STRINGSTRING
dnaJ dnaJ dnaK dnaK grpE grpE ABK70298.1 ABK70298.1 clpB clpB groL-2 groL-2 groL groL ABK72867.1 ABK72867.1 ABK71946.1 ABK71946.1 ABK75774.1 ABK75774.1 ABK73428.1 ABK73428.1
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:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
dnaJChaperone 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 [...] (390 aa)    
Predicted Functional Partners:
dnaK
Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
 0.999
grpE
Co-chaperone 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 of ATP-depend [...]
  
 
 0.999
ABK70298.1
Transcriptional regulator, MerR family protein; Identified by match to protein family HMM PF00376.
  
 
 0.996
clpB
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.
 
 
 0.979
groL-2
Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 0.959
groL
Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
  
 0.954
ABK72867.1
Conserved hypothetical proline rich protein.
 
 0.906
ABK71946.1
Conserved hypothetical proline and threonine rich protein.
 
 0.903
ABK75774.1
Conserved hypothetical proline rich protein.
  
 0.892
ABK73428.1
Conserved hypothetical protein.
  
 0.891
Your Current Organism:
Mycolicibacterium smegmatis
NCBI taxonomy Id: 246196
Other names: M. smegmatis MC2 155, Mycobacterium smegmatis MC2 155, Mycolicibacterium smegmatis MC2 155
Server load: low (22%) [HD]