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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
Deba_3228Heat shock protein Hsp20; COGs: COG0071 Molecular chaperone (small heat shock protein); InterPro IPR008978:IPR002068; KEGG: afr:AFE_2086 heat shock protein, HSP20 family; PFAM: heat shock protein Hsp20; SPTR: B7J4U6 Heat shock protein, Hsp20 family; PFAM: Hsp20/alpha crystallin family; Belongs to the small heat shock protein (HSP20) family. (126 aa)    
Predicted Functional Partners:
clpB
ATP-dependent chaperone ClpB; 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.
 
 
 0.860
lon-3
ATP-dependent protease La; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner.
  
  
 0.794
Deba_2571
ATP-binding region ATPase domain protein; InterPro IPR003594; KEGG: sfu:Sfum_3853 hypothetical protein; PFAM: ATP-binding region ATPase domain protein; SPTR: A0LQ20 Putative uncharacterized protein; PFAM: Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase.
  
 
 0.659
grpE
GrpE protein; 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-dependent i [...]
  
  
 0.575
dnaK
Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
  
 
 0.559
dnaK-2
Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
  
 
 0.559
Deba_3031
KEGG: gvi:glr2966 hypothetical protein; SPTR: Q7NCL2 Glr2966 protein.
  
 
 0.558
hslV
20S proteasome A and B subunits; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
   
  
 0.542
Deba_2147
Transcriptional regulator, LuxR family; InterPro IPR016032:IPR000792:IPR011991; KEGG: sfu:Sfum_0947 two component LuxR family transcriptional regulator; PFAM: regulatory protein LuxR; SMART: regulatory protein LuxR; SPTR: A0LGU1 Two component transcriptional regulator, LuxR family; PFAM: Bacterial regulatory proteins, luxR family.
    
 
 0.541
hslU
Heat shock protein HslVU, ATPase subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis.
   
  
 0.505
Your Current Organism:
Desulfarculus baarsii
NCBI taxonomy Id: 644282
Other names: D. baarsii DSM 2075, Desulfarculus baarsii 2st 14, Desulfarculus baarsii DSM 2075, Desulfarculus baarsii str. DSM 2075, Desulfarculus baarsii strain DSM 2075
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