• Version:
  • 11.0 (preview - - version 10.5 still available here)
STRINGSTRING
Mettu_0640 protein (Methylobacter tundripaludum) - STRING interaction network
"Mettu_0640" - TIGRFAM: ATP-dependent Clp protease ATP-binding subunit clpA 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_0640TIGRFAM- ATP-dependent Clp protease ATP-binding subunit clpA; PFAM- ATPase associated with various cellular activities, AAA-2; ATPase, AAA-type, core; Clp, N-terminal; Clp ATPase, C-terminal; KEGG- mca-MCA1789 ATP-dependent Clp protease, ATP-binding subunit ClpA; SMART- ATPase, AAA+ type, core; Belongs to the ClpA/ClpB family (757 aa)    
Predicted Functional Partners:
clpS
ATP-dependent Clp protease adapter protein ClpS; Involved in the modulation of the specificity of the ClpAP-mediated ATP-dependent protein degradation (107 aa)
 
  0.998
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)
   
 
  0.919
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)
   
 
  0.907
dnaK
Chaperone protein DnaK; Acts as a chaperone (644 aa)
 
 
  0.879
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 [...] (376 aa)
   
  0.847
Mettu_3149
KEGG- aas-Aasi_0854 hypothetical protein; PFAM- Heat shock protein DnaJ, N-terminal; Sel1-like; SMART- Heat shock protein DnaJ, N-terminal; Sel1-like (362 aa)
 
  0.841
Mettu_1170
KEGG- hch-HCH_05817 serine/threonine protein kinase; PFAM- Serine/threonine-protein kinase-like domain; SMART- Serine/threonine-protein kinase domain; Protein phosphatase 2C-related; Tyrosine-protein kinase, subgroup, catalytic domain (578 aa)
   
  0.833
Mettu_3601
Heat shock protein 70; KEGG- sli-Slin_1429 DnaK-type molecular chaperone DnaK; manually curated; PFAM- Heat shock protein 70 (432 aa)
 
 
  0.826
Mettu_1896
KEGG- noc-Noc_1382 heat shock protein DnaJ-like; PFAM- Heat shock protein DnaJ, N-terminal; Chaperone DnaJ, C-terminal; SMART- Heat shock protein DnaJ, N-terminal (318 aa)
 
  0.821
Mettu_3413
KEGG- hiq-CGSHiGG_00130 Sel1 domain-containing protein; PFAM- Heat shock protein DnaJ, N-terminal; Sel1-like; SMART- Heat shock protein DnaJ, N-terminal; Sel1-like (222 aa)
   
  0.820
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
Server load: low (8%) [HD]