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NCBI: 10-JUN-2013

Summary[edit source | edit]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL0833 [new locus tag: SACOL_RS04290 ]
  • pan locus tag?: SAUPAN002695000
  • symbol: clpP
  • pan gene symbol?: clpP
  • synonym:
  • product: ATP-dependent Clp protease proteolytic subunit

Genome View[edit source | edit]

Gene[edit source | edit]

General[edit source | edit]

  • type: CDS
  • locus tag: SACOL0833 [new locus tag: SACOL_RS04290 ]
  • symbol: clpP
  • product: ATP-dependent Clp protease proteolytic subunit
  • replicon: chromosome
  • strand: +
  • coordinates: 859951..860538
  • length: 588
  • essential: unknown other strains

Accession numbers[edit source | edit]

Phenotype[edit source | edit]

Share your knowledge and add information here. [edit]

DNA sequence[edit source | edit]

  • 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 source | edit]

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 source | edit]

  • locus tag: SACOL0833 [new locus tag: SACOL_RS04290 ]
  • symbol: ClpP
  • description: ATP-dependent Clp protease proteolytic subunit
  • length: 195
  • theoretical pI: 4.89682
  • theoretical MW: 21513.4
  • GRAVY: -0.188205

Function[edit source | edit]

  • reaction:
    EC 3.4.21.92?  ExPASy
    Endopeptidase ClpHydrolysis 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 processingProtein fateDegradation of proteins, peptides, and glycopeptidesATP-dependent Clp endopeptidase, proteolytic subunit ClpP (TIGR00493; EC 3.4.21.92; HMM-score: 346.7)
    and 3 more
    Genetic information processingProtein fateDegradation of proteins, peptides, and glycopeptidessignal peptide peptidase SppA, 36K type (TIGR00706; EC 3.4.-.-; HMM-score: 28.4)
    Genetic information processingProtein fateDegradation of proteins, peptides, and glycopeptidessignal peptide peptidase SppA, 67K type (TIGR00705; EC 3.4.-.-; HMM-score: 21.7)
    MetabolismEnergy metabolismOther4-hydroxy-2-oxovalerate aldolase (TIGR03217; EC 4.1.3.39; HMM-score: 12.9)
  • TheSEED:  
    Protein MetabolismProtein degradationProteasome bacterial ATP-dependent Clp protease proteolytic subunit (EC 3.4.21.92) 
    and 2 more
    Protein degradationProteolysis in bacteria, ATP-dependent ATP-dependent Clp protease proteolytic subunit (EC 3.4.21.92) 
    Regulation and Cell signalingRegulation and Cell signaling - no subcategorycAMP 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 & interactions[edit source | edit]

  • domains:
  • modifications:
  • cofactors:
  • effectors:
  • protein partners:
    SACOL2654(arcC2)carbamate kinase  [1] (data from MRSA252)
    SACOL2232(rplP)50S ribosomal protein L16  [1] (data from MRSA252)
    SACOL1257(rplS)50S ribosomal protein L19  [1] (data from MRSA252)

Localization[edit source | edit]

  • 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
    • Ymax: 0.148
    • Ymax_pos: 59
    • Cmax: 0.205
    • Cmax_pos: 59
    • Smax: 0.172
    • Smax_pos: 53
    • Smean: 0.098
    • D: 0.129
  • predicted transmembrane helices (TMHMM): 0

Accession numbers[edit source | edit]

Protein sequence[edit source | edit]

  • MNLIPTVIETTNRGERAYDIYSRLLKDRIIMLGSQIDDNVANSIVSQLLFLQAQDSEKDIYLYINSPGGSVTAGFAIYDTIQHIKPDVQTICIGMAASMGSFLLAAGAKGKRFALPNAEVMIHQPLGGAQGQATEIEIAANHILKTREKLNRILSERTGQSIEKIQKDTDRDNFLTAEEAKEYGLIDEVMVPETK

Experimental data[edit source | edit]

  • experimentally validated: PeptideAtlas
    experimental localization: Cytoplasmic [2] [3] [4] [5]
    quantitative data / protein copy number per cell: 4814 [6]

Expression & Regulation[edit source | edit]

Operon[edit source | edit]

  • clpP no polycistronic organisation predicted

Regulation[edit source | edit]

  • sigma factor:
  • regulator:

Transcription pattern[edit source | edit]

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

Protein stability[edit source | edit]

  • half-life: 23.33 h [7]

Biological Material[edit source | edit]

Mutants[edit source | edit]

Expression vector[edit source | edit]

lacZ fusion[edit source | edit]

GFP fusion[edit source | edit]

two-hybrid system[edit source | edit]

FLAG-tag construct[edit source | edit]

Antibody[edit source | edit]

Other Information[edit source | edit]

You are kindly invited to share additional interesting facts.

Literature[edit source | edit]

References[edit source | edit]

  1. 1.0 1.1 1.2 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)
  2. Dörte Becher, Kristina Hempel, Susanne Sievers, Daniela Zühlke, Jan Pané-Farré, Andreas Otto, Stephan Fuchs, Dirk Albrecht, Jörg Bernhardt, Susanne Engelmann, Uwe Völker, Jan Maarten van Dijl, Michael Hecker
    A proteomic view of an important human pathogen--towards the quantification of the entire Staphylococcus aureus proteome.
    PLoS ONE: 2009, 4(12);e8176
    [PubMed:19997597] [WorldCat.org] [DOI] (I e)
  3. Kristina Hempel, Jan Pané-Farré, Andreas Otto, Susanne Sievers, Michael Hecker, Dörte Becher
    Quantitative cell surface proteome profiling for SigB-dependent protein expression in the human pathogen Staphylococcus aureus via biotinylation approach.
    J. Proteome Res.: 2010, 9(3);1579-90
    [PubMed:20108986] [WorldCat.org] [DOI] (I p)
  4. Kristina Hempel, Florian-Alexander Herbst, Martin Moche, Michael Hecker, Dörte Becher
    Quantitative proteomic view on secreted, cell surface-associated, and cytoplasmic proteins of the methicillin-resistant human pathogen Staphylococcus aureus under iron-limited conditions.
    J. Proteome Res.: 2011, 10(4);1657-66
    [PubMed:21323324] [WorldCat.org] [DOI] (I p)
  5. Andreas Otto, Jan Maarten van Dijl, Michael Hecker, Dörte Becher
    The Staphylococcus aureus proteome.
    Int. J. Med. Microbiol.: 2014, 304(2);110-20
    [PubMed:24439828] [WorldCat.org] [DOI] (I p)
  6. Daniela Zühlke, Kirsten Dörries, Jörg Bernhardt, Sandra Maaß, Jan Muntel, Volkmar Liebscher, Jan Pané-Farré, Katharina Riedel, Michael Lalk, Uwe Völker, Susanne Engelmann, Dörte Becher, Stephan Fuchs, Michael Hecker
    Costs of life - Dynamics of the protein inventory of Staphylococcus aureus during anaerobiosis.
    Sci Rep: 2016, 6;28172
    [PubMed:27344979] [WorldCat.org] [DOI] (I e)
  7. Stephan Michalik, Jörg Bernhardt, Andreas Otto, Martin Moche, Dörte Becher, Hanna Meyer, Michael Lalk, Claudia Schurmann, Rabea Schlüter, Holger Kock, Ulf Gerth, Michael Hecker
    Life and death of proteins: a case study of glucose-starved Staphylococcus aureus.
    Mol. Cell Proteomics: 2012, 11(9);558-70
    [PubMed:22556279] [WorldCat.org] [DOI] (I p)

Relevant publications[edit source | edit]