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
EIM63655.1Inorganic pyrophosphatase/exopolyphosphatase; PFAM: DHH family; DHHA2 domain. (306 aa)    
Predicted Functional Partners:
atpF-3
ATP synthase, F0 subunit b; Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0); Belongs to the ATPase B chain family.
  
  
  0.782
atpE-2
ATP synthase, F0 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.
     
 0.767
atpG
ATP synthase, F1 gamma subunit; 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.
     
 0.756
atpC-2
ATP synthase, F1 epsilon subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane.
     
 0.756
atpH
ATP synthase, F1 delta subunit; 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.
   
 
  0.751
atpE
ATP synthase, F0 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.
     
 0.707
atpC
Alternate F1F0 ATPase, F1 subunit epsilon; Produces ATP from ADP in the presence of a proton gradient across the membrane.
     
 0.693
EIM62180.1
PFAM: ATP synthase; TIGRFAM: alternate F1F0 ATPase, F1 subunit gamma; ATP synthase, F1 gamma subunit.
     
 0.693
pheT
phenylalanyl-tRNA synthetase, beta subunit; PFAM: tRNA synthetase B5 domain; Ferredoxin-fold anticodon binding domain; B3/4 domain; Putative tRNA binding domain; TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit, non-spirochete bacterial; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily.
   
    0.669
atpB
Alternate F1F0 ATPase, F0 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.
  
 
 0.665
Your Current Organism:
Desulfobacter postgatei
NCBI taxonomy Id: 879212
Other names: D. postgatei 2ac9, Desulfobacter postgatei 2ac9, Desulfobacter postgatei DSM 2034, Desulfobacter postgatei str. 2ac9, Desulfobacter postgatei strain 2ac9
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