STRINGSTRING
dnaJ dnaJ dnaK dnaK grpE grpE hrcA hrcA CHR53_25250 CHR53_25250 CHR53_27645 CHR53_27645 CHR53_27905 CHR53_27905 groS groS groL groL clpB clpB htpG htpG CHR53_11745 CHR53_11745
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
dnaJUnannotated protein; 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, DnaK [...] (378 aa)
dnaKUnannotated protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. (611 aa)
grpEUnannotated 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-depe [...] (204 aa)
hrcAUnannotated protein; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. (344 aa)
CHR53_25250Unannotated protein. (263 aa)
CHR53_27645Unannotated protein. (388 aa)
CHR53_27905Unannotated protein. (396 aa)
groSUnannotated protein; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. (95 aa)
groLUnannotated protein; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (542 aa)
clpBUnannotated 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)
htpGUnannotated protein; Molecular chaperone. Has ATPase activity. (627 aa)
CHR53_11745Unannotated protein. (171 aa)
Your Current Organism:
Bacillus mesonae
NCBI taxonomy Id: 1193713
Other names: B. mesonae, Bacillus mesonae Liu et al. 2014, Bacillus sp. FJAT-13985, CGMCC1.12238, DSM 25968, strain FJAT-13985
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