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
SDK08451.1Thioredoxin. (185 aa)    
Predicted Functional Partners:
msrA
Peptide methionine sulfoxide reductase msrA/msrB; Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
   
 0.982
msrA-3
Peptide-methionine (S)-S-oxide reductase; Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
   
 0.982
SDJ72239.1
Flagellar motor switch protein FliN/FliY.
    
   0.898
SDJ74959.1
Cytochrome c oxidase subunit 2; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).
   
 
 0.889
SDJ75620.1
Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin).
  
 0.869
SDK16506.1
Cytochrome c oxidase subunit 2; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).
   
 
 0.848
SDJ75774.1
Protein SCO1/2.
 
 
 0.826
SDJ65120.1
Dihydrolipoamide dehydrogenase.
   
 0.739
SDJ75338.1
Dihydrolipoamide dehydrogenase.
   
 0.739
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, [...]
    
 0.706
Your Current Organism:
Sediminibacillus albus
NCBI taxonomy Id: 407036
Other names: CGMCC 1.6502, DSM 19340, S. albus, Sediminibacillus albus Wang et al. 2009, Virgibacillus sp. NHBX5, strain NHBX5
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