ATP-dependent Clp protease proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family.

ATP-dependent protease ATP-binding subunit; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP.

ATP-dependent Clp protease proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family.

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

ATP-dependent Clp protease proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family.

Cell division protein FtsZ; Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity.

ATP-dependent Clp protease proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family.

Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.

ATP-dependent Clp protease proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family.

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

ATP-dependent Clp protease proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 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 [...]

ATP-dependent Clp protease proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family.

Heat shock protein 90; Molecular chaperone. Has ATPase activity.

ATP-dependent Clp protease proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family.

DNA-binding ATP-dependent protease La; 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.

ATP-dependent Clp protease proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family.

DNA-directed RNA polymerase beta subunit; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.

ATP-dependent Clp protease proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family.

Trigger factor; Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase; Belongs to the FKBP-type PPIase family. Tig subfamily.

ATP-dependent protease ATP-binding subunit; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP.

ATP-dependent Clp protease proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family.

ATP-dependent protease ATP-binding subunit; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP.

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

ATP-dependent protease ATP-binding subunit; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP.

Cell division protein FtsZ; Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity.

ATP-dependent protease ATP-binding subunit; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP.

Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.

ATP-dependent protease ATP-binding subunit; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP.

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

ATP-dependent protease ATP-binding subunit; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP.

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 [...]

ATP-dependent protease ATP-binding subunit; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP.

Heat shock protein 90; Molecular chaperone. Has ATPase activity.

ATP-dependent protease ATP-binding subunit; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP.

DNA-binding ATP-dependent protease La; 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.

ATP-dependent protease ATP-binding subunit; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP.

Transcription termination factor Rho; Facilitates transcription termination by a mechanism that involves Rho binding to the nascent RNA, activation of Rho's RNA- dependent ATPase activity, and release of the mRNA from the DNA template.

ATP-dependent protease ATP-binding subunit; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP.

DNA-directed RNA polymerase beta subunit; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.