Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Carbapenem-hydrolyzing beta-lactamase KPC

Gene

bla

Organism
Klebsiella oxytoca
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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

Catalytic activityi

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

Enzyme regulationi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei69 – 691Acyl-ester intermediateBy similarity
Active sitei167 – 1671Proton acceptorBy similarity

GO - Molecular functioni

  1. beta-lactamase activity Source: UniProtKB-EC

GO - Biological processi

  1. beta-lactam antibiotic catabolic process Source: InterPro
  2. response to antibiotic Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Antibiotic resistance

Names & Taxonomyi

Protein namesi
Recommended name:
Carbapenem-hydrolyzing beta-lactamase KPC (EC:3.5.2.6)
Alternative name(s):
Carbapenem-hydrolyzing beta-lactamase KPC-2
Gene namesi
Name:bla
Synonyms:kpc, kpc2
Encoded oniPlasmid conjugative 70kb0 Publication
OrganismiKlebsiella oxytoca
Taxonomic identifieri571 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeKlebsiella

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence AnalysisAdd
BLAST
Chaini25 – 293269Carbapenem-hydrolyzing beta-lactamase KPCPRO_0000349144Add
BLAST

Interactioni

Structurei

3D structure databases

ProteinModelPortaliQ848S6.
SMRiQ848S6. Positions 30-293.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni233 – 2353Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the class-A beta-lactamase family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.40.710.10. 1 hit.
InterProiIPR012338. Beta-lactam/transpept-like.
IPR000871. Beta-lactam_class-A/D.
[Graphical view]
PRINTSiPR00118. BLACTAMASEA.
SUPFAMiSSF56601. SSF56601. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q848S6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLYRRLVLL SCLSWPLAGF SATALTNLVA EPFAKLEQDF GGSIGVYAMD
60 70 80 90 100
TGSGATVSYR AEERFPLCSS FKGFLAAAVL ARSQQQAGLL DTPIRYGKNA
110 120 130 140 150
LVPWSPISEK YLTTGMTVAE LSAAAVQYSD NAAANLLLKE LGGPAGLTAF
160 170 180 190 200
MRSIGDTTFR LDRWELELNS AIPGDARDTS SPRAVTESLQ KLTLGSALAA
210 220 230 240 250
PQRQQFVDWL KGNTTGNHRI RAAVPADWAV GDKTGTCGVY GTANDYAVVW
260 270 280 290
PTGRAPIVLA VYTRAPNKDD KHSEAVIAAA ARLALEGLGV NGQ
Length:293
Mass (Da):31,115
Last modified:May 31, 2003 - v1
Checksum:i13EB2FC28005EE5F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY210886 Genomic DNA. Translation: AAO53443.1.
RefSeqiYP_009089096.1. NG_041239.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY210886 Genomic DNA. Translation: AAO53443.1.
RefSeqiYP_009089096.1. NG_041239.1.

3D structure databases

ProteinModelPortaliQ848S6.
SMRiQ848S6. Positions 30-293.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

BindingDBiQ848S6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di3.40.710.10. 1 hit.
InterProiIPR012338. Beta-lactam/transpept-like.
IPR000871. Beta-lactam_class-A/D.
[Graphical view]
PRINTSiPR00118. BLACTAMASEA.
SUPFAMiSSF56601. SSF56601. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Carbapenem-resistant strain of Klebsiella oxytoca harboring carbapenem-hydrolyzing beta-lactamase KPC-2."
    Yigit H., Queenan A.M., Rasheed J.K., Biddle J.W., Domenech-Sanchez A., Alberti S., Bush K., Tenover F.C.
    Antimicrob. Agents Chemother. 47:3881-3889(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBSTRATES, ENZYME REGULATION.
    Strain: 3127.

Entry informationi

Entry nameiBLKPC_KLEOX
AccessioniPrimary (citable) accession number: Q848S6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 1, 2008
Last sequence update: May 31, 2003
Last modified: January 6, 2015
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Plasmid

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.