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Protein

Carbapenem-hydrolyzing beta-lactamase KPC

Gene

bla

Organism
Klebsiella pneumoniae
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Hydrolyzes carbapenems, penicillins, cephalosporins and monobactams 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)DescriptionActionsGraphical viewLength
Active sitei69Acyl-ester intermediateBy similarity1
Active sitei167Proton acceptorBy similarity1

GO - Molecular functioni

GO - Biological processi

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-1
Gene namesi
Name:bla
Synonyms:kpc, kpc1
Encoded oniPlasmid nonconjugative 50kb0 Publication
OrganismiKlebsiella pneumoniae
Taxonomic identifieri573 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeKlebsiella

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL6132.
DrugBankiDB09060. Avibactam.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 24Sequence analysisAdd BLAST24
ChainiPRO_000034914325 – 293Carbapenem-hydrolyzing beta-lactamase KPCAdd BLAST269

Interactioni

Chemistry databases

BindingDBiQ9F663.

Structurei

Secondary structure

1293
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni28 – 30Combined sources3
Helixi31 – 40Combined sources10
Beta strandi42 – 50Combined sources9
Turni51 – 53Combined sources3
Beta strandi56 – 60Combined sources5
Helixi68 – 70Combined sources3
Helixi71 – 83Combined sources13
Turni87 – 91Combined sources5
Helixi98 – 100Combined sources3
Helixi106 – 110Combined sources5
Turni111 – 114Combined sources4
Helixi118 – 127Combined sources10
Helixi131 – 141Combined sources11
Helixi143 – 153Combined sources11
Helixi167 – 169Combined sources3
Helixi182 – 193Combined sources12
Beta strandi195 – 198Combined sources4
Helixi200 – 211Combined sources12
Turni217 – 219Combined sources3
Helixi220 – 223Combined sources4
Beta strandi228 – 235Combined sources8
Helixi239 – 241Combined sources3
Beta strandi243 – 250Combined sources8
Beta strandi257 – 264Combined sources8
Helixi274 – 287Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4ZBEX-ray1.80A26-289[»]
5EECX-ray1.87A/B25-293[»]
ProteinModelPortaliQ9F663.
SMRiQ9F663.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9F663.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni233 – 235Substrate bindingBy similarity3

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

KOiK18768.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

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

Q9F663-1 [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:September 2, 2008 - v2
Checksum:i13EB2FC28005EE5F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF297554 Genomic DNA. Translation: AAG13410.1. Sequence problems.
RefSeqiWP_004199234.1. NZ_MDVO01000032.1.
YP_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.
YP_009070099.1. NC_025166.1.
YP_009071849.1. NC_025187.1.

Genome annotation databases

GeneIDi13914015.
13914300.
13914665.
13923837.
14458347.
15077276.
15564405.
15799359.
18261808.
18983479.
18983482.
18983485.
18985416.
20493883.
20494301.
23339714.
6993854.
6993864.
6993875.
9389494.
KEGGiag:AAG13410.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF297554 Genomic DNA. Translation: AAG13410.1. Sequence problems.
RefSeqiWP_004199234.1. NZ_MDVO01000032.1.
YP_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.
YP_009070099.1. NC_025166.1.
YP_009071849.1. NC_025187.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4ZBEX-ray1.80A26-289[»]
5EECX-ray1.87A/B25-293[»]
ProteinModelPortaliQ9F663.
SMRiQ9F663.
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

BindingDBiQ9F663.
ChEMBLiCHEMBL6132.
DrugBankiDB09060. Avibactam.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi13914015.
13914300.
13914665.
13923837.
14458347.
15077276.
15564405.
15799359.
18261808.
18983479.
18983482.
18983485.
18985416.
20493883.
20494301.
23339714.
6993854.
6993864.
6993875.
9389494.
KEGGiag:AAG13410.

Phylogenomic databases

KOiK18768.

Miscellaneous databases

EvolutionaryTraceiQ9F663.
PROiQ9F663.

Family and domain databases

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

Entry informationi

Entry nameiBLKPC_KLEPN
AccessioniPrimary (citable) accession number: Q9F663
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: September 2, 2008
Last modified: November 30, 2016
This is version 75 of the entry and version 2 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 Klebsiella (KPC-1 and KPC-2); they were later shown to be identical.

Keywords - Technical termi

3D-structure, Plasmid

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.