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Q9F663

- BLKPC_KLEPN

UniProt

Q9F663 - BLKPC_KLEPN

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Protein

Carbepenem-hydrolyzing beta-lactamase KPC

Gene

bla

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 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:
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 – 2424Sequence AnalysisAdd
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 – 303Combined sources
Helixi31 – 4010Combined sources
Beta strandi42 – 509Combined sources
Turni51 – 533Combined sources
Beta strandi56 – 605Combined sources
Helixi68 – 703Combined sources
Helixi71 – 8313Combined sources
Turni87 – 915Combined sources
Helixi98 – 1003Combined sources
Helixi106 – 1105Combined sources
Turni111 – 1144Combined sources
Helixi118 – 12710Combined sources
Helixi131 – 14111Combined sources
Helixi143 – 15311Combined sources
Helixi167 – 1693Combined sources
Helixi182 – 19312Combined sources
Beta strandi195 – 1984Combined sources
Helixi200 – 21112Combined sources
Turni217 – 2193Combined sources
Helixi220 – 2234Combined sources
Beta strandi228 – 2358Combined sources
Helixi239 – 2413Combined sources
Beta strandi243 – 2508Combined sources
Beta strandi257 – 2648Combined sources
Helixi274 – 28714Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9F663.

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.

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.
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 58 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