(15):5423-34. [15826180 ]
  2. Chen Y, Delmas J, Sirot J, Shoichet B, Bonnet R: Atomic resolution structures of CTX-M beta-lactamases: extended spectrum activities from increased mobility and decreased stability. J Mol Biol. 2005 Apr 29;348(2):349-62. [15811373 ]
  3. Chen Y, Bonnet R, Shoichet BK: The acylation mechanism of CTX-M beta-lactamase at 0.88 a resolution. J Am Chem Soc. 2007 May 2;129(17):5378-80. Epub 2007 Apr 5. [17408273 ]
  4. Chen Y, Shoichet BK: Molecular docking and ligand specificity in fragment-based inhibitor discovery. Nat Chem Biol. 2009 May;5(5):358-64. doi: 10.1038/nchembio.155. Epub 2009 Mar 22. [19305397 ]
  5. Delmas J, Leyssene D, Dubois D, Birck C, Vazeille E, Robin F, Bonnet R: Structural insights into substrate recognition and product expulsion in CTX-M enzymes. J Mol Biol. 2010 Jul 2;400(1):108-20. doi: 10.1016/j.jmb.2010.04.062. Epub 2010 May 7. [20452359 ]
  6. Nichols DA, Jaishankar P, Larson W, Smith E, Liu G, Beyrouthy R, Bonnet R, Renslo AR, Chen Y: Structure-based design of potent and ligand-efficient inhibitors of CTX-M class A beta-lactamase. J Med Chem. 2012 Mar 8;55(5):2163-72. doi: 10.1021/jm2014138. Epub 2012 Feb 14. [22296601 ]
  7. Tondi D, Venturelli A, Bonnet R, Pozzi C, Shoichet BK, Costi MP: Targeting class A and C serine beta-lactamases with a broad-spectrum boronic acid derivative. J Med Chem. 2014 Jun 26;57(12):5449-58. doi: 10.1021/jm5006572. Epub 2014 Jun 16. [24882105 ]

From www.t3db.ca