STRINGSTRING
clpS protein (Synechococcus elongatus PCC7942) - STRING interaction network
"clpS" - ATP-dependent Clp protease adapter protein ClpS in Synechococcus elongatus PCC7942
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
clpSATP-dependent Clp protease adapter protein ClpS; Involved in the modulation of the specificity of the ClpAP-mediated ATP-dependent protein degradation (95 aa)    
Predicted Functional Partners:
ABB56721.1
annotation not available (277 aa)
 
        0.919
ABB56292.1
annotation not available (824 aa)
   
 
  0.757
ABB56723.1
annotation not available (114 aa)
              0.578
clpB1
Chaperone protein ClpB 1; 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). Necessary for thermotolerance; Belongs [...] (883 aa)
   
 
  0.577
clpX
ATP-dependent Clp protease ATP-binding subunit ClpX; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP (449 aa)
     
   
  0.544
clpR
Putative ATP-dependent Clp protease proteolytic subunit-like; Has lost the two conserved residues (Ser and His) proposed to be part of the active site. Therefore it could be inactive (228 aa)
     
   
  0.541
clpP3
ATP-dependent Clp protease proteolytic subunit 3; 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 (199 aa)
     
   
  0.538
clpB2
Chaperone protein ClpB 2; 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) (895 aa)
   
 
  0.528
dps
DNA protection during starvation protein; Protects DNA from oxidative damage by sequestering intracellular Fe(2+) ion and storing it in the form of Fe(3+) oxyhydroxide mineral. One hydrogen peroxide oxidizes two Fe(2+) ions, which prevents hydroxyl radical production by the Fenton reaction (By similarity). Dps binds the chromosome non- specifically, forming a highly ordered and stable dps-DNA co- crystal within which chromosomal DNA is condensed and protected from diverse damages. Soluble dps might function in iron homeostasis under high iron concentration, while the dps-DNA complex mi [...] (176 aa)
     
      0.462
ABB56141.1
annotation not available (168 aa)
     
      0.462
Your Current Organism:
Synechococcus elongatus PCC7942
NCBI taxonomy Id: 1140
Other names: Anacystis nidulans R2, S. elongatus PCC 7942, Synechococcus elongatus PCC 7942, Synechococcus elongatus PCC7942, Synechococcus leopoliensis UTEX 2434, Synechococcus leopoliensis strain PCC 7942, Synechococcus sp. IAM M-200, Synechococcus sp. PCC 7942
Server load: low (13%) [HD]