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Q9F663

- BLKPC_KLEPN

UniProt

Q9F663 - BLKPC_KLEPN

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Protein

Carbepenem-hydrolyzing beta-lactamase KPC

Gene
bla, kpc, kpc1
Organism
Klebsiella pneumoniae
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei69 – 691Acyl-ester intermediate By similarity
Active sitei167 – 1671Proton acceptor By 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:
Carbepenem-hydrolyzing beta-lactamase KPC (EC:3.5.2.6)
Alternative name(s):
Carbepenem-hydrolyzing beta-lactamase KPC-1
Gene namesi
Name:bla
Synonyms:kpc, kpc1
Encoded oniPlasmid nonconjugative 50kb0 Publication
OrganismiKlebsiella pneumoniae
Taxonomic identifieri573 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeKlebsiella

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424 Reviewed predictionAdd
BLAST
Chaini25 – 293269Carbepenem-hydrolyzing beta-lactamase KPCPRO_0000349143Add
BLAST

Interactioni

Structurei

Secondary structure

1
293
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni28 – 303
Helixi31 – 4010
Beta strandi42 – 509
Turni51 – 533
Beta strandi56 – 605
Helixi68 – 703
Helixi71 – 8313
Turni87 – 915
Helixi98 – 1003
Helixi106 – 1105
Turni111 – 1144
Helixi118 – 12710
Helixi131 – 14111
Helixi143 – 15311
Helixi167 – 1693
Helixi182 – 19312
Beta strandi195 – 1984
Helixi200 – 21112
Turni217 – 2193
Helixi220 – 2234
Beta strandi228 – 2358
Helixi239 – 2413
Beta strandi243 – 2508
Beta strandi257 – 2648
Helixi274 – 28714

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliQ9F663.
SMRiQ9F663. Positions 30-293.

Miscellaneous databases

EvolutionaryTraceiQ9F663.

Family & Domainsi

Region

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

Sequence similaritiesi

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.

Q9F663-1 [UniParc]FASTAAdd to Basket

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MSLYRRLVLL SCLSWPLAGF SATALTNLVA EPFAKLEQDF GGSIGVYAMD    50
TGSGATVSYR AEERFPLCSS FKGFLAAAVL ARSQQQAGLL DTPIRYGKNA 100
LVPWSPISEK YLTTGMTVAE LSAAAVQYSD NAAANLLLKE LGGPAGLTAF 150
MRSIGDTTFR LDRWELELNS AIPGDARDTS SPRAVTESLQ KLTLGSALAA 200
PQRQQFVDWL KGNTTGNHRI RAAVPADWAV GDKTGTCGVY GTANDYAVVW 250
PTGRAPIVLA VYTRAPNKDD KHSEAVIAAA ARLALEGLGV NGQ 293
Length:293
Mass (Da):31,115
Last modified:September 2, 2008 - v2
Checksum:i13EB2FC28005EE5F
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF297554 Genomic DNA. Translation: AAG13410.1. Sequence problems.
RefSeqiYP_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.

Genome annotation databases

GeneIDi13914015.
13914300.
13914665.
13923837.
14458242.
15077276.
15564405.
15799359.
18261808.
18983479.
18983482.
18983485.
18985416.
6993854.
6993864.
6993875.
9389494.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF297554 Genomic DNA. Translation: AAG13410.1 . Sequence problems.
RefSeqi 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.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2OV5 X-ray 1.85 A/B/C 30-290 [» ]
3E2K X-ray 2.10 A/B 30-293 [» ]
3E2L X-ray 1.87 A/B 30-293 [» ]
3RXW X-ray 1.26 A 26-289 [» ]
3RXX X-ray 1.62 A 26-289 [» ]
ProteinModelPortali Q9F663.
SMRi Q9F663. Positions 30-293.
ModBasei Search...
MobiDBi Search...

Chemistry

BindingDBi Q9F663.
ChEMBLi CHEMBL6132.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 13914015.
13914300.
13914665.
13923837.
14458242.
15077276.
15564405.
15799359.
18261808.
18983479.
18983482.
18983485.
18985416.
6993854.
6993864.
6993875.
9389494.

Miscellaneous databases

EvolutionaryTracei Q9F663.

Family and domain databases

Gene3Di 3.40.710.10. 1 hit.
InterProi IPR012338. Beta-lactam/transpept-like.
IPR000871. Beta-lactam_class-A/D.
[Graphical view ]
PRINTSi PR00118. BLACTAMASEA.
SUPFAMi SSF56601. SSF56601. 1 hit.
ProtoNeti Search...

Publicationsi

  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.

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: July 9, 2014
This is version 56 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

External Data

Dasty 3

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