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
prmB[LSU ribosomal protein L3P]-glutamine N5-methyltransferase; Specifically methylates the 50S ribosomal protein L3 on a specific glutamine residue; Belongs to the protein N5-glutamine methyltransferase family. PrmB subfamily. (305 aa)    
Predicted Functional Partners:
prfA
Bacterial peptide chain release factor 1 (bRF-1); Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
 
 0.982
aroC
Chorismate synthase; Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.
 
  
 0.876
atpH
ATP synthase F1 subcomplex delta subunit; 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.
  
   0.835
atpA-2
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.
  
   0.778
SIP90440.1
Ubiquinol-cytochrome c reductase cytochrome c1 subunit.
  
 
   0.770
atpD
ATP synthase F1 subcomplex beta subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.
  
   0.761
atpC
ATP synthase F1 subcomplex epsilon subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane.
  
   0.761
atpE
F-type H+-transporting ATPase 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.
  
   0.731
SIQ72470.1
V/A-type H+-transporting ATPase subunit K.
  
   0.662
atpG
ATP synthase F1 subcomplex gamma subunit; 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.
  
   0.651
Your Current Organism:
Marinobacterium stanieri
NCBI taxonomy Id: 49186
Other names: ATCC 27130, CCUG 16021, CIP 106697, DSM 7027, LMG 6847, LMG:6847, M. stanieri, