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slr1330 protein (Synechocystis sp. PCC6803) - STRING interaction network
"slr1330" - ATP synthase epsilon subunit in Synechocystis sp. PCC6803
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experimentally determined
Predicted Interactions
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gene co-occurrence
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textmining
co-expression
protein homology
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slr1330ATP synthase epsilon subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane (136 aa)    
Predicted Functional Partners:
atpA
ATP synthase a subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit (503 aa)
 
  0.999
slr1329
ATP synthase 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 (483 aa)
  0.999
sll1325
ATP synthase d 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 (185 aa)
 
  0.999
sll1327
ATP synthase g 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 (314 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 (179 aa)
 
  0.999
ssl2615
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 (81 aa)
   
  0.999
sll1323
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 (143 aa)
 
  0.999
sll1322
ATP synthase subunit a; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane (248 aa)
 
  0.997
adk1
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 (187 aa)
     
 
  0.979
adk2
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 (181 aa)
     
 
  0.967
Your Current Organism:
Synechocystis sp. PCC6803
NCBI taxonomy Id: 1148
Other names: Aphanocapsa sp. (strain N-1), Aphanocapsa sp. N-1, S. sp. PCC 6803, Synechocystis, Synechocystis PCC6803, Synechocystis sp. (ATCC 27184), Synechocystis sp. (PCC 6803), Synechocystis sp. (strain PCC 6803), Synechocystis sp. ATCC 27184, Synechocystis sp. PCC 6803, Synechocystis sp. PCC 6803 A, Synechocystis sp. PCC 6803 B, Synechocystis sp. PCC6803
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