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
yfjQPutative divalent cation transport protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative transporter. (319 aa)    
Predicted Functional Partners:
yloB
P-type calcium transport ATPase; This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of calcium.
  
  
 0.932
mgtE
Magnesium transporter; Acts as a magnesium transporter.
  
  
 0.810
rsbV
Anti-anti-sigma factor (antagonist of RsbW); Positive regulator of sigma-B activity. Non-phosphorylated RsbV binds to RsbW, preventing its association with sigma-B. When phosphorylated, releases RsbW, which is then free to complex with and inactivate sigma-B.
  
    0.662
sigF
RNA polymerase sporulation-specific sigma factor (sigma-F); Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is responsible for the expression of sporulation specific genes. Interaction with SpoIIAB inhibits sigma-F activity throughout the cell before the formation of the asymmetric septum; after septation the interaction is confined to the mother cell, and sigma F activity is released in the prespore. Responsible for expression of csfB (the anti-sigma-G factor Gin).
  
    0.591
yfjP
Putative DNA-modified purine glycosidase; Hydrolysis of the deoxyribose N-glycosidic bond to excise 3- methyladenine, 3-methylguanine, 7-methylguanine, O2-methylthymine, and O2-methylcytosine from the damaged DNA polymer formed by alkylation lesions; Belongs to the alkylbase DNA glycosidase AlkA family.
       0.557
yqxL
Putative CorA-type Mg(2+) transporter; Mediates influx of magnesium ions. Alternates between open and closed states. Activated by low cytoplasmic Mg(2+) levels. Inactive when cytoplasmic Mg(2+) levels are high. May also mediate uptake of Co(2+).
  
   
0.555
ysnF
Putative stress response protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; phenotype.
  
    0.546
yfjR
Putative beta-hydroxyacid dehydrogenase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the HIBADH-related family.
       0.535
yfkM
General stress protein 18; Functions in the protection against aldehyde-stress, possibly by degrading damaged proteins.
  
  
 0.511
rsbW
Switch protein/serine kinase and anti-sigma factor (inhibitory sigma-B binding protein); 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).
  
    0.482
Your Current Organism:
Bacillus subtilis 168
NCBI taxonomy Id: 224308
Other names: B. subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis 168, Bacillus subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis str. BGSC 1A700
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