Map Methionine aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.

Integral membrane protein.

rplQ 50S ribosomal protein L17; Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.

Protease II.

Holliday junction DNA helicase ruvB; The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing.

Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.

Chaperone protein DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, D [...]

Gap Glyceraldehyde 3-phosphate dehydrogenase; Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.

groEL 60 kDa chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.