Subsystem: Proteolysis in bacteria, ATP-dependent

This subsystem's description is:

The cytosolic pathway leading to release of amino acids from an intact protein can be divided into two parts based on the utilization of metabolic energy: the proximal ATP-dependent steps are followed by ATP-independent events. This basic model of protein unfolding followed by degradation is conserved in eubacteria, archaea and eukaryotes and involves several steps (for the best review see Ref.1). First, ATP-dependent enzymes are responsible for the recognition, unfolding and cleavage of substrate proteins into large peptides. These enzymes harbor a domain conferring ATPase activity, belonging to the ATPase family associated with various cellular activities (AAA) in the same polypeptide (e.g., Lon) or associated with a different polypeptide-containing ATPase activity (e.g., ClpA, ClpX, ClpY, 19S regulator). Substrat proteins are unfolded by regulators via conformational changes driven by ATP hydrolysis. Next, unfolded substrate proteins are actively translocated into the proteolytic chambers present in the proteases, which make the initial cuts to generate large peptides. These are cleaved into smaller peptides and, finally, into amino acids, which are recycled into the cellular pool. The ATP-independent steps of the cytosolic protein degradation pathway are often referred to as “downstream processing of peptides”.

======Variant codes:========================

1 - Lon + ClpP + ClpQY
2 - Lon + ClpP (no heat shock operon ClpQY);
3 - Lon is absent (like in many Gram-positive bacteria);
4 - ClpP is absent;
5 - just ClpP (no Lon and ClpQY) (like in Synechococcus);
6 - just Lon

For more information, please check out the description and the additional notes tabs, below

DiagramFunctional RolesSubsystem SpreadsheetDescriptionAdditional Notes 

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