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NCBI: 26-AUG-2013

Summary[edit | edit source]

  • organism: Staphylococcus aureus N315
  • locus tag: SA0723 [new locus tag: SA_RS04120 ]
  • 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: SA0723 [new locus tag: SA_RS04120 ]
  • symbol: clpP
  • product: ATP-dependent Clp protease proteolytic subunit
  • replicon: chromosome
  • strand: +
  • coordinates: 827630..828217
  • length: 588
  • essential: no 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: SA0723 [new locus tag: SA_RS04120 ]
  • 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: data available for COL, NCTC8325
  • protein localization: data available for COL
  • quantitative data / protein copy number per cell: data available for COL
  • interaction partners:
    SA2425(arcC)carbamate kinase  [1] (data from MRSA252)
    SA2040(rplP)50S ribosomal protein L16  [1] (data from MRSA252)
    SA1084(rplS)50S ribosomal protein L19  [1] (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; RegPrecise 

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. 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)

Relevant publications[edit | edit source]

Alexander Scherl, Patrice François, Manuela Bento, Jacques M Deshusses, Yvan Charbonnier, Véronique Converset, Antoine Huyghe, Nadia Walter, Christine Hoogland, Ron D Appel, Jean-Charles Sanchez, Catherine G Zimmermann-Ivol, Garry L Corthals, Denis F Hochstrasser, Jacques Schrenzel
Correlation of proteomic and transcriptomic profiles of Staphylococcus aureus during the post-exponential phase of growth.
J Microbiol Methods: 2005, 60(2);247-57
[PubMed:15590099] [WorldCat.org] [DOI] (P p)
Mitsutaka Shoji, Longzhu Cui, Risa Iizuka, Akira Komoto, Hui-min Neoh, Yukiko Watanabe, Tomomi Hishinuma, Keiichi Hiramatsu
walK and clpP mutations confer reduced vancomycin susceptibility in Staphylococcus aureus.
Antimicrob Agents Chemother: 2011, 55(8);3870-81
[PubMed:21628539] [WorldCat.org] [DOI] (I p)