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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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Co-expression
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[Homology]
Score
dnaKChaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. (630 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 [...]
 
 0.980
Plim_0663
PFAM: chaperone DnaJ domain protein; heat shock protein DnaJ domain protein; SMART: heat shock protein DnaJ domain protein; KEGG: dvu:DVU1876 DnaJ protein, putative.
 
  0.931
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 [...]
 
  0.911
clpB
ATP-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.
  
 
 0.854
Plim_1055
PFAM: glycosyl transferase family 2; Methyltransferase type 12; Methyltransferase type 11; TPR repeat-containing protein; Methionine biosynthesis MetW protein; Tetratricopeptide TPR_2 repeat protein; SMART: Tetratricopeptide domain protein; KEGG: gbm:Gbem_3740 glycosyl transferase family 2.
  
 0.795
Plim_0602
PFAM: RNA polymerase alpha subunit domain protein; TPR repeat-containing protein; Tetratricopeptide TPR_2 repeat protein; SMART: Tetratricopeptide domain protein; KEGG: dol:Dole_1087 TPR repeat-containing protein.
  
 0.788
Plim_1779
PFAM: ATP-binding region ATPase domain protein; KEGG: mxa:MXAN_1393 ATPase, histidine kinase-, DNA gyrase B-, and HSP90-like domain protein.
   
 0.777
htpG
Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity.
   
 0.777
groL-3
Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 0.731
groL
Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 0.729
Your Current Organism:
Planctopirus limnophila
NCBI taxonomy Id: 521674
Other names: P. limnophila DSM 3776, Planctomyces limnophilus ATCC 43296, Planctomyces limnophilus DSM 3776, Planctomyces limnophilus str. DSM 3776, Planctomyces limnophilus strain DSM 3776, Planctopirus limnophila DSM 3776, Planctopirus limnophilus DSM 3776
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