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Gene Review

clpC  -  endopeptidase

Staphylococcus aureus RF122

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Disease relevance of clpC


High impact information on clpC


Chemical compound and disease context of clpC


Biological context of clpC


Anatomical context of clpC


Associations of clpC with chemical compounds

  • In this study, clinical thymidine-dependent SCVs displayed altered expression of citB, clpC, and arcA genes, reduced acetate catabolization, and enhanced survival [21].
  • In contrast with the fragment produced by elastase, which was inactive, the fragments resulting from V8 proteinase and proline-specific endopeptidase treatment retained activity [22].
  • Two other proteases (mouse submaxillaris protease and lysyl endopeptidase) with specificities similar to trypsin generated a distribution of GTF-S peptides that was also greatly enriched in the glucan-binding peptide [23].
  • Lysostaphin is an endopeptidase that cleaves the pentaglycine cross-bridges of the staphylococcal cell wall rapidly lysing the bacteria [24].
  • In conclusion, our results demonstrate that sprE encodes a highly specific serine-type glutamyl endopeptidase, the maturation of which is dependent on the presence of gelatinase [16].

Other interactions of clpC


Analytical, diagnostic and therapeutic context of clpC


  1. Staphylococcus aureus ClpC is required for stress resistance, aconitase activity, growth recovery, and death. Chatterjee, I., Becker, P., Grundmeier, M., Bischoff, M., Somerville, G.A., Peters, G., Sinha, B., Harraghy, N., Proctor, R.A., Herrmann, M. J. Bacteriol. (2005) [Pubmed]
  2. Amino acid sequences of the two subunits of a phospholipase A2 inhibitor from the blood plasma of Trimeresurus flavoviridis. Sequence homologies with pulmonary surfactant apoprotein and animal lectins. Inoue, S., Kogaki, H., Ikeda, K., Samejima, Y., Omori-Satoh, T. J. Biol. Chem. (1991) [Pubmed]
  3. Purification and amino acid sequence of a bitter gourd inhibitor against an acidic amino acid-specific endopeptidase of Streptomyces griseus. Ogata, F., Miyata, T., Fujii, N., Yoshida, N., Noda, K., Makisumi, S., Ito, A. J. Biol. Chem. (1991) [Pubmed]
  4. Cytoplasmic orientation and two-domain structure of the multidrug transporter, P-glycoprotein, demonstrated with sequence-specific antibodies. Yoshimura, A., Kuwazuru, Y., Sumizawa, T., Ichikawa, M., Ikeda, S., Uda, T., Akiyama, S. J. Biol. Chem. (1989) [Pubmed]
  5. Characterization of a unique glycosylated anchor endopeptidase that cleaves the LPXTG sequence motif of cell surface proteins of Gram-positive bacteria. Lee, S.G., Pancholi, V., Fischetti, V.A. J. Biol. Chem. (2002) [Pubmed]
  6. Anchoring of surface proteins to the cell wall of Staphylococcus aureus. III. Lipid II is an in vivo peptidoglycan substrate for sortase-catalyzed surface protein anchoring. Perry, A.M., Ton-That, H., Mazmanian, S.K., Schneewind, O. J. Biol. Chem. (2002) [Pubmed]
  7. Porphyromonas gingivalis DPP-7 represents a novel type of dipeptidylpeptidase. Banbula, A., Yen, J., Oleksy, A., Mak, P., Bugno, M., Travis, J., Potempa, J. J. Biol. Chem. (2001) [Pubmed]
  8. Characterization of Staphylococcus aureus cell wall glycan strands, evidence for a new beta-N-acetylglucosaminidase activity. Boneca, I.G., Huang, Z.H., Gage, D.A., Tomasz, A. J. Biol. Chem. (2000) [Pubmed]
  9. The primary structure of coagulation factor IX/factor X-binding protein isolated from the venom of Trimeresurus flavoviridis. Homology with asialoglycoprotein receptors, proteoglycan core protein, tetranectin, and lymphocyte Fc epsilon receptor for immunoglobulin E. Atoda, H., Hyuga, M., Morita, T. J. Biol. Chem. (1991) [Pubmed]
  10. Clp ATPases are required for stress tolerance, intracellular replication and biofilm formation in Staphylococcus aureus. Frees, D., Chastanet, A., Qazi, S., Sørensen, K., Hill, P., Msadek, T., Ingmer, H. Mol. Microbiol. (2004) [Pubmed]
