STRINGSTRING
hrcA hrcA dnaJ dnaJ OBJ90234.1 OBJ90234.1 groEL groEL OBJ87992.1 OBJ87992.1 clpB clpB OBJ86320.1 OBJ86320.1 dnaJ-2 dnaJ-2 grpE grpE dnaK dnaK htpG htpG groEL-4 groEL-4
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:
hrcAHeat-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)
dnaJMolecular chaperone 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, [...] (383 aa)
OBJ90234.1Molecular chaperone Hsp70; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heat shock protein 70 family. (509 aa)
groELMolecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (397 aa)
OBJ87992.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (610 aa)
clpBATP-dependent chaperone ClpB; 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. (848 aa)
OBJ86320.1MerR family transcriptional regulator; Derived by automated computational analysis using gene prediction method: Protein Homology. (129 aa)
dnaJ-2Molecular chaperone 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, [...] (389 aa)
grpENucleotide 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 [...] (216 aa)
dnaKMolecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. (622 aa)
htpGMolecular chaperone HtpG; Molecular chaperone. Has ATPase activity. (648 aa)
groEL-4Molecular chaperone GroEL; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. (100 aa)
Your Current Organism:
Mycobacterium gordonae
NCBI taxonomy Id: 1778
Other names: ATCC 14470, CCUG 21801, CCUG 21811, CIP 104529, DSM 44160, JCM 6382, M. gordonae, NCTC 10267
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