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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

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: 301.2)
    and 2 more
    NfeD1b_N; NfeD1b, N-terminal domain (PF25145; HMM-score: 15.5)
    Peptidase_S49; Peptidase family S49 (PF01343; HMM-score: 12.4)

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
  • DeepLocPro: Cytoplasmic
    • Cytoplasmic Score: 0.8898
    • Cytoplasmic Membrane Score: 0.0536
    • Cell wall & surface Score: 0.002
    • Extracellular Score: 0.0545
  • 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]

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. Jump up to: 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)

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

This data comes from external databases and cannot be edited.

Protein[edit | edit source]

Protein Data Bank: 3QWD

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: 301.2)
    and 2 more
    NfeD1b_N; NfeD1b, N-terminal domain (PF25145; HMM-score: 15.5)
    Peptidase_S49; Peptidase family S49 (PF01343; HMM-score: 12.4)

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
  • DeepLocPro: Cytoplasmic
    • Cytoplasmic Score: 0.8898
    • Cytoplasmic Membrane Score: 0.0536
    • Cell wall & surface Score: 0.002
    • Extracellular Score: 0.0545
  • 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)

  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)

Expression & Regulation[edit | edit source]

Operon[edit | edit source]

Regulation[edit | edit source]

  • regulator: CtsR (repression) regulon

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]

This data comes from external databases and cannot be edited.

This data comes from external databases and cannot be edited.

This data comes from external databases and cannot be edited.

This data comes from external databases and cannot be edited.

This data comes from external databases and cannot be edited.

This data comes from external databases and cannot be edited.

This data comes from external databases and cannot be edited.

Other Information[edit | edit source]

Literature[edit | edit source]

References[edit | edit source]

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)