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
clpPClp protease ClpP; 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. (225 aa)    
Predicted Functional Partners:
clpX
Clp protease ATP-binding protein; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP.
 0.999
clpA
Clp protease ClpX; ATPase and specificity subunit of the ClpA-ClpP ATP dependent serine protease; directs protease to specific substrates; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the ClpA/ClpB family.
 
 
 0.973
KKB64575.1
ATPase AAA; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the ClpA/ClpB family.
 
 
 0.972
clpB
Protein disaggregation chaperone; 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.
 
 
 0.972
KKB65340.1
ATPase AAA; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the ClpA/ClpB family.
 
 
 0.971
KKB62800.1
ATPase AAA; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the ClpA/ClpB family.
 
 
 0.971
groS
Molecular chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
 
 
 0.925
clpS
Clp protease ClpS; Involved in the modulation of the specificity of the ClpAP- mediated ATP-dependent protein degradation; Belongs to the ClpS family.
   
 
 0.902
hrcA
HrcA family transcriptional regulator; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons.
   
  
 0.883
grpE
Heat shock 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- [...]
  
 
 0.858
Your Current Organism:
Robbsia andropogonis
NCBI taxonomy Id: 28092
Other names: ATCC 19311 [[Pseudomonas woodsii]], ATCC 23061, Aplanobacter stizolobii, Bacterium andropogoni, Bacterium woodsii, Burkholderia andropogonis, CCUG 32772, CFBP 2421, CIP 105771, DSM 9511, DSM 9884 [[Pseudomonas woodsii]], IBSBF 199, ICMP 2807, ICMP 3967 [[Pseudomonas woodsii]], JCM 10487, LMG 2129, LMG 2362 [[Pseudomonas woodsii]], LMG:2129, LMG:2362 [[Pseudomonas woodsii]], NCPPB 934, NCPPB 968 [[Pseudomonas woodsii]], NRRL B-14296, Paraburkholderia andropogonis, Pseudomonas andropogonis, Pseudomonas stizolobii, Pseudomonas woodsii, R. andropogonis, strain PW 102 [[Pseudomonas woodsii]]
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