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Summary[edit | edit source]

  • pan ID?: SAUPAN002695000
  • symbol?: clpP
  • synonym:
  • description?: ATP-dependent Clp protease proteolytic subunit

      descriptions from strain specific annotations:

    • ATP-dependent Clp protease proteolytic subunit
    • ATP-dependent Clp endopeptidase proteolytic subunit ClpP
    • ATP-dependent Clp protease, proteolytic subunit ClpP
    • ATP-dependent endopeptidase clp proteolytic subunit
    • putative ATP-dependent Clp protease proteolyticsubunit
  • strand?: +
  • coordinates?: 3187331..3187918
  • synteny block?: BlockID0019270
  • occurrence?: in 100% of 34 strains

clpP : clp proteolytic system core protease subunit ClpP [1]

• A crystal structure is available : 9IRM

The ClpP protease is responsible for ATP-dependent proteolysis of misfolded or targeted proteins. Partner chaperones power ClpP proteolysis with their ATPase activity and provide target protein specificity and unfolding activities but are themselves often dependent on allosteric activation by a third "activating protein" partner. ClpP monomers self-organize into two stacked rings of heptamers forming a compact proteolytic barrel.

Orthologs[edit | edit source]

    COL:
    SACOL0833 (clpP)
    N315:
    SA0723 (clpP)
    NCTC8325:
    Newman:
    NWMN_0736 (clpP)
    USA300_FPR3757:
    04-02981:
    SA2981_0746 (clpP)
    08BA02176:
    C248_0857 (clpP)
    11819-97:
    MS7_0819 (clpP)
    6850:
    RSAU_000744 (clpP)
    71193:
    ST398NM01_0846
    ECT-R 2:
    ECTR2_719 (clpP)
    ED133:
    SAOV_0807
    ED98:
    SAAV_0733 (clpP)
    HO 5096 0412:
    SAEMRSA15_06940 (clpP)
    JH1:
    SaurJH1_0809 (clpP)
    JH9:
    SaurJH9_0793 (clpP)
    JKD6008:
    SAA6008_00783 (clpP)
    JKD6159:
    SAA6159_00725 (clpP)
    JSNZ:
    JSNZ_000742 (clpP)
    LGA251:
    SARLGA251_07010 (clpP)
    M013:
    M013TW_0758
    MRSA252:
    SAR0823 (clpP)
    MSHR1132:
    SAMSHR1132_07130
    MSSA476:
    SAS0733 (clpP)
    Mu3:
    SAHV_0765 (clpP)
    Mu50:
    SAV0768 (clpP)
    MW2:
    MW0730 (clpP)
    RF122:
    SAB0722 (clpP)
    ST398:
    SAPIG0846 (clpP)
    T0131:
    SAT0131_00840
    TCH60:
    HMPREF0772_12412 (clpP)
    TW20:
    SATW20_08430 (clpP)
    USA300_TCH1516:
    USA300HOU_0797 (clpP)
    VC40:
    SAVC_03485 (clpP)

Genome Viewer[edit | edit source]

COL
N315
NCTC8325
Newman
USA300_FPR3757

Alignments[edit | edit source]

  • alignment of orthologues:
    CLUSTAL format alignment by MAFFT L-INS-i (v7.307)


    COL             MNLIPTVIETTNRGERAYDIYSRLLKDRIIMLGSQIDDNVANSIVSQLLFLQAQDSEKDI
    N315            MNLIPTVIETTNRGERAYDIYSRLLKDRIIMLGSQIDDNVANSIVSQLLFLQAQDSEKDI
    NCTC8325        MNLIPTVIETTNRGERAYDIYSRLLKDRIIMLGSQIDDNVANSIVSQLLFLQAQDSEKDI
    Newman          MNLIPTVIETTNRGERAYDIYSRLLKDRIIMLGSQIDDNVANSIVSQLLFLQAQDSEKDI
    USA300_FPR3757  MNLIPTVIETTNRGERAYDIYSRLLKDRIIMLGSQIDDNVANSIVSQLLFLQAQDSEKDI
                    ************************************************************

    COL             YLYINSPGGSVTAGFAIYDTIQHIKPDVQTICIGMAASMGSFLLAAGAKGKRFALPNAEV
    N315            YLYINSPGGSVTAGFAIYDTIQHIKPDVQTICIGMAASMGSFLLAAGAKGKRFALPNAEV
    NCTC8325        YLYINSPGGSVTAGFAIYDTIQHIKPDVQTICIGMAASMGSFLLAAGAKGKRFALPNAEV
    Newman          YLYINSPGGSVTAGFAIYDTIQHIKPDVQTICIGMAASMGSFLLAAGAKGKRFALPNAEV
    USA300_FPR3757  YLYINSPGGSVTAGFAIYDTIQHIKPDVQTICIGMAASMGSFLLAAGAKGKRFALPNAEV
                    ************************************************************

    COL             MIHQPLGGAQGQATEIEIAANHILKTREKLNRILSERTGQSIEKIQKDTDRDNFLTAEEA
    N315            MIHQPLGGAQGQATEIEIAANHILKTREKLNRILSERTGQSIEKIQKDTDRDNFLTAEEA
    NCTC8325        MIHQPLGGAQGQATEIEIAANHILKTREKLNRILSERTGQSIEKIQKDTDRDNFLTAEEA
    Newman          MIHQPLGGAQGQATEIEIAANHILKTREKLNRILSERTGQSIEKIQKDTDRDNFLTAEEA
    USA300_FPR3757  MIHQPLGGAQGQATEIEIAANHILKTREKLNRILSERTGQSIEKIQKDTDRDNFLTAEEA
                    ************************************************************

    COL             KEYGLIDEVMVPETK
    N315            KEYGLIDEVMVPETK
    NCTC8325        KEYGLIDEVMVPETK
    Newman          KEYGLIDEVMVPETK
    USA300_FPR3757  KEYGLIDEVMVPETK
                    ***************

  1. Astrid Illigmann, Marie-Theres Vielberg, Markus Lakemeyer, Felix Wolf, Taulant Dema, Patrik Stange, Wolfgang Kuttenlochner, Elisa Liebhart, Andreas Kulik, Nicole D Staudt, Imran Malik, Stephanie Grond, Stephan A Sieber, Leonard Kaysser, Michael Groll, Heike Brötz-Oesterhelt
    Structure of Staphylococcus aureus ClpP Bound to the Covalent Active-Site Inhibitor Cystargolide A.
    Angew Chem Int Ed Engl: 2024, 63(3);e202314028
    [PubMed:38029352] [WorldCat.org] [DOI] (I p)
    Lijuan Xu, Camilla Henriksen, Viktor Mebus, Romain Guérillot, Andreas Petersen, Nicolas Jacques, Jhih-Hang Jiang, Rico J E Derks, Elena Sánchez-López, Martin Giera, Kirsten Leeten, Timothy P Stinear, Cécile Oury, Benjamin P Howden, Anton Y Peleg, Dorte Frees
    A Clinically Selected Staphylococcus aureus clpP Mutant Survives Daptomycin Treatment by Reducing Binding of the Antibiotic and Adapting a Rod-Shaped Morphology.
    Antimicrob Agents Chemother: 2023, 67(6);e0032823
    [PubMed:37184389] [WorldCat.org] [DOI] (I p)
    Volker C Kirsch, Christian Fetzer, Stephan A Sieber
    Global Inventory of ClpP- and ClpX-Regulated Proteins in Staphylococcus aureus.
    J Proteome Res: 2021, 20(1);867-879
    [PubMed:33210542] [WorldCat.org] [DOI] (I p)