Beta-lactamase

Details

Name
Beta-lactamase
Kind
protein
Synonyms
  • 3.5.2.6
  • Penicillinase
Gene Name
blaZ
UniProtKB Entry
P00807Swiss-Prot
Organism
Staphylococcus aureus
NCBI Taxonomy ID
1280
Amino acid sequence
>lcl|BSEQ0016061|Beta-lactamase
MKKLIFLIVIALVLSACNSNSSHAKELNDLEKKYNAHIGVYALDTKSGKEVKFNSDKRFA
YASTSKAINSAILLEQVPYNKLNKKVHINKDDIVAYSPILEKYVGKDITLKALIEASMTY
SDNTANNKIIKEIGGIKKVKQRLKELGDKVTNPVRYEIELNYYSPKSKKDTSTPAAFGKT
LNKLIANGKLSKENKKFLLDLMLNNKSGDTLIKDGVPKDYKVADKSGQAITYASRNDVAF
VYPKGQSEPIVLVIFTNKDNKSDKPNDKLISETAKSVMKEF
Number of residues
281
Molecular Weight
31348.98
Theoretical pI
10.15
GO Classification
Functions
beta-lactamase activity
Processes
beta-lactam antibiotic catabolic process / response to antibiotic
General Function
Not Available
Specific Function
beta-lactamase activity
Pfam Domain Function
Signal Regions
1-24
Transmembrane Regions
Not Available
Cellular Location
Cytoplasmic
Gene sequence
>lcl|BSEQ0016062|Beta-lactamase (blaZ)
TTGAAAAAGTTAATATTTTTAATTGTAATTGCTTTAGTTTTAAGTGCATGTAATTCAAAC
AGTTCACATGCCAAAGAGTTAAATGATTTAGAAAAAAAATATAATGCTCATATTGGTGTT
TATGCTTTAGATACTAAAAGTGGTAAGGAAGTAAAATTTAATTCAGATAAGAGATTTGCC
TATGCTTCAACTTCAAAAGCGATAAATAGTGCTATTTTGTTAGAACAAGTACCTTATAAT
AAGTTAAATAAAAAAGTACATATTAACAAAGATGATATAGTTGCTTATTCTCCTATTTTA
GAAAAATATGTAGGAAAAGATATCACTTTAAAAGCACTTATTGAGGCTTCAATGACATAT
AGTGATAATACAGCAAACAATAAAATTATAAAAGAAATCGGTGGAATCAAAAAAGTTAAA
CAACGTCTAAAAGAACTAGGAGATAAAGTAACAAATCCAGTTAGATATGAGATAGAATTA
AATTACTATTCACCAAAGAGCAAAAAAGATACTTCAACACCTGCTGCTTTCGGTAAGACT
TTAAATAAACTTATCGCAAATGGAAAATTAAGCAAAGAAAACAAAAAATTCTTACTTGAT
TTAATGTTAAATAATAAAAGCGGAGATACTTTAATTAAAGACGGTGTTCCAAAAGACTAT
AAGGTTGCTGATAAAAGTGGTCAAGCAATAACATATGCTTCTAGAAATGATGTTGCTTTT
GTTTATCCTAAGGGCCAATCTGAACCTATTGTTTTAGTCATTTTTACGAATAAAGACAAT
AAAAGTGATAAGCCAAATGATAAGTTGATAAGTGAAACCGCCAAGAGTGTAATGAAGGAA
TTTTAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP00807
UniProtKB Entry NameBLAC_STAAU
GenBank Protein ID581568
GenBank Gene IDX04121
PDB ID(s)1ALQ, 1BLC, 1BLH, 1BLP, 1DJA, 1DJB, 1DJC, 1GHI, 1GHM, 1GHP, 1KGE, 1KGF, 1KGG, 1OME, 1PIO, 3BLM
KEGG IDpg:13874750
NCBI Gene ID13874750
General References
  1. Chan PT: Nucleotide sequence of the Staphylococcus aureus PC1 beta-lactamase gene. Nucleic Acids Res. 1986 Jul 25;14(14):5940. [Article]
  2. Gillespie MT, Skurray RA: Nucleotide sequence of the blaZ gene of the Staphylococcus aureus beta-lactamase transposon Tn4002. Nucleic Acids Res. 1989 Nov 11;17(21):8854. [Article]
  3. Rowland SJ, Dyke KG: Tn552, a novel transposable element from Staphylococcus aureus. Mol Microbiol. 1990 Jun;4(6):961-75. [Article]
  4. Wang PZ, Novick RP: Nucleotide sequence and expression of the beta-lactamase gene from Staphylococcus aureus plasmid pI258 in Escherichia coli, Bacillus subtilis, and Staphylococcus aureus. J Bacteriol. 1987 Apr;169(4):1763-6. [Article]
  5. McLaughlin JR, Murray CL, Rabinowitz JC: Unique features in the ribosome binding site sequence of the gram-positive Staphylococcus aureus beta-lactamase gene. J Biol Chem. 1981 Nov 10;256(21):11283-91. [Article]
  6. Ambler RP: The amino acid sequence of Staphylococcus aureus penicillinase. Biochem J. 1975 Nov;151(2):197-218. [Article]
  7. Herzberg O, Moult J: Bacterial resistance to beta-lactam antibiotics: crystal structure of beta-lactamase from Staphylococcus aureus PC1 at 2.5 A resolution. Science. 1987 May 8;236(4802):694-701. [Article]
  8. Herzberg O: Refined crystal structure of beta-lactamase from Staphylococcus aureus PC1 at 2.0 A resolution. J Mol Biol. 1991 Feb 20;217(4):701-19. [Article]
  9. Banerjee S, Pieper U, Kapadia G, Pannell LK, Herzberg O: Role of the omega-loop in the activity, substrate specificity, and structure of class A beta-lactamase. Biochemistry. 1998 Mar 10;37(10):3286-96. [Article]
  10. Chen CC, Herzberg O: Relocation of the catalytic carboxylate group in class A beta-lactamase: the structure and function of the mutant enzyme Glu166-->Gln:Asn170-->Asp. Protein Eng. 1999 Jul;12(7):573-9. [Article]

