Beta-lactamase

Details

Name
Beta-lactamase
Synonyms
  • 3.5.2.6
  • blaP
  • Penicillinase
Gene Name
penP
Organism
Bacillus licheniformis
Amino acid sequence
>lcl|BSEQ0011047|Beta-lactamase
MKLWFSTLKLKKAAAVLLFSCVALAGCANNQTNASQPAEKNEKTEMKDDFAKLEEQFDAK
LGIFALDTGTNRTVAYRPDERFAFASTIKALTVGVLLQQKSIEDLNQRITYTRDDLVNYN
PITEKHVDTGMTLKELADASLRYSDNAAQNLILKQIGGPESLKKELRKIGDEVTNPERFE
PELNEVNPGETQDTSTARALVTSLRAFALEDKLPSEKRELLIDWMKRNTTGDALIRAGVP
DGWEVADKTGAASYGTRNDIAIIWPPKGDPVVLAVLSSRDKKDAKYDDKLIAEATKVVMK
ALNMNGK
Number of residues
307
Molecular Weight
33995.36
Theoretical pI
5.61
GO Classification
Functions
beta-lactamase activity
Processes
beta-lactam antibiotic catabolic process / response to antibiotic
Components
plasma membrane
General Function
Beta-lactamase activity
Specific Function
Not Available
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cell membrane
Gene sequence
>lcl|BSEQ0002941|924 bp
ATGAAATTATGGTTCAGTACTTTAAAACTGAAAAAGGCTGCAGCAGTGTTGCTTTTCTCT
TGCGTCGCGCTTGCAGGATGCGCTAACAATCAAACGAATGCCTCGCAACCTGCCGAGAAG
AATGAAAAGACGGAGATGAAAGATGATTTTGCAAAACTTGAGGAACAATTTGATGCAAAA
CTCGGGATCTTTGCATTGGATACAGGTACAAACCGGACGGTAGCGTATCGGCCGGATGAG
CGTTTTGCTTTTGCTTCGACGATTAAGGCTTTAACTGTAGGCGTGCTTTTGCAACAGAAA
TCAATAGAAGATCTGAACCAGAGAATAACATATACACGTGATGATCTTGTAAACTACAAC
CCGATTACGGAAAAGCACGTTGATACGGGAATGACGCTCAAAGAGCTTGCGGATGCTTCG
CTTCGATATAGTGACAATGCGGCACAGAATCTCATTCTTAAACAAATTGGCGGACCTGAA
AGTTTGAAAAAGGAACTGAGGAAGATTGGTGATGAGGTTACAAATCCCGAACGATTCGAA
CCAGAGTTAAATGAAGTGAATCCGGGTGAAACTCAGGATACCAGTACAGCAAGAGCACTT
GTCACAAGCCTTCGAGCCTTTGCTCTTGAAGATAAACTTCCAAGTGAAAAACGCGAGCTT
TTAATCGATTGGATGAAACGAAATACCACTGGAGACGCCTTAATCCGTGCCGGTGTGCCG
GACGGTTGGGAAGTGGCTGATAAAACTGGAGCGGCATCATATGGAACCCGGAATGACATT
GCCATCATTTGGCCGCCAAAAGGAGATCCTGTCGTTCTTGCAGTATTATCCAGCAGGGAT
AAAAAGGACGCCAAGTATGATGATAAACTTATTGCAGAGGCAACAAAGGTGGTAATGAAA
GCCTTAAACATGAACGGCAAATAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP00808
UniProtKB Entry NameBLAC_BACLI
GenBank Protein ID39575
GenBank Gene IDV00093
General References
  1. Neugebauer K, Sprengel R, Schaller H: Penicillinase from Bacillus licheniformis: nucleotide sequence of the gene and implications for the biosynthesis of a secretory protein in a Gram-positive bacterium. Nucleic Acids Res. 1981 Jun 11;9(11):2577-88. [Article]
  2. Kroyer J, Chang S: The promoter-proximal region of the Bacillus licheniformis penicillinase gene: Nucleotide sequence and predicted leader peptide sequence. Gene. 1981 Dec;15(4):343-7. [Article]
  3. Meadway RJ: The amino acid sequence of penicillinase from Bacillus licheniformis. Biochem J. 1969 Nov;115(3):12P-13P. [Article]
  4. Wittman V, Wong HC: Regulation of the penicillinase genes of Bacillus licheniformis: interaction of the pen repressor with its operators. J Bacteriol. 1988 Jul;170(7):3206-12. [Article]
  5. Izui K, Nielsen JB, Caulfield MP, Lampen JO: Large exopenicillinase, initial extracellular form detected in cultures of Bacillus licheniformis. Biochemistry. 1980 Apr 29;19(9):1882-6. [Article]
  6. Moews PC, Knox JR, Dideberg O, Charlier P, Frere JM: Beta-lactamase of Bacillus licheniformis 749/C at 2 A resolution. Proteins. 1990;7(2):156-71. [Article]
  7. Knox JR, Moews PC: Beta-lactamase of Bacillus licheniformis 749/C. Refinement at 2 A resolution and analysis of hydration. J Mol Biol. 1991 Jul 20;220(2):435-55. [Article]
  8. Fonze E, Vanhove M, Dive G, Sauvage E, Frere JM, Charlier P: Crystal structures of the Bacillus licheniformis BS3 class A beta-lactamase and of the acyl-enzyme adduct formed with cefoxitin. Biochemistry. 2002 Feb 12;41(6):1877-85. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB04261Carbamic AcidexperimentalunknownDetails
DB04272Citric acidapproved, nutraceutical, vet_approvedyesweak inhibitorDetails
DB01331CefoxitinapprovedunknownsubstrateDetails