EC Number   |
Natural Substrates |
|---|
   3.6.5.4 | more |
the cpFtsY membrane-binding motif plays a critical role in the intramolecular communication that regulates cpSRP receptor functions at the membrane |
| 3.6.5.4 | GTP + H2O |
the multidomain protein SRP54 acts as a key player in SRP-mediated protein transport, the GTPase drives the SRP cycle |
| 3.6.5.4 | more |
the sensor protein KdpD requires the signal recognition particle for its targeting to the membrane, small amphiphilic region of 27 residues within the amino-terminal domain of KdpD (amino acids 22-48) is recognized by SRP and targets the protein to the membrane, depletion of the Ffh component of SRP largely inhibits KdpD insertion |
| 3.6.5.4 | GTP + H2O |
the signal recognition particle mediates the co-translational targeting of nascent proteins to the bacterial plasma membrane. During this process, two GTPases, one in the signal recognition particle and one in the signal recogition particle receptor, form a complex in which both proteins reciprocally activate the GTPase reaction of one another. Crystal structures of the complex of signal recognition particle and signal recogition particle receptor show that the two GTPases associate via an unusually extensive and highly cooperative interaction surface and form a composite active site at the interface. GTPase activation proceeds through a unique mechanism, stimulated by both interactions between the twinned GTP molecules across the dimer interface and by conformational rearrangements that position catalytic residues in each active site with respect to the bound substrate |
| 3.6.5.4 | more |
the signal recognition particle pathway is important for virulence factor secretion in Streptococcus pyogenes |
