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ssuB | Aliphatic sulfonate ABC transporter ATP-binding protein; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family. (861 aa) | ||||
htpG | Hypothetical protein; Molecular chaperone. Has ATPase activity. (634 aa) | ||||
clpA | ATP-dependent Clp protease ATP-binding subunit ClpA; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the ClpA/ClpB family. (760 aa) | ||||
clpS | ATP-dependent Clp protease adapter ClpS; Involved in the modulation of the specificity of the ClpAP- mediated ATP-dependent protein degradation; Belongs to the ClpS family. (108 aa) | ||||
dnaJ | TetR family transcriptional regulator; 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 [...] (375 aa) | ||||
dnaK | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. (641 aa) | ||||
grpE | Nucleotide exchange factor GrpE; 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 rounds [...] (172 aa) | ||||
hrcA | Heat-inducible transcriptional repressor HrcA; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. (343 aa) | ||||
BJD11_15590 | Peptidylprolyl isomerase; Frameshifted; Derived by automated computational analysis using gene prediction method: Protein Homology. (458 aa) | ||||
APO91352.1 | Molecular chaperone HtpG; Derived by automated computational analysis using gene prediction method: Protein Homology. (622 aa) | ||||
cbpA | Cytochrome C biogenesis protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (299 aa) | ||||
APO91460.1 | Heat-shock protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the small heat shock protein (HSP20) family. (158 aa) | ||||
lon | Endopeptidase 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. (823 aa) | ||||
clpX | ATP-dependent protease ATP-binding subunit ClpX; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. (428 aa) | ||||
clpP | ATP-dependent Clp endopeptidase, proteolytic subunit ClpP; 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. (208 aa) | ||||
hslU | HslU--HslV peptidase ATPase subunit; 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. (455 aa) | ||||
hslV | HslU--HslV peptidase proteolytic subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. (183 aa) | ||||
groL | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (546 aa) | ||||
groS | Co-chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. (95 aa) |