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
sigI8RNA polymerase, sigma 28 subunit, FliA/WhiG subfamily; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released; Belongs to the sigma-70 factor family. SigI subfamily. (254 aa)    
Predicted Functional Partners:
rsgI8
Hypothetical protein; Anti-sigma factor for SigI8. Negatively regulates SigI8 activity through direct interaction.
 
    0.938
rsgI7
Hypothetical protein; Anti-sigma factor for SigI7. Negatively regulates SigI7 activity through direct interaction.
 
  
 0.855
rsgI1
Type 3a cellulose-binding domain protein; Anti-sigma factor for SigI1. Negatively regulates SigI1 activity through direct interaction. Binding of the polysaccharide substrate to the extracellular C-terminal sensing domain of RsgI1 may induce a conformational change in its N-terminal cytoplasmic region, leading to the release and activation of SigI1 (Probable).
 
  
 0.836
rsgI4
Type 3a cellulose-binding domain protein; Anti-sigma factor for SigI4. Negatively regulates SigI4 activity through direct interaction. Binding of the polysaccharide substrate to the extracellular C-terminal sensing domain of RsgI4 may induce a conformational change in its N-terminal cytoplasmic region, leading to the release and activation of SigI4.
 
  
 0.812
rsgI5
alpha-L-arabinofuranosidase B; Anti-sigma factor for SigI5. Negatively regulates SigI5 activity through direct interaction. Binding of the polysaccharide substrate to the extracellular C-terminal sensing domain of RsgI5 may induce a conformational change in its N-terminal cytoplasmic region, leading to the release and activation of SigI5.
  
  
 0.793
Cthe_2246
KEGG: cce:Ccel_0092 anti-sigma-28 factor FlgM family protein; TIGRFAM: Anti-sigma-28 factor FlgM family protein; PFAM: Anti-sigma-28 factor FlgM family protein.
  
 
 0.792
rsgI3
PA14 domain protein; Anti-sigma factor for SigI3. Negatively regulates SigI3 activity through direct interaction. Binding of the polysaccharide substrate to the extracellular C-terminal sensing domain of RsgI3 may induce a conformational change in its N-terminal cytoplasmic region, leading to the release and activation of SigI3.
  
  
 0.661
rsgI2
Type 3a cellulose-binding domain protein; Anti-sigma factor for SigI2. Negatively regulates SigI2 activity through direct interaction. Binding of the polysaccharide substrate to the extracellular C-terminal sensing domain of RsgI2 may induce a conformational change in its N-terminal cytoplasmic region, leading to the release and activation of SigI2.
 
  
 0.652
rpoB
DNA-directed RNA polymerase, beta subunit; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
    
 
 0.649
rpoC
DNA-directed RNA polymerase, beta' subunit; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
    
 
 0.628
Your Current Organism:
Hungateiclostridium thermocellum
NCBI taxonomy Id: 203119
Other names: Clostridium thermocellum ATCC 27405, H. thermocellum ATCC 27405, Hungateiclostridium thermocellum ATCC 27405, Ruminiclostridium thermocellum ATCC 27405
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