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ABI61528.1 | Molecular chaperones (DnaJ family). (204 aa) | ||||
dnaJ | 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 [...] (376 aa) | ||||
dnaK | Chaperone protein dnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. (632 aa) | ||||
grpE | grpE protein; 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 of ATP-dependent i [...] (226 aa) | ||||
htpG | Chaperone protein htpG; Molecular chaperone. Has ATPase activity. (696 aa) | ||||
ABI61275.1 | Outer membrane protein. (259 aa) | ||||
ABI61339.1 | DnaJ-like protein djlA. (276 aa) | ||||
secB | Protein translocase subunit secB; One of the proteins required for the normal export of preproteins out of the cell cytoplasm. It is a molecular chaperone that binds to a subset of precursor proteins, maintaining them in a translocation-competent state. It also specifically binds to its receptor SecA. (182 aa) | ||||
ABI63167.1 | 33 kDa chaperonin; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family. (317 aa) | ||||
ABI63094.1 | Peptidyl-prolyl cis-trans isomerase. (468 aa) | ||||
groS | 10 kDa chaperonin GROES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. (101 aa) | ||||
groL | 60 kDa chaperonin GROEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (544 aa) | ||||
ureE | Urease accessory protein ureE; Involved in urease metallocenter assembly. Binds nickel. Probably functions as a nickel donor during metallocenter assembly. Belongs to the UreE family. (176 aa) | ||||
clpB | clpB 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. (865 aa) | ||||
ABI62649.1 | ATP-dependent clp protease ATP-binding subunit clpA; Belongs to the ClpA/ClpB family. (851 aa) | ||||
ABI62359.1 | Curved DNA-binding protein. (298 aa) | ||||
ABI62226.1 | Chaperone protein ecpD. (239 aa) | ||||
tig | Trigger factor, ppiase; 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. (444 aa) | ||||
clpX | ATP-dependent endopeptidase clp 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. (420 aa) | ||||
ABI62115.1 | Peptidyl-prolyl cis-trans isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. (186 aa) | ||||
ABI61839.1 | Hypothetical protein. (301 aa) |