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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
KML36870.1Anti-sigma-factor antagonist; Derived by automated computational analysis using gene prediction method: Protein Homology. (280 aa)    
Predicted Functional Partners:
KML44215.1
Serine/threonine protein kinase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.942
KML44220.1
Phosphoserine phosphatase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.924
KML43753.1
Flagellar motor switch protein FliN; FliN is one of three proteins (FliG, FliN, FliM) that form the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation. Belongs to the FliN/MopA/SpaO family.
  
   0.870
rsbW
Serine/threonine protein kinase; Negative regulator of sigma-B activity. Phosphorylates and inactivates its specific antagonist protein, RsbV. Upon phosphorylation of RsbV, RsbW is released and binds to sigma-B, thereby blocking its ability to form an RNA polymerase holoenzyme (E-sigma-B).
 
 0.810
KML44216.1
Phosphoserine phosphatase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.784
spoIIAB
Anti-sigma F factor; Binds to sigma F and blocks its ability to form an RNA polymerase holoenzyme (E-sigma F). Phosphorylates SpoIIAA on a serine residue. This phosphorylation may enable SpoIIAA to act as an anti- anti-sigma factor that counteracts SpoIIAB and thus releases sigma F from inhibition.
  
 0.754
KML44845.1
Diguanylate cyclase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.753
KML41311.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.713
KML39752.1
Chemotaxis protein CheV; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.713
KML44553.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.693
Your Current Organism:
Bacillus firmus
NCBI taxonomy Id: 1399
Other names: ATCC 14575, B. firmus, BCRC 11730, Bacillaceae bacterium HQ2, Bacillus sp. JP44SK20, Bacillus sp. LK28, Bacillus sp. NCIM 2264, Bacillus sp. NCIM 2462, CCM 2213, CCRC 11730, CCRC:11730, CCUG 7418, CIP 52.70, DSM 12, IAM 12464, IFO 15306, JCM 2512, LMG 7125, LMG:7125, NBRC 15306, NCAIM B.01087, NCCB 48015, NCIB 9366, NCIMB 9366, NCTC 10335, NRRL B-14307, NRRL NRS-613, VKM B-498
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