Acetoin utilization protein AcuC.

Lon protease; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner.

Proteasome-associated ATPase; ATPase which is responsible for recognizing, binding, unfolding and translocation of pupylated proteins into the bacterial 20S proteasome core particle. May be essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C-termini of the proteasomal ATPase may function like a 'key in a lock' to induce gate opening and therefore regulate proteolysis.

Molecular chaperone Hsp31 and glyoxalase 3.

Proteasome subunit beta 1; Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. Belongs to the peptidase T1B family.

ATP-dependent zinc metalloprotease FtsH; Belongs to the AAA ATPase family.

Hypothetical protein.

Proteasome subunit alpha 2; Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. Belongs to the peptidase T1A family.