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
NPD11_673[C] COG0221 Inorganic pyrophosphatase. (116 aa)    
Predicted Functional Partners:
AQM61136.1
[C] COG1227 Inorganic pyrophosphatase/exopolyphosphatase.
     
 0.913
AQM60010.1
HAD-SF-IA-v1: HAD hydrolase, IA, variant 1 family protein; [R] COG0546 Predicted phosphatases.
   
 
  0.909
atpF
ATP synthase F0, B subunit; 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.
   
 
 0.843
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.
   
 
 0.829
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.
  
 
 0.794
ntpD
V-type ATPase, D subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane.
   
 
  0.781
ntpK
V-type sodium ATPase subunit K; [C] COG0636 F0F1-type ATP synthase, subunit c/Archaeal/vacuolar-type H+-ATPase, subunit K; Belongs to the V-ATPase proteolipid subunit family.
   
 
 0.765
atpE
ATP synthase F0, C 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.
   
 
 0.765
atpA
ATP synthase F1, alpha subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
  
 
 0.761
ntpB
V-type sodium ATPase subunit B; Produces ATP from ADP in the presence of a proton gradient across the membrane. The V-type beta chain is a regulatory subunit.
   
 
 0.759
Your Current Organism:
Clostridium baratii
NCBI taxonomy Id: 1561
Other names: ATCC 27638, Acuformis perennis, BCRC 14541, C. baratii, CCRC 14541, CCRC:14541, CCUG 24033, CIP 104306, Clostridium barati, Clostridium paraperfringens, Clostridium perenne, DSM 601, Inflabilis barati
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