  11. Complete amino acid sequence of plastocyanin from a green alga, Enteromorpha prolifera. Simpson, R.J., Moritz, R.L., Nice, E.C., Grego, B., Yoshizaki, F., Sugimura, Y., Freeman, H.C., Murata, M. Eur. J. Biochem. (1986) [Pubmed]
  12. Secretory expression of a glutamic-acid-specific endopeptidase (SPase) from Staphylococcus aureus ATCC12600 in Bacillus subtilis. Kakudo, S., Yoshikawa, K., Tamaki, M., Nakamura, E., Teraoka, H. Appl. Microbiol. Biotechnol. (1992) [Pubmed]
  13. The complete amino acid sequence of prolactin from the sea turtle (Chelonia mydas). Yasuda, A., Kawauchi, H., Papkoff, H. Gen. Comp. Endocrinol. (1990) [Pubmed]
  14. Identification of the Staphylococcus aureus etd pathogenicity island which encodes a novel exfoliative toxin, ETD, and EDIN-B. Yamaguchi, T., Nishifuji, K., Sasaki, M., Fudaba, Y., Aepfelbacher, M., Takata, T., Ohara, M., Komatsuzawa, H., Amagai, M., Sugai, M. Infect. Immun. (2002) [Pubmed]
  15. The lysostaphin endopeptidase resistance gene (epr) specifies modification of peptidoglycan cross bridges in Staphylococcus simulans and Staphylococcus aureus. DeHart, H.P., Heath, H.E., Heath, L.S., LeBlanc, P.A., Sloan, G.L. Appl. Environ. Microbiol. (1995) [Pubmed]
  16. Molecular diversity of a putative virulence factor: purification and characterization of isoforms of an extracellular serine glutamyl endopeptidase of Enterococcus faecalis with different enzymatic activities. Kawalec, M., Potempa, J., Moon, J.L., Travis, J., Murray, B.E. J. Bacteriol. (2005) [Pubmed]
  17. Bacillus intermedius glutamyl endopeptidase. Molecular cloning and nucleotide sequence of the structural gene. Rebrikov, D.V., Akimkina, T.V., Shevelev, A.B., Demidyuk, I.V., Bushueva, A.M., Kostrov, S.V., Chestukhina, G.G., Stepanov, V.M. J. Protein Chem. (1999) [Pubmed]
  18. Amino acid sequence of starfish oocyte depactin. Takagi, T., Konishi, K., Mabuchi, I. J. Biol. Chem. (1988) [Pubmed]
  19. The amino acid sequence and interaction with the nucleosome core DNA of transition protein 4 from boar late spermatid nuclei. Akama, K., Ichimura, H., Sato, H., Kojima, S., Miura, K., Hayashi, H., Komatsu, Y., Nakano, M. Eur. J. Biochem. (1995) [Pubmed]
  20. Amino acid sequence of porcine cardiac muscle troponin C. Kobayashi, T., Takagi, T., Konishi, K., Morimoto, S., Ohtsuki, I. J. Biochem. (1989) [Pubmed]
  21. Enhanced Post-Stationary-Phase Survival of a Clinical Thymidine-Dependent Small-Colony Variant of Staphylococcus aureus Results from Lack of a Functional Tricarboxylic Acid Cycle. Chatterjee, I., Herrmann, M., Proctor, R.A., Peters, G., Kahl, B.C. J. Bacteriol. (2007) [Pubmed]
  22. Proteolysis and deglycosylation of human C1 inhibitor. Effect on functional properties. Reboul, A., Prandini, M.H., Colomb, M.G. Biochem. J. (1987) [Pubmed]
  23. Isolation of a glucan-binding domain of glucosyltransferase (1,6-alpha-glucan synthase) from Streptococcus sobrinus. Mooser, G., Wong, C. Infect. Immun. (1988) [Pubmed]
  24. Comparison of four methods for determining lysostaphin susceptibility of various strains of Staphylococcus aureus. Kusuma, C.M., Kokai-Kun, J.F. Antimicrob. Agents Chemother. (2005) [Pubmed]
  25. Latent LytM at 1.3A resolution. Odintsov, S.G., Sabala, I., Marcyjaniak, M., Bochtler, M. J. Mol. Biol. (2004) [Pubmed]
  26. Amino acid sequence of sweet-taste-suppressing peptide (gurmarin) from the leaves of Gymnema sylvestre. Kamei, K., Takano, R., Miyasaka, A., Imoto, T., Hara, S. J. Biochem. (1992) [Pubmed]
  27. Programming of enzyme specificity by substrate mimetics: investigations on the Glu-specific V8 protease reveals a novel general principle of biocatalysis. Wehofsky, N., Bordusa, F. FEBS Lett. (1999) [Pubmed]
  28. Characterization and molecular cloning of a glutamyl endopeptidase from Staphylococcus epidermidis. Ohara-Nemoto, Y., Ikeda, Y., Kobayashi, M., Sasaki, M., Tajika, S., Kimura, S. Microb. Pathog. (2002) [Pubmed]
  29. The primary structure of a membrane-associated phospholipase A2 from human spleen. Kanda, A., Ono, T., Yoshida, N., Tojo, H., Okamoto, M. Biochem. Biophys. Res. Commun. (1989) [Pubmed]
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