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:
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Gene Fusion
Cooccurrence
Coexpression
Experiments
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[Homology]
Score
groLChaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (543 aa)    
Predicted Functional Partners:
groS
Chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
 
 0.999
dnaK
Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
 
 
 0.969
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 [...]
  
 0.948
htpG
Molecular chaperone HtpG; Molecular chaperone. Has ATPase activity.
   
 
 0.893
SMB90765.1
InterPro IPR001268; COGs: COG3261 Ni Fe-hydrogenase III large subunit; KEGG: nam:NAMH_0750 hydrogenase-3, subunit E; SPTR: Q0W2B9 Hydrogenase, large subunit-like protein (HycE-like); PFAM: NADH dehydrogenase (ubiquinone) 30 kDa subunit.
    
 
 0.880
SMB82225.1
Flagellar motor switch protein FliN/FliY; InterPro IPR001172:IPR001543:IPR007597:IPR012826; COGs: COG1776 Chemotaxis protein CheC inhibitor of MCP methylation; KEGG: sde:Sde_2174 surface presentation of antigens (SpoA) protein; SPTR: A2U857 CheC, inhibitor of MCP methylation; PFAM: surface presentation of antigens (SPOA) protein; CheC domain protein; TIGRFAM: flagellar motor switch protein FliN.
    
 
 0.860
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, [...]
 
 0.859
SMB95650.1
Thioredoxin; InterPro IPR006662:IPR013766:IPR017937:IPR005746; COGs: COG3118 Thioredoxin domain-containing protein; KEGG: sat:SYN_00045 thioredoxin; SPTR: P0A0K5 Thioredoxin; PFAM: Thioredoxin domain; TIGRFAM: thioredoxin; Belongs to the thioredoxin family.
  
 
 0.775
guaB
Inosine-5'-monophosphate dehydrogenase; Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. Belongs to the IMPDH/GMPR family.
  
 0.766
nnrE
NAD(P)H-hydrate epimerase; Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of bot [...]
  
   0.753
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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