EC Number   |
General Information |
Reference |
|---|
   3.4.21.102 | evolution |
the enzyme CtpB belongs to the widespread family of PDZ-proteases |
731635 |
| 3.4.21.102 | more |
the CtpB protease is organized as a dimeric ring with the catalytic site burried within a tunnel. The PDZ domain controls access to the protease tunnel. Residues Ser309, Lys334, and Gln338 function as catalytic triad mediating cleavage of the 4FA substrate. A peptide ligand, which copurifies and cocrystallizes with CtpB, is observed at the entrance of the protease tunnel near the catalytic triad |
731635 |
| 3.4.21.102 | physiological function |
a mutant lacking CtpA retains all D1 protein in precursor form, confirming that CtpA is solely responsible for processing. A knockout Ctpa mutant is lethal under normal growth conditions but is viable with sucrose under low-light conditions. Viable plants show deficiencies in PSII and thylakoid stacking. The mutant retains both monomer and dimer forms of the PSII complexes that, although nonfunctional, contain both the core and extrinsic subunits. This mutant is also essentially devoid of PSII supercomplexes. A knock-down mutant expressing about 2% wild-type level of CtpA shows normal growth under low light but is stunted and accumulats D1 protein precursor under high light |
732822 |
| 3.4.21.102 | physiological function |
disruption of the ctpA gene leads to decreased heat tolerance and increased sensitivity when exposed to components of the host immune system. The ctpA mutant strain is attenuated for virulence in a murine model of infection |
732467 |
| 3.4.21.102 | physiological function |
heterologous expression in the 4E-3 mutant strain of the model non-nitrogen-fixing cyanobacterium Synechocystis sp. PCC 6803, which lacks any psbA gene. The resultant strain cannot grow photoautotrophically. These Synechocystis 6803 cells are incapable of PSII-mediated oxygen evolution. This D1 isoform, sentinel D1, represents a class of D1 protein that, when incorporated in a PSII complex, ensures that PSII cannot mediate water oxidation, thus allowing oxygen-sensitive processes such as nitrogen fixation to occur in cyanobacterial cells |
732180 |
| 3.4.21.102 | physiological function |
Lack of protease Prc suppresses bile sensitivity in Dam-, Wec-, PhoP-, DamX-, and SeqA- mutants of Salmonella enterica, and increases bile resistance in the wild type. Changes in the activity of penicillin binding proteins PBP3, PBP4, PBP5/6 and PBP7 are detected in a Prc- background, suggesting that peptidoglycan remodeling might contribute to bile resistance |
-, 731957 |
| 3.4.21.102 | physiological function |
photosystem II core protein D1 is inserted into the thylakoid membrane with a C-terminal extension which requires cleavage by C-terminal processing protease CtpA, to allow subsequent assembly of the oxygen-evolving complex. D1 precursor insertion as well as its conversion to mature D1 under various light conditions is seen only in the thylakoid membrane |
755032 |
| 3.4.21.102 | physiological function |
PrC plays a protective role in oxidative stress in Clonostachys rosea. PrC is required for protection against stress-induced inhibition of conidial germination in the presence of nematode cuticle and plays a role in scavenging reactive oxygen species by oxidants and heat shock |
-, 718260 |
| 3.4.21.102 | physiological function |
protease Prc is involved in virulence. Mutation of Prc also results in susceptibility to multiple environmental stresses, including H2O2, sodium dodecylsulfate, and osmolarity stresses. The amounts of 34 periplasmic proteins are lower in the Prc mutant than in wild-type. These proteins are associated with proteolysis, biosynthesis of macromolecules, carbohydrate or energy metabolism, signal transduction, and protein translocation or folding. Prc stabilizes and directly binds to dipeptidyl peptidase DppP which contributes to full virulence |
732544 |
| 3.4.21.102 | physiological function |
spore formation in Bacillus subtilis relies on a regulated intramembrane proteolysis pathway, involving the enzyme, that synchronizes mother-cell and forespore development. Activating protease CtpB assembles a gated protease tunnel regulating cell-cell signaling during spore formation. Activation of the SpoIV RIP pathway is induced by the concerted activity of enzyme CtpB and a second signaling protease, SpoIVB. Molecular basis of this SpoIV transmembrane signaling, the enzyme resembles a minimal version of a self-compartmentalizing protease regulated by a unique allosteric mechanism, overview |
731635 |
