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atpH protein (Desulfovibrio vulgaris Hildenborough) - STRING interaction network
"atpH" - ATP synthase subunit delta in Desulfovibrio vulgaris Hildenborough
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experimentally determined
Predicted Interactions
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gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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atpHATP 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 (183 aa)    
Predicted Functional Partners:
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 (502 aa)
 
  0.999
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
atpD
ATP 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 (470 aa)
 
  0.999
atpC
ATP synthase epsilon chain; Produces ATP from ADP in the presence of a proton gradient across the membrane (134 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 (176 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 (233 aa)
 
  0.998
DVU_0780
ATP synthase F0, B’ subunit, putative; Identified by match to protein family HMM PF00430; Belongs to the ATPase B chain family (131 aa)
 
  0.997
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 (82 aa)
 
  0.995
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 (223 aa)
   
 
  0.931
DVU_3011
Uncharacterized protein; Identified by similarity to OMNI-CC2858 (264 aa)
   
 
  0.928
Your Current Organism:
Desulfovibrio vulgaris Hildenborough
NCBI taxonomy Id: 882
Other names: D. vulgaris str. Hildenborough, Desulfovibrio vulgaris (STRAIN HILDENBOROUGH), Desulfovibrio vulgaris ATCC 29579, Desulfovibrio vulgaris Hildenborough, Desulfovibrio vulgaris str. Hildenborough, Desulfovibrio vulgaris subsp. vulgaris (strain Hildenborough), Desulfovibrio vulgaris subsp. vulgaris ATCC 29579, Desulfovibrio vulgaris subsp. vulgaris str. Hildenborough
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