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Q9F663

- BLKPC_KLEPN

UniProt

Q9F663 - BLKPC_KLEPN

Protein

Carbepenem-hydrolyzing beta-lactamase KPC

Gene

bla

Organism
Klebsiella pneumoniae
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 57 (01 Oct 2014)
      Sequence version 2 (02 Sep 2008)
      Previous versions | rss
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    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

    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 – 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.
    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

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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: October 1, 2014
    This is version 57 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