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groL protein (Methylobacter tundripaludum) - STRING interaction network
"groL" - 60 kDa chaperonin in Methylobacter tundripaludum
Nodes:
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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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
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[Homology]
Score
groL60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (550 aa)    
Predicted Functional Partners:
groS
10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter (95 aa)
 
  0.999
dnaK
Chaperone protein DnaK; Acts as a chaperone (644 aa)
 
  0.991
htpG
Chaperone protein HtpG; Molecular chaperone. Has ATPase activity (642 aa)
   
 
  0.976
grpE
Protein 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- dependent [...] (203 aa)
 
  0.970
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; Belongs to the ClpA/ClpB family (858 aa)
   
 
  0.950
Mettu_3601
Heat shock protein 70; KEGG- sli-Slin_1429 DnaK-type molecular chaperone DnaK; manually curated; PFAM- Heat shock protein 70 (432 aa)
   
  0.906
clpP
ATP-dependent Clp protease proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins; Belongs to the peptidase S14 family (215 aa)
 
 
  0.902
Mettu_0730
KEGG- svo-SVI_3119 serine/threonine protein kinase; PFAM- Serine/threonine-protein kinase-like domain; Leucine-rich repeat; SMART- Serine/threonine-protein kinase domain; Tyrosine-protein kinase, subgroup, catalytic domain; Leucine-rich repeat, typical subtype (448 aa)
       
  0.901
rpoH
RNA polymerase sigma factor RpoH; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is involved in regulation of expression of heat shock genes (285 aa)
   
 
  0.901
Mettu_3235
KEGG- mca-MCA1305 DnaK-related protein; Belongs to the heat shock protein 70 family (646 aa)
   
  0.897
Your Current Organism:
Methylobacter tundripaludum
NCBI taxonomy Id: 697282
Other names: M. tundripaludum SV96, Methylobacter sp. SV96, Methylobacter tundripaludum, Methylobacter tundripaludum DSM 17260, Methylobacter tundripaludum SV96, Methylobacter tundripaludum str. SV96, Methylobacter tundripaludum strain SV96
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