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
AARI_15400Putative methyltransferase; Match to protein domain PF05175. This domain is found in ribosomal RNA small subunit methyltransferase C as well as other methyltransferases. (408 aa)    
Predicted Functional Partners:
prfA
Peptide chain release factor 1; Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
  
 
 0.861
AARI_26150
5.2 Protein of unknown function similar to proteins from other organisms.
    
 0.710
atpC
H(+)-transporting two-sector ATPase, epsilon chain; Produces ATP from ADP in the presence of a proton gradient across the membrane.
 
   0.577
atpE
H(+)-transporting two-sector ATPase, chain 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.
  
   0.573
atpH
H(+)-transporting two-sector ATPase, delta chain; 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; Belongs to the ATPase delta chain family.
  
   0.567
AARI_15410
Match to PF04101: Glycosyltransferase family 28 N-terminal domain. This family family comprises enzymes with a number of known activities; 1,2-diacylglycerol 3-beta-galactosyltransferase (EC 2.4.1.46); 1,2-diacylglycerol 3-beta-glucosyltransferase (EC 2.4.1.157); beta-N-acetylglucosamine transferase (EC 2.4.1).
       0.565
atpG
H(+)-transporting two-sector ATPase, 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.
  
   0.540
atpA
H(+)-transporting two-sector ATPase, alpha chain; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. Belongs to the ATPase alpha/beta chains family.
  
   0.539
atpD
H(+)-transporting two-sector ATPase, beta chain; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits; Belongs to the ATPase alpha/beta chains family.
  
   0.521
AARI_15420
Putative transcriptional regulator; Match to PF00440: bacterial regulatory proteins, tetR family.
       0.412
Your Current Organism:
Glutamicibacter arilaitensis
NCBI taxonomy Id: 861360
Other names: Arthrobacter arilaitensis CIP 108037, Arthrobacter arilaitensis Re117, G. arilaitensis Re117, Glutamicibacter arilaitensis Re117
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.