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
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Gene Fusion
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[Homology]
Score
hslOMolecular chaperone Hsp33; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. (296 aa)    
Predicted Functional Partners:
SMB86431.1
Ribosomal 50S subunit-recycling heat shock protein, contains S4 domain; InterPro IPR002942; COGs: COG1188 Ribosome-associated heat shock protein implicated in the recycling of the 50S subunit (S4 paralog); SPTR: Q9KGI8 Uncharacterized protein BH0073; SMART: RNA-binding S4 domain protein; PFAM: RNA-binding S4 domain protein; KEGG: afr:AFE_0164 S4 domain protein.
 
  
 0.847
grpE
Molecular chaperone GrpE; 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 [...]
   
  
 0.727
hslU
ATP-dependent HslUV protease ATP-binding 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.
   
  
 0.688
hslV
ATP dependent peptidase CodWX, CodW component. Threonine peptidase. MEROPS family T01B; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
  
  
 0.661
dnaJ
Molecular chaperone DnaJ; 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. Several rounds of ATP-dependent interactions between DnaJ, [...]
  
  
 0.638
msrA
Peptide methionine sulfoxide reductase msrA/msrB; Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
     
 0.623
SMB93455.1
Riboflavin transporter FmnP; Mediates riboflavin uptake, may also transport FMN and roseoflavin. Probably a riboflavin-binding protein that interacts with the energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates. The substrates themselves are bound by transmembrane, not extracytoplasmic soluble proteins; Belongs to the prokaryotic riboflavin transporter (P-RFT) (TC 2.A.87) family.
 
     0.576
SMB90879.1
Chaperonin GroEL (HSP60 family); InterPro IPR017998:IPR001844:IPR002423:IPR002194; COGs: COG0459 Chaperonin GroEL (HSP60 family); KEGG: t-complex protein 1, gamma subunit, putative; K09495 T-complex protein 1 subunit gamma; SPTR: A1HR08 Chaperonin Cpn60/TCP-1; PFAM: chaperonin Cpn60/TCP-1.
   
  
 0.563
groL
Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
   
  
 0.563
SMB93303.1
InterPro IPR008616:IPR008532:IPR006025; COGs: COG1293 RNA-binding protein homologous to eukaryotic snRNP; KEGG: pca:Pcar_1454 RNA-binding protein; SPTR: A2UB94 Fibronectin-binding A-like; PFAM: Fibronectin-binding A domain protein; protein of unknown function DUF814.
 
     0.531
Your Current Organism:
Desulfonispora thiosulfatigenes
NCBI taxonomy Id: 656914
Other names: D. thiosulfatigenes DSM 11270, Desulfonispora thiosulfatigenes DSM 11270, Desulfonispora thiosulfatigenes str. DSM 11270, Desulfonispora thiosulfatigenes strain DSM 11270
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