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NCBI: 03-AUG-2016

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus NCTC8325
  • locus tag: SAOUHSC_00790
  • pan locus tag?: SAUPAN002695000
  • symbol: clpP
  • pan gene symbol?: clpP
  • synonym:
  • product: ATP-dependent Clp protease proteolytic subunit

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SAOUHSC_00790
  • symbol: clpP
  • product: ATP-dependent Clp protease proteolytic subunit
  • replicon: chromosome
  • strand: +
  • coordinates: 772413..773000
  • length: 588
  • essential: yes [1] DEG other strains

⊟Accession numbers[edit | edit source]

⊟Phenotype[edit | edit source]

Share your knowledge and add information here. [edit]

⊟DNA sequence[edit | edit source]

  • 1
    61
    121
    181
    241
    301
    361
    421
    481
    541
    ATGAATTTAATTCCTACAGTTATTGAAACAACAAACCGCGGTGAACGTGCATATGATATA
    TACTCACGTTTATTAAAAGACCGTATTATTATGTTAGGTTCACAAATTGATGACAACGTA
    GCAAATTCAATCGTATCACAGTTATTATTCTTACAAGCGCAAGACTCAGAGAAAGATATT
    TATTTATACATTAATTCACCAGGTGGAAGTGTAACAGCTGGTTTTGCGATTTATGATACA
    ATTCAACACATTAAACCTGATGTTCAAACAATTTGTATCGGTATGGCTGCATCAATGGGA
    TCATTCTTATTAGCAGCTGGTGCAAAAGGTAAACGTTTCGCGTTACCAAATGCAGAAGTA
    ATGATTCACCAACCATTAGGTGGTGCTCAAGGACAAGCAACTGAAATCGAAATTGCTGCA
    AATCACATTTTAAAAACACGTGAAAAATTAAACCGCATTTTATCAGAGCGTACTGGTCAA
    AGTATTGAAAAAATACAAAAAGACACAGATCGTGATAACTTCTTAACTGCAGAAGAAGCT
    AAAGAATATGGCTTAATTGATGAAGTGATGGTACCTGAAACAAAATAA
    60
    120
    180
    240
    300
    360
    420
    480
    540
    588

⊟Protein[edit | edit source]

Protein Data Bank: 3QWD
Protein Data Bank: 3V5E
Protein Data Bank: 3V5I
Protein Data Bank: 4MXI
Protein Data Bank: 5C90
Protein Data Bank: 5VZ2
Protein Data Bank: 5W18

⊟General[edit | edit source]

  • locus tag: SAOUHSC_00790
  • symbol: ClpP
  • description: ATP-dependent Clp protease proteolytic subunit
  • length: 195
  • theoretical pI: 4.89682
  • theoretical MW: 21513.4
  • GRAVY: -0.188205

⊟Function[edit | edit source]

  • reaction:
    EC 3.4.21.92?  ExPASy
    Endopeptidase Clp Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. Alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec; and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs)
  • TIGRFAM:
    Genetic information processing Protein fate Degradation of proteins, peptides, and glycopeptides ATP-dependent Clp endopeptidase, proteolytic subunit ClpP (TIGR00493; EC 3.4.21.92; HMM-score: 346.7)
    and 3 more
    Genetic information processing Protein fate Degradation of proteins, peptides, and glycopeptides signal peptide peptidase SppA, 36K type (TIGR00706; EC 3.4.-.-; HMM-score: 28.4)
    Genetic information processing Protein fate Degradation of proteins, peptides, and glycopeptides signal peptide peptidase SppA, 67K type (TIGR00705; EC 3.4.-.-; HMM-score: 21.7)
    Metabolism Energy metabolism Other 4-hydroxy-2-oxovalerate aldolase (TIGR03217; EC 4.1.3.39; HMM-score: 12.9)
  • TheSEED  :
    • ATP-dependent Clp protease proteolytic subunit ClpP (EC 3.4.21.92)
    Protein Metabolism Protein degradation Proteasome bacterial  ATP-dependent Clp protease proteolytic subunit (EC 3.4.21.92)
    and 2 more
    Protein Metabolism Protein degradation Proteolysis in bacteria, ATP-dependent  ATP-dependent Clp protease proteolytic subunit (EC 3.4.21.92)
    Regulation and Cell signaling Regulation and Cell signaling - no subcategory cAMP signaling in bacteria  ATP-dependent Clp protease proteolytic subunit (EC 3.4.21.92)
  • PFAM:
    ClpP_crotonase (CL0127) CLP_protease; Clp protease (PF00574; HMM-score: 298.6)
    and 1 more
    Peptidase_S49; Peptidase family S49 (PF01343; HMM-score: 12.3)

