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
ANQ23164.1RNA polymerase subunit sigma; Bacteria have multiple sigma factors which are active under specific conditions; the sigma factor binds with the catalytic core of RNA polymerase to produce the holoenzyme and directs bacterial core RNA polymerase to specific promoter elements to initiate transcription; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the sigma-70 factor family. ECF subfamily. (194 aa)    
Predicted Functional Partners:
ANQ22416.1
Transcriptional regulator; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.981
ANQ22608.1
Anti-sigma E factor; An anti-sigma factor for extracytoplasmic function (ECF) sigma factor sigma-E (RpoE). ECF sigma factors are held in an inactive form by an anti-sigma factor until released by regulated intramembrane proteolysis (RIP). RIP occurs when an extracytoplasmic signal triggers a concerted proteolytic cascade to transmit information and elicit cellular responses. The membrane-spanning regulatory substrate protein is first cut periplasmically (site-1 protease, S1P, DegS), then within the membrane itself (site-2 protease, S2P, RseP), while cytoplasmic proteases finish degradi [...]
 
 
 0.911
ANQ22417.1
2-dehydropantoate 2-reductase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 
 0.746
rpoC
DNA-directed RNA polymerase subunit beta; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
    
 
 0.731
rpoB
DNA-directed RNA polymerase subunit beta; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
    
 
 0.725
ANQ22418.1
ATP-dependent protease; Derived by automated computational analysis using gene prediction method: Protein Homology.
     
 0.702
ANQ22239.1
RNA polymerase subunit sigma; Bacteria have multiple sigma factors which are active under specific conditions; the sigma factor binds with the catalytic core of RNA polymerase to produce the holoenzyme and directs bacterial core RNA polymerase to specific promoter elements to initiate transcription; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the sigma-70 factor family. ECF subfamily.
  
   
 0.695
ANQ20877.1
Chemotaxis protein CheR; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
   0.685
rpoA
DNA-directed RNA polymerase subunit alpha; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
  
 
 
 0.557
rpoZ
DNA-directed RNA polymerase subunit omega; Promotes RNA polymerase assembly. Latches the N- and C- terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits.
    
 
 0.497
Your Current Organism:
Vibrio natriegens
NCBI taxonomy Id: 691
Other names: ATCC 14048, Beneckea natriegens, CAIM 12, CCUG 16371, CCUG 4980 A, CIP 103193, DSM 759, IFO 15636, LMG 10935, LMG:10935, NBRC 15636, NCCB 73019, NCMB 857, NCMB:857, NCTC 11319, Pseudomonas natriegens, V. natriegens
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