Proteolytic subunit of ClpA-ClpP and ClpX-ClpP ATP-dependent serine proteases; 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. May play the role of a master protease which is attracted to different substrates by different specificity factors such as ClpA or ClpX. Participates in the final steps of RseA-sigma-E degradation, liberating sigma-E to induce the extracytoplasmic-stress response. Degrades antitoxin MazE.

ATPase and specificity subunit of ClpX-ClpP ATP-dependent serine protease; ATP-dependent specificity component of the Clp protease. Uses cycles of ATP binding and hydrolysis to unfold proteins and translocate them to the ClpP protease. It directs the protease to specific substrates both with and without the help of adapter proteins such as SspB. Participates in the final steps of RseA-sigma-E degradation, liberating sigma-E to induce the extracytoplasmic-stress response. It may bind to the lambda O substrate protein and present it to the ClpP protease in a form that can be recognized a [...]

Proteolytic subunit of ClpA-ClpP and ClpX-ClpP ATP-dependent serine proteases; 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. May play the role of a master protease which is attracted to different substrates by different specificity factors such as ClpA or ClpX. Participates in the final steps of RseA-sigma-E degradation, liberating sigma-E to induce the extracytoplasmic-stress response. Degrades antitoxin MazE.

Chaperone Hsp70, with co-chaperone DnaJ; Plays an essential role in the initiation of phage lambda DNA replication, where it acts in an ATP-dependent fashion with the DnaJ protein to release lambda O and P proteins from the preprimosomal complex. DnaK is also involved in chromosomal DNA replication, possibly through an analogous interaction with the DnaA protein. Also participates actively in the response to hyperosmotic shock.

Proteolytic subunit of ClpA-ClpP and ClpX-ClpP ATP-dependent serine proteases; 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. May play the role of a master protease which is attracted to different substrates by different specificity factors such as ClpA or ClpX. Participates in the final steps of RseA-sigma-E degradation, liberating sigma-E to induce the extracytoplasmic-stress response. Degrades antitoxin MazE.

Molecular chaperone and ATPase component of HslUV protease; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis.

Proteolytic subunit of ClpA-ClpP and ClpX-ClpP ATP-dependent serine proteases; 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. May play the role of a master protease which is attracted to different substrates by different specificity factors such as ClpA or ClpX. Participates in the final steps of RseA-sigma-E degradation, liberating sigma-E to induce the extracytoplasmic-stress response. Degrades antitoxin MazE.

Peptidase component of the HslUV protease; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. The complex has been shown to be involved in the specific degradation of heat shock induced transcription factors such as RpoH and SulA. In addition, small hydrophobic peptides are also hydrolyzed by HslV. HslV has weak protease activity even in the absence of HslU, but this activity is induced more than 100-fold in the presence of HslU. HslU recognizes protein substrates and unfolds these before guiding them to HslV for hydrolysis. [...]

Proteolytic subunit of ClpA-ClpP and ClpX-ClpP ATP-dependent serine proteases; 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. May play the role of a master protease which is attracted to different substrates by different specificity factors such as ClpA or ClpX. Participates in the final steps of RseA-sigma-E degradation, liberating sigma-E to induce the extracytoplasmic-stress response. Degrades antitoxin MazE.

beta-D-galactosidase; Protein involved in carbohydrate catabolic process; Belongs to the glycosyl hydrolase 2 family.

Proteolytic subunit of ClpA-ClpP and ClpX-ClpP ATP-dependent serine proteases; 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. May play the role of a master protease which is attracted to different substrates by different specificity factors such as ClpA or ClpX. Participates in the final steps of RseA-sigma-E degradation, liberating sigma-E to induce the extracytoplasmic-stress response. Degrades antitoxin MazE.

RNA polymerase, sigma 32 (sigma H) factor; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is involved in regulation of expression of heat shock genes. Intracellular concentration of free RpoH protein increases in response to heat shock, which causes association with RNA polymerase (RNAP) and initiation of transcription of heat shock genes, including numerous global transcriptional regulators and genes involved in maintaining membrane functionality and homeostasis. RpoH is then quic [...]

ATPase and specificity subunit of ClpX-ClpP ATP-dependent serine protease; ATP-dependent specificity component of the Clp protease. Uses cycles of ATP binding and hydrolysis to unfold proteins and translocate them to the ClpP protease. It directs the protease to specific substrates both with and without the help of adapter proteins such as SspB. Participates in the final steps of RseA-sigma-E degradation, liberating sigma-E to induce the extracytoplasmic-stress response. It may bind to the lambda O substrate protein and present it to the ClpP protease in a form that can be recognized a [...]