⊟Structure, modifications & cofactors[edit | edit source]

  • domains:
  • modifications:
  • cofactors:
  • effectors:

⊟Localization[edit | edit source]

  • PSORTb: Cytoplasmic
    • Cytoplasmic Score: 9.67
    • Cytoplasmic Membrane Score: 0.01
    • Cellwall Score: 0.15
    • Extracellular Score: 0.17
    • Internal Helices: 0
  • LocateP: Intracellular
    • Prediction by SwissProt Classification: Cytoplasmic
    • Pathway Prediction: No pathway
    • Intracellular possibility: 1
    • Signal peptide possibility: -1
    • N-terminally Anchored Score: -1
    • Predicted Cleavage Site: No CleavageSite
  • SignalP: no predicted signal peptide
    • SP(Sec/SPI): 0.003841
    • TAT(Tat/SPI): 0.000397
    • LIPO(Sec/SPII): 0.000526
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MNLIPTVIETTNRGERAYDIYSRLLKDRIIMLGSQIDDNVANSIVSQLLFLQAQDSEKDIYLYINSPGGSVTAGFAIYDTIQHIKPDVQTICIGMAASMGSFLLAAGAKGKRFALPNAEVMIHQPLGGAQGQATEIEIAANHILKTREKLNRILSERTGQSIEKIQKDTDRDNFLTAEEAKEYGLIDEVMVPETK

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas [2] [3]
  • protein localization: data available for COL
  • quantitative data / protein copy number per cell: data available for COL
  • interaction partners:
    SAOUHSC_02505(rplP)50S ribosomal protein L16  [4] (data from MRSA252)
    SAOUHSC_01211(rplS)50S ribosomal protein L19  [4] (data from MRSA252)
    SAOUHSC_02965carbamate kinase  [4] (data from MRSA252)

⊟Expression & Regulation[edit | edit source]

⊟Operon[edit | edit source]

⊟Regulation[edit | edit source]

  • regulator: CtsR* (repression) regulon
    CtsR*(TF)important in Heat shock response; compare RegPrecise for N315  [5]

⊟Transcription pattern[edit | edit source]

⊟Protein synthesis (provided by Aureolib)[edit | edit source]

⊟Protein stability[edit | edit source]

  • half-life: no data available

⊟Biological Material[edit | edit source]

⊟Mutants[edit | edit source]

⊟Expression vector[edit | edit source]

⊟lacZ fusion[edit | edit source]

⊟GFP fusion[edit | edit source]

⊟two-hybrid system[edit | edit source]

⊟FLAG-tag construct[edit | edit source]

⊟Antibody[edit | edit source]

⊟Other Information[edit | edit source]

You are kindly invited to share additional interesting facts.

⊟Literature[edit | edit source]

⊟References[edit | edit source]

