STRINGSTRING
trx-1 protein (Pseudomonas aeruginosa) - STRING interaction network
"trx-1" - Thioredoxin: thioredoxin in Pseudomonas aeruginosa
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
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proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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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 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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[Homology]
Score
trx-1Thioredoxin- thioredoxin (289 aa)    
Predicted Functional Partners:
gltB
annotation not available (1481 aa)
     
      0.919
trxB3
TRX_reduct- thioredoxin-disulfide reductase; Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family (316 aa)
 
 
  0.895
trxB1
TRX_reduct- thioredoxin-disulfide reductase; Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family (316 aa)
 
 
  0.893
grpE
Protein 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- dependent [...] (186 aa)
 
   
  0.794
dsbD1
Thiol-disulfide interchange protein DsbD; Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm. This transfer involves a cascade of disulfide bond formation and reduction steps (591 aa)
         
  0.784
dnaK
Chaperone protein DnaK; Acts as a chaperone (637 aa)
 
 
  0.780
hslU
ATP-dependent protease 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 (447 aa)
   
 
  0.776
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 [...] (377 aa)
 
 
  0.763
DR97_3808
annotation not available (220 aa)
              0.744
ribD
Riboflavin biosynthesis protein RibD; Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5’-phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)- pyrimidinedione 5’-phosphate; In the C-terminal section; belongs to the HTP reductase family (373 aa)
   
   
  0.714
Your Current Organism:
Pseudomonas aeruginosa
NCBI taxonomy Id: 287
Other names: ATCC 10145, ATCC 10145-U, Bacillus aeruginosus, Bacillus pyocyaneus, Bacterium aeruginosum, Bacterium pyocyaneum, CCEB 481, CCUG 28447, CCUG 29297, CCUG 551, CFBP 2466, CIP 100720, DSM 50071, IBCS 277, IFO 12689, JCM 5962, Micrococcus pyocyaneus, NBRC 12689, NCCB 76039, NCIB 8295, NCIMB 8295, NCTC 10332, NRRL B-771, P. aeruginosa, Pseudomonas aeruginosa, Pseudomonas polycolor, Pseudomonas pyocyanea, Pseudomonas sp. RV3, RH 815, VKM B-588, bacterium ASFP-37, bacterium ASFP-38, bacterium ASFP-45, bacterium ASFP-46, bacterium ASFP-48
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