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
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[Homology]
Score
ktrAPotassium uptake protein; Catalytic subunit of the KtrAB potassium uptake transporter. The 2 major potassium transporter complexes KtrAB and KtrCD confer resistance to both suddenly imposed and prolonged osmotic stress. (222 aa)    
Predicted Functional Partners:
ktrB
Potassium transporter ATPase; Integral membrane subunit of the KtrAB potassium uptake transporter. The 2 major potassium transporter complexes KtrAB and KtrCD confer resistance to both suddenly imposed and prolonged osmotic stress.
 
 0.999
ktrD
K+-transporting ATPase; Integral membrane subunit of the KtrCD potassium uptake transporter. The 2 major potassium transporter complexes KtrAB and KtrCD confer resistance to both suddenly imposed and prolonged osmotic stress; Belongs to the TrkH potassium transport family. Ktr (TC 2.A.38.4) subfamily.
 
 0.991
ydaO
Putative metabolite transporter; High-affinity potassium transporter.
  
  
 0.961
carA
Arginine-specific carbamoyl-phosphate synthetase (small subunit); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme.
      
 0.938
pstA
Phosphate ABC transporter (permease); Part of the binding-protein-dependent transport system YqgGHIJK. Probably responsible for the translocation of the substrate across the membrane (By similarity); Belongs to the binding-protein-dependent transport system permease family. CysTW subfamily.
     
 0.923
yaaQ
Conserved hypothetical protein; Binds cyclic di-AMP (c-di-AMP) and is probably involved in c- di-AMP-mediated signaling pathways. In vitro, can also bind cyclic GMP- AMP (3'3'-cGAMP), with lower affinity, but not c-di-GMP or 2'3'-cGAMP.
      
 0.848
yqfF
Putative membrane associate hydrolase; Probably has phosphodiesterase (PDE) activity against cyclic- di-AMP (c-di-AMP); may be the major c-di-AMP PDE in the cell. In B.subtilis c-di-AMP is a second messenger that mediates growth, DNA repair and cell wall homeostasis; it is toxic when present in excess.
      
 0.753
cdnD
Phosphodiesterase acting on cyclic dinucleotides; Has phosphodiesterase (PDE) activity against cyclic-di-AMP (c-di-AMP) and to a much lesser extent against cyclic-di-GMP (c-di-GMP) in the DHH/DHHA1 domains. Also has ATPase activity, probably via the GGDEF domain. Overexpression leads to increased sensitivity to methyl methanesulfonate (MMS) and H(2)O(2). Overexpression leads to extreme sensitivity to the beta-lactam antibiotic cefuroxime (CEF), probably dependent on PDE activity. May monitor cellular heme or NO levels. In B.subtilis c-di-AMP is a second messenger that mediates growth, [...]
   
  
 0.753
yxkD
Efflux transporter; Evidence 1a: Function experimentally demonstrated in the studied strain; transporter.
  
  
 0.716
ykkC
Efflux transporter; Probably involved in guanidinium transport. In vitro, confers resistance to a broad range of toxic compounds such as cationic dyes, neutral and anionic antimicrobials.
   
  
 0.686
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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