Proteolytic subunit of ClpA-ClpP and ClpX-ClpP ATP-dependent serine proteases; 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. May play the role of a master protease which is attracted to different substrates by different specificity factors such as ClpA or ClpX. Participates in the final steps of RseA-sigma-E degradation, liberating sigma-E to induce the extracytoplasmic-stress response. Degrades antitoxin MazE.

ATPase and specificity subunit of ClpX-ClpP ATP-dependent serine protease; ATP-dependent specificity component of the Clp protease. Uses cycles of ATP binding and hydrolysis to unfold proteins and translocate them to the ClpP protease. It directs the protease to specific substrates both with and without the help of adapter proteins such as SspB. Participates in the final steps of RseA-sigma-E degradation, liberating sigma-E to induce the extracytoplasmic-stress response. It may bind to the lambda O substrate protein and present it to the ClpP protease in a form that can be recognized a [...]

Chaperone Hsp70, with co-chaperone DnaJ; Plays an essential role in the initiation of phage lambda DNA replication, where it acts in an ATP-dependent fashion with the DnaJ protein to release lambda O and P proteins from the preprimosomal complex. DnaK is also involved in chromosomal DNA replication, possibly through an analogous interaction with the DnaA protein. Also participates actively in the response to hyperosmotic shock.

ATPase and specificity subunit of ClpX-ClpP ATP-dependent serine protease; ATP-dependent specificity component of the Clp protease. Uses cycles of ATP binding and hydrolysis to unfold proteins and translocate them to the ClpP protease. It directs the protease to specific substrates both with and without the help of adapter proteins such as SspB. Participates in the final steps of RseA-sigma-E degradation, liberating sigma-E to induce the extracytoplasmic-stress response. It may bind to the lambda O substrate protein and present it to the ClpP protease in a form that can be recognized a [...]

Molecular chaperone and ATPase component of HslUV protease; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis.

ATPase and specificity subunit of ClpX-ClpP ATP-dependent serine protease; ATP-dependent specificity component of the Clp protease. Uses cycles of ATP binding and hydrolysis to unfold proteins and translocate them to the ClpP protease. It directs the protease to specific substrates both with and without the help of adapter proteins such as SspB. Participates in the final steps of RseA-sigma-E degradation, liberating sigma-E to induce the extracytoplasmic-stress response. It may bind to the lambda O substrate protein and present it to the ClpP protease in a form that can be recognized a [...]

Peptidase component of the HslUV protease; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. The complex has been shown to be involved in the specific degradation of heat shock induced transcription factors such as RpoH and SulA. In addition, small hydrophobic peptides are also hydrolyzed by HslV. HslV has weak protease activity even in the absence of HslU, but this activity is induced more than 100-fold in the presence of HslU. HslU recognizes protein substrates and unfolds these before guiding them to HslV for hydrolysis. [...]

ATPase and specificity subunit of ClpX-ClpP ATP-dependent serine protease; ATP-dependent specificity component of the Clp protease. Uses cycles of ATP binding and hydrolysis to unfold proteins and translocate them to the ClpP protease. It directs the protease to specific substrates both with and without the help of adapter proteins such as SspB. Participates in the final steps of RseA-sigma-E degradation, liberating sigma-E to induce the extracytoplasmic-stress response. It may bind to the lambda O substrate protein and present it to the ClpP protease in a form that can be recognized a [...]

beta-D-galactosidase; Protein involved in carbohydrate catabolic process; Belongs to the glycosyl hydrolase 2 family.

ATPase and specificity subunit of ClpX-ClpP ATP-dependent serine protease; ATP-dependent specificity component of the Clp protease. Uses cycles of ATP binding and hydrolysis to unfold proteins and translocate them to the ClpP protease. It directs the protease to specific substrates both with and without the help of adapter proteins such as SspB. Participates in the final steps of RseA-sigma-E degradation, liberating sigma-E to induce the extracytoplasmic-stress response. It may bind to the lambda O substrate protein and present it to the ClpP protease in a form that can be recognized a [...]

RNA polymerase, sigma 32 (sigma H) factor; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is involved in regulation of expression of heat shock genes. Intracellular concentration of free RpoH protein increases in response to heat shock, which causes association with RNA polymerase (RNAP) and initiation of transcription of heat shock genes, including numerous global transcriptional regulators and genes involved in maintaining membrane functionality and homeostasis. RpoH is then quic [...]

Chaperone Hsp70, with co-chaperone DnaJ; Plays an essential role in the initiation of phage lambda DNA replication, where it acts in an ATP-dependent fashion with the DnaJ protein to release lambda O and P proteins from the preprimosomal complex. DnaK is also involved in chromosomal DNA replication, possibly through an analogous interaction with the DnaA protein. Also participates actively in the response to hyperosmotic shock.

