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
Smed_3045TIGRFAM: thioredoxin; PFAM: Thioredoxin domain; KEGG: sme:SMc03801 putative thioredoxin protein. (330 aa)    
Predicted Functional Partners:
Smed_1571
Glutathione-disulfide reductase; Maintains high levels of reduced glutathione.
  
 
 0.908
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.
  
 
 0.793
hslV
20S proteasome A and B subunits; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
  
  
 0.792
grpE
Ribulose-phosphate 3-epimerase; 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 [...]
  
  
 0.769
Smed_3215
PFAM: FxsA cytoplasmic membrane protein; KEGG: sme:SMc02787 hypothetical transmembrane protein.
   
    0.701
Smed_3046
PFAM: peptidase S16 lon domain protein; KEGG: sme:SMc03802 hypothetical protein.
 
  
 0.639
Smed_3044
PFAM: YbaK/prolyl-tRNA synthetase associated region; KEGG: sme:SMc03800 hypothetical protein.
       0.638
Smed_1619
PFAM: heat shock protein DnaJ domain protein; KEGG: sme:SMc04233 hypothetical DnaJ domain protein.
  
 
 0.603
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 [...]
  
 
 0.603
lon
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.
  
  
 0.581
Your Current Organism:
Sinorhizobium medicae
NCBI taxonomy Id: 366394
Other names: Ensifer medicae WSM419, S. medicae WSM419, Sinorhizobium medicae WSM419
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