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P22391 (BLO1_KLEOX) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Beta-lactamase OXY-1

EC=3.5.2.6
Alternative name(s):
Penicillinase
Gene names
Name:bla
OrganismKlebsiella oxytoca
Taxonomic identifier571 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeKlebsiella

Protein attributes

Sequence length291 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hydrolyzes broad-spectrum beta-lactam antibiotics. Active against cephalosporins.

Catalytic activity

A beta-lactam + H2O = a substituted beta-amino acid.

Miscellaneous

In strain KH66 OXY-1 is known as OXY-1a.

Sequence similarities

Belongs to the class-A beta-lactamase family.

Ontologies

Keywords
   Biological processAntibiotic resistance
   DomainSignal
   Molecular functionHydrolase
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processbeta-lactam antibiotic catabolic process

Inferred from electronic annotation. Source: InterPro

response to antibiotic

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionbeta-lactamase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424
Chain25 – 291267Beta-lactamase OXY-1
PRO_0000016997

Regions

Region237 – 2393Substrate binding By similarity

Sites

Active site731Acyl-ester intermediate By similarity

Natural variations

Natural variant2621L → P in strain: KH66.
Natural variant2781E → K in strain: KH66.

Secondary structure

.............................................. 291
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P22391 [UniParc].

Last modified August 1, 1991. Version 1.
Checksum: 9908F5AA97EDDC8A

FASTA29131,044
        10         20         30         40         50         60 
MLKSSWRKTA LMAAAAVPLL LASGSLWASA DAIQQKLADL EKRSGGRLGV ALINTADDSQ 

        70         80         90        100        110        120 
TLYRGDERFA MCSTGKVMAA AAVLKQSESN PEVVNKRLEI KKSDLVVWSP ITEKHLQSGM 

       130        140        150        160        170        180 
TLAELSAAAL QYSDNTAMNK MISYLGGPEK VTAFAQSIGD VTFRLDRTEP ALNSAIPGDK 

       190        200        210        220        230        240 
RDTTTPLAMA ESLRKLTLGN ALGEQQRAQL VTWLKGNTTG GQSIRAGLPA SWAVGDKTGA 

       250        260        270        280        290 
GDYGTTNDIA VIWPENHAPL VLVTYFTQPQ QDAKSRKEVL AAAAKIVTEG L 

« Hide

References

[1]"Chromosomal beta-lactamase of Klebsiella oxytoca, a new class A enzyme that hydrolyzes broad-spectrum beta-lactam antibiotics."
Arakawa Y., Ohta M., Kido N., Mori M., Ito H., Komatsu T., Fujii Y., Kato N.
Antimicrob. Agents Chemother. 33:63-70(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: E23004.
[2]"Klebsiella oxytoca: resistance to aztreonam by overproduction of the chromosomally encoded beta-lactamase."
Fournier B., Arlet G., Lagrange P.H., Philippon A.
FEMS Microbiol. Lett. 116:31-36(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: SL781 and SL7811.
[3]"Genetic characterization of resistance to extended-spectrum beta-lactams in Klebsiella oxytoca isolates recovered from patients with septicemia at hospitals in the Stockholm area."
Wu S.W., Dornbusch K., Kronvall G.
Antimicrob. Agents Chemother. 43:1294-1297(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: KH66.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M27459 Genomic DNA. Translation: AAA25084.1.
Z30177 Genomic DNA. Translation: CAA82916.1.
Z30178 Genomic DNA. Translation: CAA82917.1.
Y17715 Genomic DNA. Translation: CAB42615.1.
PIRS42075.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3BYDX-ray1.93A25-291[»]
ProteinModelPortalP22391.
SMRP22391. Positions 31-291.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.40.710.10. 1 hit.
InterProIPR001466. Beta-lactam-related.
IPR012338. Beta-lactam/transpept-like.
IPR000871. Beta-lactam_class-A/D.
IPR023650. Beta-lactam_class-A_AS.
[Graphical view]
PfamPF00144. Beta-lactamase. 1 hit.
[Graphical view]
PRINTSPR00118. BLACTAMASEA.
SUPFAMSSF56601. SSF56601. 1 hit.
PROSITEPS00146. BETA_LACTAMASE_A. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP22391.

Entry information

Entry nameBLO1_KLEOX
AccessionPrimary (citable) accession number: P22391
Secondary accession number(s): Q9S6S0
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: October 16, 2013
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references