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
hscAChaperone protein HscA; Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB. (617 aa)    
Predicted Functional Partners:
dnaJ_1
Molecular chaperone DnaJ; Chaperone Hsp40; co-chaperone with DnaK; 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; Derived by automated computational analysis using gene prediction method: Protein Homology.
 0.981
fdx2
2Fe-2S ferredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.943
htpG_1
Heat shock protein 90; Molecular chaperone. Has ATPase activity.
   
 0.932
grpE_2
Molecular chaperone GrpE; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.921
hscB
J-type co-chaperone that regulates the ATPase and peptide-binding activity of Hsc66 chaperone; may function in biogenesis of iron-sulfur proteins; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the HscB family.
 
 
 0.908
iscU
Scaffolding protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.898
clpB_2
Protein disaggregation chaperone; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.892
iscX
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.891
groEL
Molecular chaperone GroEL; 60 kDa chaperone family; promotes refolding of misfolded polypeptides especially under stressful conditions; forms two stacked rings of heptamers to form a barrel-shaped 14mer; ends can be capped by GroES; misfolded proteins enter the barrel where they are refolded when GroES binds; many bacteria have multiple copies of the groEL gene which are active under different environmental conditions; the B.japonicum protein in this cluster is expressed constitutively; in Rhodobacter, Corynebacterium and Rhizobium this protein is essential for growth; Derived by autom [...]
 
 0.840
iscA
Iron-sulfur cluster assembly protein; Is able to transfer iron-sulfur clusters to apo-ferredoxin. Multiple cycles of [2Fe2S] cluster formation and transfer are observed, suggesting that IscA acts catalytically. Recruits intracellular free iron so as to provide iron for the assembly of transient iron-sulfur cluster in IscU in the presence of IscS, L-cysteine and the thioredoxin reductase system; Belongs to the HesB/IscA family.
 
 
 0.776
Your Current Organism:
Actinobacillus equuli
NCBI taxonomy Id: 202947
Other names: A. equuli subsp. equuli, Actinobacillus equuli subsp. equuli
Server load: low (28%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.