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
KXA15520.1Putative calcium-translocating P-type ATPase, PMCA-type; KEGG: fnu:FN1022 3.5e-293 calcium-transporting ATPase K01537; Psort location: CytoplasmicMembrane, score: 10.00. (849 aa)    
Predicted Functional Partners:
KXA14254.1
Mg2+ transporter-C family protein; KEGG: hip:CGSHiEE_08975 2.6e-18 coaD; phosphopantetheine adenylyltransferase K07507; Psort location: CytoplasmicMembrane, score: 9.16.
 
 
 0.716
atpD
ATP synthase F1, beta subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.
   
 0.696
adk
Adenylate kinase; Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism; Belongs to the adenylate kinase family.
  
 
 0.678
KXA16732.1
Pyruvate kinase; KEGG: fnu:FN1765 6.6e-180 pyruvate kinase K00873; Psort location: Cytoplasmic, score: 9.97.
   
 
 0.650
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.
   
 
 0.647
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.
   
 0.646
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.
   
  0.627
KXA14141.1
Hypothetical protein; KEGG: fnu:FN1824 7.3e-39 manganese-dependent inorganic pyrophosphatase K15986; Psort location: Cytoplasmic, score: 9.26.
    
  0.606
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.
   
 0.601
atpB
ATP synthase F0, A subunit; 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.
     
 0.583
Your Current Organism:
Fusobacterium equinum
NCBI taxonomy Id: 134605
Other names: DSM 17476, F. equinum, Fusibacterium equinum, Fusobacterium equinum Dorsch et al. 2001, Fusobacterium equorum, JCM 11174, NCTC 13176, VPB 4027
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.