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Slit_0132 protein (Sideroxydans lithotrophicus) - STRING interaction network
"Slit_0132" - Cytochrome C1 in Sideroxydans lithotrophicus
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second shell of interactors
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proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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[Homology]
Score
Slit_0132Cytochrome C1 (213 aa)    
Predicted Functional Partners:
Slit_0130
ubiquinol-Cytochrome C reductase, iron-sulfur subunit; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis (170 aa)
  0.999
Slit_0131
Cytochrome b/b6 domain protein; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis (412 aa)
  0.999
Slit_2368
Peptidase M16 domain protein (454 aa)
     
  0.991
Slit_2367
Peptidase M16 domain protein (456 aa)
     
  0.991
Slit_2981
ATP synthase F1, 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 (473 aa)
     
  0.970
Slit_1123
Cytochrome C oxidase subunit III (195 aa)
   
  0.966
Slit_2983
ATP synthase F1, subunit alpha; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit (513 aa)
     
 
  0.945
atpC
ATP synthase F1, subunit epsilon; Produces ATP from ADP in the presence of a proton gradient across the membrane (141 aa)
     
      0.908
Slit_1838
Succinate dehydrogenase and fumarate reductase iron-sulfur protein (231 aa)
   
   
  0.876
atpH
ATP synthase F1, 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 (177 aa)
     
 
  0.874
Your Current Organism:
Sideroxydans lithotrophicus
NCBI taxonomy Id: 580332
Other names: S. lithotrophicus, S. lithotrophicus ES-1, Siderooxidans, Siderooxidans lithoautotrophicus, Sideroxydans, Sideroxydans lithotrophicus, Sideroxydans lithotrophicus ES-1, Sideroxydans lithotrophicus str. ES-1, Sideroxydans lithotrophicus strain ES-1, iron-oxidizing lithotroph ES-1
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