Associated Data

Drug Relations
DrugDrug groupPharmacological action?TypeActionsDetails
Degraded CephaloridineexperimentalyestargetinhibitorDetails
[[N-(Benzyloxycarbonyl)Amino]Methyl]PhosphateexperimentalyestargetinhibitorDetails
SulbactamapprovedyestargetinhibitorDetails
CefroxadinewithdrawnnoenzymesubstrateDetails
4-iodo-acetamido phenylboronic acidexperimentalyestargetinhibitorDetails
2-(N-morpholino)ethanesulfonic acidexperimentalyestargetinhibitorDetails
M-Aminophenylboronic AcidexperimentalyestargetinhibitorDetails
N-2-Thiophen-2-Yl-Acetamide Boronic AcidexperimentalyestargetinhibitorDetails
Hydrolyzed CephalothinexperimentalyestargetinhibitorDetails
4-(Carboxyvin-2-Yl)Phenylboronic AcidexperimentalyestargetinhibitorDetails
4,4'-Biphenyldiboronic AcidexperimentalyestargetinhibitorDetails
Sucroseapproved, experimental, investigationalyestargetinhibitorDetails
3-Nitrophenylboronic AcidexperimentalyestargetinhibitorDetails
4-Carboxyphenylboronic AcidexperimentalyestargetinhibitorDetails
Acylated ceftazidimeexperimentalyestargetinhibitorDetails
Benzo[B]Thiophene-2-Boronic AcidexperimentalyestargetinhibitorDetails
4-[(METHYLSULFONYL)AMINO]BENZOIC ACIDexperimentalyestargetinhibitorDetails
2-phenyl-1H-imidazole-4-carboxylic acidexperimentalyestargetinhibitorDetails
Carbamic AcidexperimentalyestargetinhibitorDetails
AcetateexperimentalyestargetinhibitorDetails
Clavulanic acidapproved, vet_approvedyestargetinhibitorDetails
NacubactaminvestigationalyestargetinhibitorDetails
CyclohexanolexperimentalyestargetmodulatorDetails
Relebactamapproved, investigationalyestargetinhibitorDetails
Vaborbactamapproved, investigationalyestargetinhibitorDetails
EnmetazobactamapprovedyestargetinhibitorDetails
TazobactamapprovedyestargetinhibitorDetails