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:
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Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
clpS-2ATP-dependent Clp protease adaptor protein ClpS; Involved in the modulation of the specificity of the ClpAP- mediated ATP-dependent protein degradation; Belongs to the ClpS family. (103 aa)    
Predicted Functional Partners:
clpA
ATP-dependent Clp protease, ATP-binding subunit; Belongs to the ClpA/ClpB family.
 
 
 0.934
aat
leucyl/phenylalanyl-tRNA-protein transferase; Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl- tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine.
 
  
 0.718
clpB
ATP-dependent Clp protease, ATP-binding subunit; 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. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Belongs to the [...]
  
 
 0.685
clpB-2
ATP-dependent Clp protease, ATP-binding subunit; Belongs to the ClpA/ClpB family.
  
 
 0.685
dps
DNA oxidation protective protein, not DNA-binding; Protects DNA from oxidative damage by sequestering intracellular Fe(2+) ion and storing it in the form of Fe(3+) oxyhydroxide mineral, which can be released after reduction. It efficiently inhibits hydroxyl radical production by the Fenton reaction. Does not bind DNA.
   
 
 0.673
Atu4777
Conserved hypothetical protein; Belongs to the Dps family.
   
 
 0.673
clpX
ATP-dependent Clp protease, ATP-binding subunit; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP.
   
  
 0.594
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.
   
 
 0.550
clpP-2
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.
   
 
 0.550
ftsH
Metalloprotease; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family.
     
 0.530
Your Current Organism:
Agrobacterium fabrum
NCBI taxonomy Id: 176299
Other names: A. fabrum str. C58, Agrobacterium fabrum str. C58, Agrobacterium tumefaciens (strain C58 / ATCC 33970), Agrobacterium tumefaciens (strain C58), Agrobacterium tumefaciens str. C58, Agrobacterium tumefaciens str. C58 (Cereon), Agrobacterium tumefaciens str. C58 (Dupont), Agrobacterium tumefaciens str. C58 (U. Washington), Rhizobium radiobacter str. C58 (Cereon), Rhizobium radiobacter str. C58 (Dupont), Rhizobium radiobacter str. C58 (U. Washington)
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