Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.4.21.92 extracted from

  • Wahl, A.; Servais, F.; Drucbert, A.S.; Foulon, C.; Fontaine, L.; Hols, P.
    Control of natural transformation in salivarius Streptococci through specific degradation of sigmaX by the MecA-ClpCP protease complex (2014), J. Bacteriol., 196, 2807-2816.
    View publication on PubMedView publication on EuropePMC

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
central competence regulator sigmax + H2O Streptococcus thermophilus adaptor protein MecA ultimately targets sigmaX for its degradation by the ClpCP protease in an ATP-dependent manner ?
-
?
central competence regulator sigmax + H2O Streptococcus thermophilus ATCC BAA-250 adaptor protein MecA ultimately targets sigmaX for its degradation by the ClpCP protease in an ATP-dependent manner ?
-
?

Organism

Organism UniProt Comment Textmining
Streptococcus thermophilus Q5M6G1
-
-
Streptococcus thermophilus ATCC BAA-250 Q5M6G1
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
central competence regulator sigmax + H2O adaptor protein MecA ultimately targets sigmaX for its degradation by the ClpCP protease in an ATP-dependent manner Streptococcus thermophilus ?
-
?
central competence regulator sigmax + H2O adaptor protein MecA ultimately targets sigmaX for its degradation by the ClpCP protease in an ATP-dependent manner Streptococcus thermophilus ATCC BAA-250 ?
-
?

Synonyms

Synonyms Comment Organism
CplC
-
Streptococcus thermophilus

General Information

General Information Comment Organism
physiological function adaptor protein MecA specifically interacts with both central competence regulator sigmax and protease ClpC, suggesting the formation of a ternary sigmaX-MecA-ClpC complex. MecA ultimately targets sigmaX for its degradation by the ClpCP protease in an ATP-dependent manner. A short sequence of 18 amino acids in the N-terminal domain of sigmaX is essential for the interaction with MecA and subsequent sigmaX degradation. Increased transformability of a MecA-deficient strain in the presence of subinducing SigX-inducing peptide concentrations suggests that the MecA-ClpCP proteolytic complex acts as an additional locking device to prevent competence under inappropriate conditions Streptococcus thermophilus