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
ADO50480.1Thioredoxin; KEGG: kva:Kvar_4946 thioredoxin; TIGRFAM: thioredoxin; PFAM: Thioredoxin domain-containing protein; Belongs to the thioredoxin family. (109 aa)    
Predicted Functional Partners:
ADO49149.1
KEGG: ecv:APECO1_1201 thioredoxin reductase; TIGRFAM: thioredoxin reductase; PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase.
 
 0.985
ADO49013.1
Delta-1-pyrroline-5-carboxylate dehydrogenase; Oxidizes proline to glutamate for use as a carbon and nitrogen source; Belongs to the aldehyde dehydrogenase family. In the N-terminal section; belongs to the proline dehydrogenase family.
    
 
 0.720
cysH
Phosphoadenosine phosphosulfate reductase; Reduction of activated sulfate into sulfite. Belongs to the PAPS reductase family. CysH subfamily.
    
 
 0.666
rho
Transcription termination factor Rho; Facilitates transcription termination by a mechanism that involves Rho binding to the nascent RNA, activation of Rho's RNA- dependent ATPase activity, and release of the mRNA from the DNA template.
  
  
 0.618
ADO47889.1
KEGG: enc:ECL_03384 tyrosine phosphatase; PFAM: Protein-tyrosine phosphatase, low molecular weight; SMART: Protein-tyrosine phosphatase, low molecular weight.
  
 
 0.602
gppA
Ppx/GppA phosphatase; Catalyzes the conversion of pppGpp to ppGpp. Guanosine pentaphosphate (pppGpp) is a cytoplasmic signaling molecule which together with ppGpp controls the 'stringent response', an adaptive process that allows bacteria to respond to amino acid starvation, resulting in the coordinated regulation of numerous cellular activities.
       0.585
dnaJ
Chaperone protein 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, D [...]
 
 
 0.564
ADO46924.1
Protein-disulfide reductase; KEGG: kpu:KP1_4621 copper-sensitivity suppressor protein B.
   
 
 0.559
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.
  
 
 0.559
ADO46763.1
KEGG: kpu:KP1_4936 glutamate synthase subunit alpha; PFAM: ferredoxin-dependent glutamate synthase; glutamine amidotransferase class-II; glutamate synthase; glutamate synthase alpha subunit domain protein.
   
 
 0.555
Your Current Organism:
Enterobacter lignolyticus
NCBI taxonomy Id: 701347
Other names: Enterobacter lignolyticus SCF1, [. lignolyticus SCF1, [Enterobacter] lignolyticus SCF1
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