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
KOO40704.1ATPase; Derived by automated computational analysis using gene prediction method: Protein Homology. (892 aa)    
Predicted Functional Partners:
KOO42995.1
NADPH--cytochrome reductase; Derived by automated computational analysis using gene prediction method: Protein Homology; In the N-terminal section; belongs to the cytochrome P450 family.
    
 0.836
KOO46846.1
Pyruvate kinase; Catalyzes the formation of phosphoenolpyruvate from pyruvate; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.801
KOO50336.1
Sodium:proton antiporter; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the monovalent cation:proton antiporter 2 (CPA2) transporter (TC 2.A.37) family.
  
 
 0.781
KOO41198.1
Sulfite reductase [NADPH] flavoprotein alpha-component; Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component.
    
 0.743
atpD
ATP F0F1 synthase subunit beta; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.
   
 0.737
atpE
ATP synthase F0F1 subunit C; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
   
 0.696
atpA
ATP F0F1 synthase subunit alpha; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
   
 
 0.691
KOO48550.1
MgtC/SapB transporter; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.686
KOO41262.1
MgtC/SapB transporter; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.686
atpH
ATP synthase F0F1 subunit delta; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
   
  0.674
Your Current Organism:
Bacillus koreensis
NCBI taxonomy Id: 284581
Other names: B. koreensis, Bacillus koreensis Lim et al. 2006, Bacillus sp. BR030, DSM 16467, KCTC 3914, strain BR030
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.