Proteolytic subunit of ClpA-ClpP and ClpX-ClpP ATP-dependent serine proteases; 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. May play the role of a master protease which is attracted to different substrates by different specificity factors such as ClpA or ClpX. Participates in the final steps of RseA-sigma-E degradation, liberating sigma-E to induce the extracytoplasmic-stress response. Degrades antitoxin MazE.

Chaperone Hsp70, with co-chaperone DnaJ; Plays an essential role in the initiation of phage lambda DNA replication, where it acts in an ATP-dependent fashion with the DnaJ protein to release lambda O and P proteins from the preprimosomal complex. DnaK is also involved in chromosomal DNA replication, possibly through an analogous interaction with the DnaA protein. Also participates actively in the response to hyperosmotic shock.

ATPase and specificity subunit of ClpX-ClpP ATP-dependent serine protease; ATP-dependent specificity component of the Clp protease. Uses cycles of ATP binding and hydrolysis to unfold proteins and translocate them to the ClpP protease. It directs the protease to specific substrates both with and without the help of adapter proteins such as SspB. Participates in the final steps of RseA-sigma-E degradation, liberating sigma-E to induce the extracytoplasmic-stress response. It may bind to the lambda O substrate protein and present it to the ClpP protease in a form that can be recognized a [...]

Chaperone Hsp70, with co-chaperone DnaJ; Plays an essential role in the initiation of phage lambda DNA replication, where it acts in an ATP-dependent fashion with the DnaJ protein to release lambda O and P proteins from the preprimosomal complex. DnaK is also involved in chromosomal DNA replication, possibly through an analogous interaction with the DnaA protein. Also participates actively in the response to hyperosmotic shock.

Molecular chaperone and ATPase component of HslUV protease; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis.

Chaperone Hsp70, with co-chaperone DnaJ; Plays an essential role in the initiation of phage lambda DNA replication, where it acts in an ATP-dependent fashion with the DnaJ protein to release lambda O and P proteins from the preprimosomal complex. DnaK is also involved in chromosomal DNA replication, possibly through an analogous interaction with the DnaA protein. Also participates actively in the response to hyperosmotic shock.

Peptidase component of the HslUV protease; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. The complex has been shown to be involved in the specific degradation of heat shock induced transcription factors such as RpoH and SulA. In addition, small hydrophobic peptides are also hydrolyzed by HslV. HslV has weak protease activity even in the absence of HslU, but this activity is induced more than 100-fold in the presence of HslU. HslU recognizes protein substrates and unfolds these before guiding them to HslV for hydrolysis. [...]

Chaperone Hsp70, with co-chaperone DnaJ; Plays an essential role in the initiation of phage lambda DNA replication, where it acts in an ATP-dependent fashion with the DnaJ protein to release lambda O and P proteins from the preprimosomal complex. DnaK is also involved in chromosomal DNA replication, possibly through an analogous interaction with the DnaA protein. Also participates actively in the response to hyperosmotic shock.

beta-D-galactosidase; Protein involved in carbohydrate catabolic process; Belongs to the glycosyl hydrolase 2 family.

Chaperone Hsp70, with co-chaperone DnaJ; Plays an essential role in the initiation of phage lambda DNA replication, where it acts in an ATP-dependent fashion with the DnaJ protein to release lambda O and P proteins from the preprimosomal complex. DnaK is also involved in chromosomal DNA replication, possibly through an analogous interaction with the DnaA protein. Also participates actively in the response to hyperosmotic shock.

RNA polymerase, sigma 32 (sigma H) factor; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is involved in regulation of expression of heat shock genes. Intracellular concentration of free RpoH protein increases in response to heat shock, which causes association with RNA polymerase (RNAP) and initiation of transcription of heat shock genes, including numerous global transcriptional regulators and genes involved in maintaining membrane functionality and homeostasis. RpoH is then quic [...]

Molecular chaperone and ATPase component of HslUV protease; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis.

Proteolytic subunit of ClpA-ClpP and ClpX-ClpP ATP-dependent serine proteases; 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. May play the role of a master protease which is attracted to different substrates by different specificity factors such as ClpA or ClpX. Participates in the final steps of RseA-sigma-E degradation, liberating sigma-E to induce the extracytoplasmic-stress response. Degrades antitoxin MazE.

Molecular chaperone and ATPase component of HslUV protease; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis.

ATPase and specificity subunit of ClpX-ClpP ATP-dependent serine protease; ATP-dependent specificity component of the Clp protease. Uses cycles of ATP binding and hydrolysis to unfold proteins and translocate them to the ClpP protease. It directs the protease to specific substrates both with and without the help of adapter proteins such as SspB. Participates in the final steps of RseA-sigma-E degradation, liberating sigma-E to induce the extracytoplasmic-stress response. It may bind to the lambda O substrate protein and present it to the ClpP protease in a form that can be recognized a [...]