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Q9F663 (BLKPC_KLEPN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 56. 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:
Carbepenem-hydrolyzing beta-lactamase KPC

EC=3.5.2.6
Alternative name(s):
Carbepenem-hydrolyzing beta-lactamase KPC-1
Gene names
Name:bla
Synonyms:kpc, kpc1
Encoded onPlasmid nonconjugative 50kb
OrganismKlebsiella pneumoniae
Taxonomic identifier573 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeKlebsiella

Protein attributes

Sequence length293 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hydrolyzes carbapenems, penicillins, cephalosporins and monobactams with varying efficiency.

Catalytic activity

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

Enzyme regulation

Not inhibited by EDTA, inhibited by clavulanic acid and tazobactam. Ref.1

Miscellaneous

Initially two different KPC beta-lactamases were identified from two different Klebsiella (KPC-1 and KPC-2); they were later shown to be identical.

Sequence similarities

Belongs to the class-A beta-lactamase family.

Ontologies

Keywords
   Biological processAntibiotic resistance
   DomainSignal
   Molecular functionHydrolase
   Technical term3D-structure
Plasmid
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 Potential
Chain25 – 293269Carbepenem-hydrolyzing beta-lactamase KPC
PRO_0000349143

Regions

Region233 – 2353Substrate binding By similarity

Sites

Active site691Acyl-ester intermediate By similarity
Active site1671Proton acceptor By similarity

Secondary structure

.............................................. 293
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9F663 [UniParc].

Last modified September 2, 2008. Version 2.
Checksum: 13EB2FC28005EE5F

FASTA29331,115
        10         20         30         40         50         60 
MSLYRRLVLL SCLSWPLAGF SATALTNLVA EPFAKLEQDF GGSIGVYAMD TGSGATVSYR 

        70         80         90        100        110        120 
AEERFPLCSS FKGFLAAAVL ARSQQQAGLL DTPIRYGKNA LVPWSPISEK YLTTGMTVAE 

       130        140        150        160        170        180 
LSAAAVQYSD NAAANLLLKE LGGPAGLTAF MRSIGDTTFR LDRWELELNS AIPGDARDTS 

       190        200        210        220        230        240 
SPRAVTESLQ KLTLGSALAA PQRQQFVDWL KGNTTGNHRI RAAVPADWAV GDKTGTCGVY 

       250        260        270        280        290 
GTANDYAVVW PTGRAPIVLA VYTRAPNKDD KHSEAVIAAA ARLALEGLGV NGQ 

« Hide

References

[1]"Novel carbapenem-hydrolyzing beta-lactamase, KPC-1, from a carbapenem-resistant strain of Klebsiella pneumoniae."
Yigit H., Queenan A.M., Anderson G.J., Domenech-Sanchez A., Biddle J.W., Steward C.D., Alberti S., Bush K., Tenover F.C.
Antimicrob. Agents Chemother. 45:1151-1161(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBSTRATES, ENZYME REGULATION.
Strain: 1534.
[2]"Novel carbapenem-hydrolyzing beta-lactamase, KPC-1, from a carbapenem-resistant strain of Klebsiella pneumoniae."
Yigit H., Queenan A.M., Anderson G.J., Domenech-Sanchez A., Biddle J.W., Steward C.D., Alberti S., Bush K., Tenover F.C.
Antimicrob. Agents Chemother. 52:809-809(2008)
Cited for: SEQUENCE REVISION TO 174.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF297554 Genomic DNA. Translation: AAG13410.1. Sequence problems.
RefSeqYP_002286834.1. NC_011382.1.
YP_002286844.1. NC_011383.1.
YP_002286855.1. NC_011383.1.
YP_003754012.1. NC_014312.1.
YP_006958635.1. NC_019152.1.
YP_006959213.1. NC_019161.1.
YP_006959400.1. NC_019165.1.
YP_006971133.1. NC_019384.1.
YP_007366474.1. NC_020132.1.
YP_007688776.1. NC_020893.1.
YP_008003445.1. NC_021238.1.
YP_008076059.1. NC_021356.1.
YP_008998912.1. NC_023331.1.
YP_009022511.1. NC_023903.1.
YP_009022618.1. NC_023904.1.
YP_009022725.1. NC_023905.1.
YP_009022831.1. NC_023906.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2OV5X-ray1.85A/B/C30-290[»]
3E2KX-ray2.10A/B30-293[»]
3E2LX-ray1.87A/B30-293[»]
3RXWX-ray1.26A26-289[»]
3RXXX-ray1.62A26-289[»]
ProteinModelPortalQ9F663.
SMRQ9F663. Positions 30-293.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBQ9F663.
ChEMBLCHEMBL6132.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID13914015.
13914300.
13914665.
13923837.
14458242.
15077276.
15564405.
15799359.
18261808.
18983479.
18983482.
18983485.
18985416.
6993854.
6993864.
6993875.
9389494.

Family and domain databases

Gene3D3.40.710.10. 1 hit.
InterProIPR012338. Beta-lactam/transpept-like.
IPR000871. Beta-lactam_class-A/D.
[Graphical view]
PRINTSPR00118. BLACTAMASEA.
SUPFAMSSF56601. SSF56601. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ9F663.

Entry information

Entry nameBLKPC_KLEPN
AccessionPrimary (citable) accession number: Q9F663
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: September 2, 2008
Last modified: July 9, 2014
This is version 56 of the entry and version 2 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