STRINGSTRING
STRING protein interaction network
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
dnaKChaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. (629 aa)    
Predicted Functional Partners:
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 [...]
 
 0.999
Dgeo_2078
PFAM: heat shock protein DnaJ-like: (1.3e-40) chaperone DnaJ-like: (9.7e-46); KEGG: dra:DR0126 DnaJ protein, ev=1e-132, 79% identity.
 0.998
dnaJ
Chaperone DnaJ-like 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 Dn [...]
 0.995
groL
Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 
 0.987
groS
Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
  
 
 0.968
Dgeo_0875
Uncharacterized secreted protein containing TPR-like repeats; KEGG: dra:DR1200 hypothetical protein, ev=1e-83, 66% identity.
  
 0.961
rplP
Ribosomal protein L16; Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs; Belongs to the universal ribosomal protein uL16 family.
   
 
 0.923
clpB
ATPase AAA-2; 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.
  
 
 0.915
Dgeo_0207
TIGRFAM: SUF system FeS assembly protein: (1.9e-44); PFAM: nitrogen-fixing NifU-like-like: (3.6e-12); KEGG: tth:TTC1374 IscU protein, ev=3e-32, 54% identity.
 
 
 0.877
Dgeo_1215
ATP-dependent Clp protease ATP-binding subunit ClpA; PFAM: AAA ATPase, central region: (4.6e-06) Clp, N terminal: (3e-10) ATPase associated with various cellular activities, AAA_5: (2.2e-05) ATPase AAA-2: (3.5e-90); SMART: ATPase: (2.1e-17); KEGG: dra:DR1117 ATP-dependent Clp protease, ATP-binding subunit ClpC, ev=0.0, 89% identity; Belongs to the ClpA/ClpB family.
  
 
 0.868
Your Current Organism:
Deinococcus geothermalis
NCBI taxonomy Id: 319795
Other names: D. geothermalis DSM 11300, Deinococcus geothermalis AG-3a, Deinococcus geothermalis CIP 105573, Deinococcus geothermalis DSM 11300, Deinococcus geothermalis str. DSM 11300, Deinococcus geothermalis strain DSM 11300
Server load: low (20%) [HD]