STRINGSTRING
ppaX protein (Bacillus cereus) - STRING interaction network
"ppaX" - Pyrophosphatase PpaX in Bacillus cereus
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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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ppaXPyrophosphatase PpaX; Hydrolyzes pyrophosphate formed during P-Ser-HPr dephosphorylation by HPrK/P. Might play a role in controlling the intracellular pyrophosphate pool (216 aa)    
Predicted Functional Partners:
lgt
Prolipoprotein diacylglyceryl transferase; Transfers the N-acyl diglyceride group on what will become the N-terminal cysteine of membrane lipoproteins (270 aa)
 
   
  0.979
ppk1
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 (702 aa)
         
  0.909
dapH_1
annotation not available (168 aa)
         
  0.896
hprK
HPr kinase/phosphorylase; Catalyzes the ATP- as well as the pyrophosphate- dependent phosphorylation of a specific serine residue in HPr, a phosphocarrier protein of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS). HprK/P also catalyzes the pyrophosphate-producing, inorganic phosphate-dependent dephosphorylation (phosphorolysis) of seryl-phosphorylated HPr (P- Ser-HPr). The two antagonistic activities of HprK/P are regulated by several intracellular metabolites, which change their concentration in response to the absence or presence of rapidly metabolisable carb [...] (309 aa)
         
  0.876
ppaC
annotation not available (309 aa)
       
    0.803
DJ87_2792
annotation not available (205 aa)
            0.788
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)
     
 
    0.701
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 (180 aa)
     
 
    0.677
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 (168 aa)
     
 
    0.673
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 (468 aa)
     
 
    0.660
Your Current Organism:
Bacillus cereus
NCBI taxonomy Id: 1396
Other names: ATCC 14579, B. cereus, BCRC 10603, Bacillus cereus, Bacillus endorhythmos, Bacillus medusa, Bacillus sp. 2479, Bacillus sp. BS2(2013b), Bacillus sp. BV4, Bacillus sp. JKR50, Bacillus sp. JKR62, Bacillus sp. JP44SK22, Bacillus sp. JP44SK37, Bacillus sp. JP44SK43, Bacillus sp. JP44SK45, Bacillus sp. JSG1(2014), Bacillus sp. KER 17, Bacillus sp. MZ-01, Bacillus sp. PXDK-1, Bacillus sp. Pf-1, Bacillus sp. V3, Bacillus sp. mmm86, CCM 2010, CCRC 10603, CCUG 7414, CIP 66.24, DSM 31, IAM 12605, IFO 15305, JCM 2152, LMG 6923, NBRC 15305, NCCB 75008, NCIMB 9373, NCTC 2599, NRRL B-3711, VKM B-504
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