Beta-lactamase

Details

Name
Beta-lactamase
Synonyms
  • 3.5.2.6
  • blaC
  • Cephalosporinase
Gene Name
ampC
Organism
Citrobacter freundii
Amino acid sequence
>lcl|BSEQ0011014|Beta-lactamase
MMKKSICCALLLTASFSTFAAAKTEQQIADIVNRTITPLMQEQAIPGMAVAIIYEGKPYY
FTWGKADIANNHPVTQQTLFELGSVSKTFNGVLGGDRIARGEIKLSDPVTKYWPELTGKQ
WRGISLLHLATYTAGGLPLQIPGDVTDKAELLRFYQNWQPQWTPGAKRLYANSSIGLFGA
LAVKSSGMSYEEAMTRRVLQPLKLAHTWITVPQSEQKNYAWGYLEGKPVHVSPGQLDAEA
YGVKSSVIDMARWVQANMDASHVQEKTLQQGIELAQSRYWRIGDMYQGLGWEMLNWPLKA
DSIINGSDSKVALAALPAVEVNPPAPAVKASWVHKTGSTGGFGSYVAFVPEKNLGIVMLA
NKSYPNPARVEAAWRILEKLQ
Number of residues
381
Molecular Weight
41974.99
Theoretical pI
9.39
GO Classification
Functions
beta-lactamase activity
Processes
antibiotic catabolic process / response to antibiotic
Components
outer membrane-bounded periplasmic space
General Function
Beta-lactamase activity
Specific Function
This protein is a serine beta-lactamase with a substrate specificity for cephalosporins.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Periplasm
Gene sequence
>lcl|BSEQ0002865|1146 bp
ATGATGAAAAAATCGATATGCTGCGCGCTGCTGCTGACAGCCTCTTTCTCCACGTTTGCT
GCCGCAAAAACAGAACAACAAATTGCCGATATCGTTAACCGCACCATCACACCACTGATG
CAGGAGCAGGCTATTCCGGGTATGGCCGTGGCGATTATCTACGAGGGGAAACCTTATTAC
TTTACCTGGGGTAAAGCCGATATCGCCAATAACCACCCAGTCACGCAGCAAACGCTGTTT
GAGCTAGGGTCGGTCAGTAAGACGTTTAACGGCGTGTTGGGCGGCGACCGTATCGCCCGC
GGCGAAATTAAGCTCAGCGATCCGGTCACGAAATACTGGCCAGAACTGACAGGCAAACAG
TGGCGGGGTATCAGCCTGCTGCACTTAGCCACCTATACAGCGGGTGGCCTGCCGCTGCAG
ATCCCCGGTGACGTTACGGATAAAGCCGAATTACTGCGCTTTTATCAAAACTGGCAACCA
CAATGGACTCCGGGCGCTAAGCGTCTTTACGCTAACTCCAGCATTGGTCTGTTTGGTGCG
CTGGCGGTGAAATCTTCAGGTATGAGCTACGAAGAGGCAATGACCAGACGCGTCCTGCAA
CCATTAAAACTGGCGCATACCTGGATTACGGTTCCGCAAAGCGAACAAAAAAACTATGCC
TGGGGCTATCTCGAAGGGAAGCCTGTGCACGTTTCTCCGGGACAACTTGACGCCGAAGCC
TATGGCGTGAAATCCAGCGTTATCGATATGGCCCGCTGGGTTCAGGCCAACATGGACGCC
AGCCACGTTCAGGAGAAAACGCTCCAGCAGGGCATTGAGCTTGCGCAGTCTCGCTACTGG
CGTATTGGTGATATGTACCAGGGATTAGGCTGGGAGATGCTGAACTGGCCGCTGAAAGCT
GATTCGATCATCAACGGCAGCGACAGCAAAGTGGCATTGGCAGCGCTTCCCGCCGTTGAG
GTAAACCCGCCAGCACCTGCCGTGAAAGCCTCATGGGTGCATAAAACAGGATCCACAGGC
GGATTTGGCAGCTACGTTGCTTTCGTTCCAGAAAAAAACCTTGGCATCGTAATGTTGGCA
AACAAAAGCTACCCCAACCCGGCTCGCGTCGAGGCGGCCTGGCGCATTCTTGAAAAACTG
CAATAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP05193
UniProtKB Entry NameAMPC_CITFR
GenBank Protein ID40452
GenBank Gene IDX03866
General References
  1. Lindberg F, Normark S: Sequence of the Citrobacter freundii OS60 chromosomal ampC beta-lactamase gene. Eur J Biochem. 1986 May 2;156(3):441-5. [PubMed:3486121]
  2. Tsukamoto K, Tachibana K, Yamazaki N, Ishii Y, Ujiie K, Nishida N, Sawai T: Role of lysine-67 in the active site of class C beta-lactamase from Citrobacter freundii GN346. Eur J Biochem. 1990 Feb 22;188(1):15-22. [PubMed:1969344]
  3. Sawai T, Yamaguchi A, Tsukamoto K: Amino acid sequence, active-site residue, and effect of suicide inhibitors on cephalosporinase of Citrobacter freundii GN346. Rev Infect Dis. 1988 Jul-Aug;10(4):721-5. [PubMed:3263684]
  4. Yamaguchi A, Adachi H, Sawai T: Identification of the active site of Citrobacter freundii beta-lactamase using dansyl-penicillin. FEBS Lett. 1987 Jun 22;218(1):126-30. [PubMed:3496243]
  5. Oefner C, D'Arcy A, Daly JJ, Gubernator K, Charnas RL, Heinze I, Hubschwerlen C, Winkler FK: Refined crystal structure of beta-lactamase from Citrobacter freundii indicates a mechanism for beta-lactam hydrolysis. Nature. 1990 Jan 18;343(6255):284-8. [PubMed:2300174]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB00355AztreonamapprovedyespotentiatorDetails