STRINGSTRING
trxA protein (Bacillus cereus) - STRING interaction network
"trxA" - Thioredoxin: thioredoxin in Bacillus cereus
Nodes:
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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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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:
some 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 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
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
trxAThioredoxin- thioredoxin; Belongs to the thioredoxin family (104 aa)    
Predicted Functional Partners:
trxB
TRX_reduct- thioredoxin-disulfide reductase; Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family (318 aa)
 
  0.985
gltA_1
annotation not available (1478 aa)
     
      0.978
ytpP_1
annotation not available (104 aa)
         
  0.809
folD
Bifunctional protein FolD; Catalyzes the oxidation of 5,10- methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10- formyltetrahydrofolate (286 aa)
   
 
 
  0.797
dnaK
Chaperone protein DnaK; Acts as a chaperone (611 aa)
 
 
  0.789
etfB
annotation not available (257 aa)
     
 
  0.780
arsC
Arsenate reductase; Catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)] (134 aa)
   
 
  0.744
uvrC
UvrABC system protein C; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5’ and 3’ sides of the lesion. The N-terminal half is responsible for the 3’ incision and the C-terminal half is responsible for the 5’ incision (594 aa)
         
  0.718
groL
60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions; Belongs to the chaperonin (HSP60) family (544 aa)
 
 
  0.707
yumC
annotation not available (329 aa)
 
 
  0.697
Your Current Organism:
Bacillus cereus
NCBI taxonomy Id: 1396
Other names: ATCC 14579, B. cereus, BCRC 10603, Bacillus cereus, Bacillus endorhythmos, Bacillus medusa, Bacillus sp. 2479, Bacillus sp. BS2(2013b), Bacillus sp. BV4, Bacillus sp. JKR50, Bacillus sp. JKR62, Bacillus sp. JP44SK22, Bacillus sp. JP44SK37, Bacillus sp. JP44SK43, Bacillus sp. JP44SK45, Bacillus sp. JSG1(2014), Bacillus sp. KER 17, Bacillus sp. MZ-01, Bacillus sp. PXDK-1, Bacillus sp. Pf-1, Bacillus sp. V3, Bacillus sp. mmm86, CCM 2010, CCRC 10603, CCUG 7414, CIP 66.24, DSM 31, IAM 12605, IFO 15305, JCM 2152, LMG 6923, NBRC 15305, NCCB 75008, NCIMB 9373, NCTC 2599, NRRL B-3711, VKM B-504
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