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
kdpBPotassium-transporting ATPase subunit B; Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit is responsible for energy coupling to the transport system. Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IA subfamily. (705 aa)    
Predicted Functional Partners:
kdpC
Potassium-transporting ATPase subunit C; Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit acts as a catalytic chaperone that increases the ATP-binding affinity of the ATP-hydrolyzing subunit KdpB by the formation of a transient KdpB/KdpC/ATP ternary complex.
 
 0.999
kdpA
Potassium-transporting ATPase subunit KdpA; Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit binds and transports the potassium across the cytoplasmic membrane.
 0.999
kdpA-2
Potassium-transporting ATPase subunit KdpA; Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit binds and transports the potassium across the cytoplasmic membrane.
 0.998
kdpC-2
Potassium-transporting ATPase subunit C; Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit acts as a catalytic chaperone that increases the ATP-binding affinity of the ATP-hydrolyzing subunit KdpB by the formation of a transient KdpB/KdpC/ATP ternary complex.
 
 0.996
OJY17454.1
Sensory histidine kinase in two-component regulatory system with KdpE; signal sensing protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.888
OJY18042.1
Sensory histidine kinase in two-component regulatory system with KdpE; signal sensing protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+.
  
 0.888
OJY21830.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+.
  
  
 0.697
OJY17340.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.634
OJY17445.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.623
OJY30750.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.529
Your Current Organism:
Myxococcales bacterium 6820
NCBI taxonomy Id: 1895795
Other names: M. bacterium 68-20, Myxococcales bacterium 68-20
Server load: low (18%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.