STRINGSTRING
ppa protein (Alcaligenes faecalis) - STRING interaction network
"ppa" - Inorganic pyrophosphatase in Alcaligenes faecalis
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second shell of interactors
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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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ppaInorganic pyrophosphatase; Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions (178 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 (513 aa)
     
 
  0.976
ppk
Polyphosphate kinase; Catalyzes the reversible transfer of the terminal phosphate of ATP to form a long-chain polyphosphate (polyP); Belongs to the polyphosphate kinase 1 (PPK1) family (690 aa)
       
  0.952
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 (473 aa)
     
  0.933
atpB
ATP synthase subunit a; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane (293 aa)
     
 
  0.930
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 (80 aa)
     
  0.927
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 (179 aa)
     
    0.925
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 (302 aa)
     
 
    0.922
atpC
ATP synthase epsilon chain; Produces ATP from ADP in the presence of a proton gradient across the membrane (140 aa)
     
 
    0.912
atpF
ATP synthase subunit b; Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0); Belongs to the ATPase B chain family (156 aa)
     
 
    0.912
JT27_17740
5-carboxymethyl-2-hydroxymuconate isomerase; Derived by automated computational analysis using gene prediction method- Protein Homology (231 aa)
              0.854
Your Current Organism:
Alcaligenes faecalis
NCBI taxonomy Id: 511
Other names: A. faecalis, ATCC 8750, Alcaligenes faecalis, Alcaligenes sp. BP11, CIP 55.84, CIP 60.80, DSM 30030, IAM 12369, IFO 13111, JCM 20522, JCM 20663, NBRC 13111, NCAIM B.01104, NCIMB 8156, NCTC 11953
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