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
AEM78503.1KEGG: tbo:Thebr_0984 PfpI familyintracellular protease; TIGRFAM: Peptidase C56, PfpI; PFAM: ThiJ/PfpI. (168 aa)    
Predicted Functional Partners:
rpsJ
30S ribosomal protein S10; Involved in the binding of tRNA to the ribosomes. Belongs to the universal ribosomal protein uS10 family.
  
 
 0.726
rplN
Ribosomal protein L14; Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome; Belongs to the universal ribosomal protein uL14 family.
   
   0.678
rplE
Ribosomal protein L5; This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; this bridge is implicated in subunit movement. Contacts the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs.
  
 
 0.616
rpsS
Ribosomal protein S19; Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA.
  
   0.610
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 [...]
  
 
 0.607
AEM78504.1
PFAM: HTH transcriptional regulator, LysR; KEGG: tte:TTE0987 transcriptional regulator; Belongs to the LysR transcriptional regulatory family.
 
   
 0.535
rplM
Ribosomal protein L13; This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly.
  
   0.531
AEM78408.1
PFAM: NADH:ubiquinone oxidoreductase, 51kDa subunit; Sucraseferredoxin-like; Soluble ligand binding domain; NADH ubiquinone oxidoreductase, F subunit, iron sulphur binding; 4Fe-4S ferredoxin, iron-sulphur binding, subgroup; KEGG: tbo:Thebr_1492 NADH dehydrogenase (quinone).
  
 
 0.524
AEM78505.1
PFAM: NADH:flavin oxidoreductase/NADH oxidase, N-terminal; FAD-dependent pyridine nucleotide-disulphide oxidoreductase; KEGG: tbo:Thebr_0985 NADH:flavin oxidoreductase/NADH oxidase.
  
 
 0.518
rpsB
Ribosomal protein S2; KEGG: tbo:Thebr_1254 30S ribosomal protein S2; TIGRFAM: Ribosomal protein S2, bacteria/mitochondria/plastid; PFAM: Ribosomal protein S2.
  
   0.510
Your Current Organism:
Thermoanaerobacter wiegelii
NCBI taxonomy Id: 697303
Other names: T. wiegelii Rt8.B1, Thermoanaerobacter wiegelii Rt8.B1, Thermoanaerobacter wiegelii str. Rt8.B1, Thermoanaerobacter wiegelii strain Rt8.B1
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.