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
ppaCManganese-dependent inorganic pyrophosphatase; Catalyzes the hydrolysis of pyrophosphate to phosphate; Derived by automated computational analysis using gene prediction method: Protein Homology. (309 aa)    
Predicted Functional Partners:
atpB
F0F1 ATP synthase subunit A; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. Belongs to the ATPase A chain family.
  
 
 0.910
atpE
F0F1 ATP synthase 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.
  
 
 0.909
atpD
F0F1 ATP 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.
     
 0.906
atpC
F0F1 ATP synthase subunit epsilon; Produces ATP from ADP in the presence of a proton gradient across the membrane.
     
 0.903
atpG
F0F1 ATP synthase subunit gamma; Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex.
     
 0.903
ANK62191.1
Manganese-dependent inorganic pyrophosphatase; Catalyzes the hydrolysis of pyrophosphate to phosphate; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 
0.902
ANK63515.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
  0.901
atpA
F0F1 ATP synthase subunit alpha; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
   
 
  0.901
atpH
F0F1 ATP synthase 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.
   
 
  0.901
ppk
RNA degradosome polyphosphate kinase; Catalyzes the reversible transfer of the terminal phosphate of ATP to form a long-chain polyphosphate (polyP). Belongs to the polyphosphate kinase 1 (PPK1) family.
     
  0.900
Your Current Organism:
Lactobacillus backii
NCBI taxonomy Id: 375175
Other names: DSM 18080, JCM 18665, L. backii, LMG 23555, LMG:23555, Lactobacillus backi, Lactobacillus backii Tohno et al. 2013, strain L1062
Server load: low (30%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.