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.
Knowledge-based Evidence
from curated databases
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Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
PSHAa2176Putative heat shock protein (Hsp70 family), actin-like ATPase domain; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy. (438 aa)    
Predicted Functional Partners:
grpE
Hsp 24 DnaK nucleotide exchange factor; 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 [...]
  
 0.938
groL
60 kDa chaperonin (Protein Cpn60) (groEL protein); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
  
 0.907
htpG
Chaperone protein htpG; Molecular chaperone. Has ATPase activity.
   
 0.894
groS
10 kDa chaperonin (Protein Cpn10) (groES protein); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
  
 
 0.849
clpB
ATP-dependent protease, Hsp 100, part of multi-chaperone system with DnaK, DnaJ, and GrpE; 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.
  
 
 0.806
clpA
ATP-dependent specificity subunit of clpA-clpP serine protease; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the ClpA/ClpB family.
  
 
 0.806
cbpA
Curved DNA-binding protein, co-chaperone of DnaK (Hsp40 family); Function of strongly homologous gene; molecular chaperone.
  
 0.805
iscU
Fe-S assembly protein; A scaffold on which IscS assembles Fe-S clusters. It is likely that Fe-S cluster coordination is flexible as the role of this complex is to build and then hand off Fe-S clusters.
  
 0.798
dnaJ
Chaperone protein dnaJ (Heat shock protein J) (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. 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. Sever [...]
  
 0.797
PSHAa0110
Putative DnaJ-class molecular chaperone; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; molecular chaperone.
  
 0.774
Your Current Organism:
Pseudoalteromonas haloplanktis
NCBI taxonomy Id: 326442
Other names: P. haloplanktis TAC125, Pseudoalteromonas haloplanktis TAC125, Pseudoalteromonas haloplanktis str. TAC125, Pseudoalteromonas haloplanktis strain TAC125
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