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
hemKMethyltransferase; Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif; Belongs to the protein N5-glutamine methyltransferase family. PrmC subfamily. (300 aa)    
Predicted Functional Partners:
prfA
Peptide chain release factor RF-1; Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
 
 
 0.997
atpE
Hypothetical protein predicted by Glimmer/Critica; 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.
  
   0.798
atpH
F-type H+-transporting ATPase 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.
  
   0.784
atpG
F-type H+-transporting ATPase 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.
  
   0.777
atpA
F-type H+-transporting ATPase subunit alpha; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
  
   0.774
atpD
F-type H+-transporting ATPase 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.
   
   0.769
atpC
F-type H+-transporting ATPase subunit epsilon; Produces ATP from ADP in the presence of a proton gradient across the membrane.
   
   0.769
sua5
SUA5/YciO/YrdC/YwlC family protein; Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine.
 
  
 0.684
plsX
Glycerol-3-phosphate acyltransferase PlsX; Catalyzes the reversible formation of acyl-phosphate (acyl- PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
   
    0.596
metK
S-adenosylmethionine synthetase; Belongs to the AdoMet synthase family.
    
 0.579
Your Current Organism:
Acetobacter ghanensis
NCBI taxonomy Id: 431306
Other names: A. ghanensis, Acetobacter ghanensis Cleenwerck et al. 2007, Acetobacter sp. 384, Acetobacter sp. 444B, DSM 18895, LMG 23848, LMG:23848, strain 430A, strain R-29337
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