STRINGSTRING
Mettu_3601 protein (Methylobacter tundripaludum) - STRING interaction network
"Mettu_3601" - Heat shock protein 70 in Methylobacter tundripaludum
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:
some 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 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
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
Mettu_3601Heat shock protein 70 (432 aa)    
Predicted Functional Partners:
grpE
HSP-70 cofactor ; 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 [...] (203 aa)
 
  0.993
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, [...] (376 aa)
 
  0.993
groL
Protein Cpn60 ; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (550 aa)
 
  0.981
Mettu_0730
Serine/threonine protein kinase (448 aa)
     
  0.947
Mettu_1896
Heat shock protein DnaJ domain protein (318 aa)
 
  0.946
htpG
High temperature protein G ; Molecular chaperone. Has ATPase activity (642 aa)
     
  0.944
hrcA
Heat-inducible transcription repressor HrcA ; Negative regulator of class I heat shock genes (grpE- dnaK-dnaJ and groELS operons). Prevents heat-shock induction of these operons (372 aa)
   
   
  0.931
clpB
Chaperone protein 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 (858 aa)
   
 
  0.920
Mettu_0640
ATP-dependent Clp protease, ATP-binding subunit clpA (757 aa)
   
 
  0.920
Mettu_3391
Nitrogen fixation protein NifU ; May be involved in the formation or repair of [Fe-S] clusters present in iron-sulfur proteins (301 aa)
 
 
  0.889
Your Current Organism:
Methylobacter tundripaludum
NCBI taxonomy Id: 697282
Other names: M. tundripaludum, M. tundripaludum SV96, Methylobacter, Methylobacter sp. SV96, Methylobacter tundripaludum, Methylobacter tundripaludum DSM 17260, Methylobacter tundripaludum SV96, Methylobacter tundripaludum Wartiainen et al. 2006, Methylobacter tundripaludum str. SV96, Methylobacter tundripaludum strain SV96
Server load: low (6%) [HD]