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atpD protein (Chlorobium phaeovibrioides) - STRING interaction network
"atpD" - ATP synthase subunit beta in Chlorobium phaeovibrioides
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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atpDATP 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; Belongs to the ATPase alpha/beta chains family (462 aa)    
Predicted Functional Partners:
atpG
ATP synthase gamma chain; 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 (291 aa)
  0.999
Cvib_0024
PFAM- H+-transporting two-sector ATPase, delta/epsilon subunit; KEGG- plt-Plut_0020 ATP synthase F1, epsilon subunit (88 aa)
   
  0.999
atpA
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; Belongs to the ATPase alpha/beta chains family (526 aa)
 
0.999
atpF
ATP synthase subunit b; 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 (175 aa)
 
  0.999
atpH
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; Belongs to the ATPase delta chain family (181 aa)
 
  0.999
atpB
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 (348 aa)
 
  0.999
atpE
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 (75 aa)
 
  0.990
Cvib_0866
PFAM- CoA-binding domain protein; ATP-citrate lyase/succinyl-CoA ligase; KEGG- plt-Plut_1062 citrate lyase, subunit 2 (610 aa)
   
   
  0.944
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 (218 aa)
     
 
  0.926
Cvib_0807
TIGRFAM- anaerobic ribonucleoside-triphosphate reductase; PFAM- ATP-cone domain protein; KEGG- swo-Swol_2273 oxygen-sensitive ribonucleoside-triphosphate reductase (717 aa)
         
    0.900
Your Current Organism:
Chlorobium phaeovibrioides
NCBI taxonomy Id: 290318
Other names: C. phaeovibrioides DSM 265, Chlorobium phaeovibrioides, Chlorobium phaeovibrioides DSM 265, Chlorobium phaeovibrioides DSM265, Chlorobium vibrioforme f. thiosulfatophilum DSM 265, Prosthecochloris vibrioformis DSM 265
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