  1. ↑ Roy R Chaudhuri, Andrew G Allen, Paul J Owen, Gil Shalom, Karl Stone, Marcus Harrison, Timothy A Burgis, Michael Lockyer, Jorge Garcia-Lara, Simon J Foster, Stephen J Pleasance, Sarah E Peters, Duncan J Maskell, Ian G Charles
    Comprehensive identification of essential Staphylococcus aureus genes using Transposon-Mediated Differential Hybridisation (TMDH).
    BMC Genomics: 2009, 10;291
    [PubMed:19570206] [WorldCat.org] [DOI] (I e)
  2. ↑ Maren Depke, Stephan Michalik, Alexander Rabe, Kristin Surmann, Lars Brinkmann, Nico Jehmlich, Jörg Bernhardt, Michael Hecker, Bernd Wollscheid, Zhi Sun, Robert L Moritz, Uwe Völker, Frank Schmidt
    A peptide resource for the analysis of Staphylococcus aureus in host-pathogen interaction studies.
    Proteomics: 2015, 15(21);3648-61
    [PubMed:26224020] [WorldCat.org] [DOI] (I p)
  3. ↑ Stephan Michalik, Maren Depke, Annette Murr, Manuela Gesell Salazar, Ulrike Kusebauch, Zhi Sun, Tanja C Meyer, Kristin Surmann, Henrike Pförtner, Petra Hildebrandt, Stefan Weiss, Laura Marcela Palma Medina, Melanie Gutjahr, Elke Hammer, Dörte Becher, Thomas Pribyl, Sven Hammerschmidt, Eric W Deutsch, Samuel L Bader, Michael Hecker, Robert L Moritz, Ulrike Mäder, Uwe Völker, Frank Schmidt
    A global Staphylococcus aureus proteome resource applied to the in vivo characterization of host-pathogen interactions.
    Sci Rep: 2017, 7(1);9718
    [PubMed:28887440] [WorldCat.org] [DOI] (I e)
  4. ↑ 4.0 4.1 4.2 Artem Cherkasov, Michael Hsing, Roya Zoraghi, Leonard J Foster, Raymond H See, Nikolay Stoynov, Jihong Jiang, Sukhbir Kaur, Tian Lian, Linda Jackson, Huansheng Gong, Rick Swayze, Emily Amandoron, Farhad Hormozdiari, Phuong Dao, Cenk Sahinalp, Osvaldo Santos-Filho, Peter Axerio-Cilies, Kendall Byler, William R McMaster, Robert C Brunham, B Brett Finlay, Neil E Reiner
    Mapping the protein interaction network in methicillin-resistant Staphylococcus aureus.
    J Proteome Res: 2011, 10(3);1139-50
    [PubMed:21166474] [WorldCat.org] [DOI] (I p)
  5. ↑ 5.0 5.1 5.2 5.3 Ulrike Mäder, Pierre Nicolas, Maren Depke, Jan Pané-Farré, Michel Debarbouille, Magdalena M van der Kooi-Pol, Cyprien Guérin, Sandra Dérozier, Aurelia Hiron, Hanne Jarmer, Aurélie Leduc, Stephan Michalik, Ewoud Reilman, Marc Schaffer, Frank Schmidt, Philippe Bessières, Philippe Noirot, Michael Hecker, Tarek Msadek, Uwe Völker, Jan Maarten van Dijl
    Staphylococcus aureus Transcriptome Architecture: From Laboratory to Infection-Mimicking Conditions.
    PLoS Genet: 2016, 12(4);e1005962
    [PubMed:27035918] [WorldCat.org] [DOI] (I e)

⊟Relevant publications[edit | edit source]

Antje Michel, Franziska Agerer, Christof R Hauck, Mathias Herrmann, Joachim Ullrich, Jörg Hacker, Knut Ohlsen
Global regulatory impact of ClpP protease of Staphylococcus aureus on regulons involved in virulence, oxidative stress response, autolysis, and DNA repair.
J Bacteriol: 2006, 188(16);5783-96
[PubMed:16885446] [WorldCat.org] [DOI] (P p)Sebastian R Geiger, Thomas Böttcher, Stephan A Sieber, Patrick Cramer
A conformational switch underlies ClpP protease function.
Angew Chem Int Ed Engl: 2011, 50(25);5749-52
[PubMed:21544912] [WorldCat.org] [DOI] (I p)Malte Gersch, Anja List, Michael Groll, Stephan A Sieber
Insights into structural network responsible for oligomerization and activity of bacterial virulence regulator caseinolytic protease P (ClpP) protein.
J Biol Chem: 2012, 287(12);9484-94
[PubMed:22291011] [WorldCat.org] [DOI] (I p)Jingyuan Feng, Stephan Michalik, Anders N Varming, Julie H Andersen, Dirk Albrecht, Lotte Jelsbak, Stefanie Krieger, Knut Ohlsen, Michael Hecker, Ulf Gerth, Hanne Ingmer, Dorte Frees
Trapping and proteomic identification of cellular substrates of the ClpP protease in Staphylococcus aureus.
J Proteome Res: 2013, 12(2);547-58
[PubMed:23253041] [WorldCat.org] [DOI] (I p)

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