STRINGSTRING
STRING protein interaction network
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
ppaXPyrophosphatase; Hydrolyzes pyrophosphate formed during P-Ser-HPr dephosphorylation by HPrK/P. Might play a role in controlling the intracellular pyrophosphate pool. (217 aa)    
Predicted Functional Partners:
lgt
Prolipoprotein diacylglyceryl transferase; Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins; Belongs to the Lgt family.
 
  
 0.929
KQL53084.1
Acetyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
    0.898
cinA
Damage-inducible protein CinA; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the CinA family.
    
  0.738
KQL50995.1
PTS glucose transporter subunit IICBA; Phosphoenolpyruvate-dependent sugar phosphotransferase system; catalyzes the phosphorylation of incoming sugar substrates concomitant with their translocation across the cell membrane; IIB is phosphorylated by IIA and then transfers the phosphoryl group to the sugar; IIC forms the translocation channel; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
  0.735
KQL51258.1
PTS beta-glucoside transporter subunit IIABC; Phosphoenolpyruvate-dependent sugar phosphotransferase system; catalyzes the phosphorylation of incoming sugar substrates concomitant with their translocation across the cell membrane; IIB is phosphorylated by IIA and then transfers the phosphoryl group to the sugar; IIC forms the translocation channel; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
  0.735
guaB
Inosine-5'-monophosphate dehydrogenase; Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. Belongs to the IMPDH/GMPR family.
    
  0.728
atpG
ATP synthase F0F1 subunit gamma; 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.
   
 
  0.695
atpF
ATP synthase F0F1 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.
   
 
  0.687
atpH
ATP synthase F0F1 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.
   
 
  0.686
atpD
ATP F0F1 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.
   
 
  0.684
Your Current Organism:
Bacillus shackletonii
NCBI taxonomy Id: 157838
Other names: B. shackletonii, Bacillus shackletonii Logan et al. 2004, CIP 107762, LMG 18435, LMG:18435, bacterium LMG 18435, strain Logan B1724, strain SSI024
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