Periplasmic serine protease Do, heat shock protein; Belongs to the peptidase S1C family.

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

Periplasmic serine protease Do, heat shock protein; Belongs to the peptidase S1C family.

Periplasmic protein disulfide isomerase I.

Periplasmic serine protease Do, heat shock protein; Belongs to the peptidase S1C family.

Co-chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.

Periplasmic serine protease Do, heat shock protein; Belongs to the peptidase S1C family.

Hsp 24 nucleotide exchange factor; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. 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 roun [...]

Periplasmic serine protease Do, heat shock protein; Belongs to the peptidase S1C family.

Preprotein translocase SecY; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.

Periplasmic serine protease Do, heat shock protein; Belongs to the peptidase S1C family.

Translocase; Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving both as a receptor for the preprotein-SecB complex and as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane.

Periplasmic serine protease Do, heat shock protein; Belongs to the peptidase S1C family.

Inner membrane protein translocase component YidC; Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispanning membrane proteins.

Dna-J like membrane chaperone protein; Regulatory DnaK co-chaperone. Direct interaction between DnaK and DjlA is needed for the induction of the wcaABCDE operon, involved in the synthesis of a colanic acid polysaccharide capsule, possibly through activation of the RcsB/RcsC phosphotransfer signaling pathway. The colanic acid capsule may help the bacterium survive conditions outside the host.

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

Dna-J like membrane chaperone protein; Regulatory DnaK co-chaperone. Direct interaction between DnaK and DjlA is needed for the induction of the wcaABCDE operon, involved in the synthesis of a colanic acid polysaccharide capsule, possibly through activation of the RcsB/RcsC phosphotransfer signaling pathway. The colanic acid capsule may help the bacterium survive conditions outside the host.

Hsp 24 nucleotide exchange factor; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. 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 roun [...]

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

Periplasmic serine protease Do, heat shock protein; Belongs to the peptidase S1C family.

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

Dna-J like membrane chaperone protein; Regulatory DnaK co-chaperone. Direct interaction between DnaK and DjlA is needed for the induction of the wcaABCDE operon, involved in the synthesis of a colanic acid polysaccharide capsule, possibly through activation of the RcsB/RcsC phosphotransfer signaling pathway. The colanic acid capsule may help the bacterium survive conditions outside the host.

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

Co-chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.

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

Hsp 24 nucleotide exchange factor; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. 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 roun [...]

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

Preprotein translocase SecY; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.

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

Thioredoxin; Belongs to the thioredoxin family.

Periplasmic protein disulfide isomerase I.

Periplasmic serine protease Do, heat shock protein; Belongs to the peptidase S1C family.

Periplasmic protein disulfide isomerase I.

Outer-membrane lipoprotein carrier protein precursor; Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane).

Co-chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.

Periplasmic serine protease Do, heat shock protein; Belongs to the peptidase S1C family.

Co-chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.

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

Co-chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.

Hsp 24 nucleotide exchange factor; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. 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 roun [...]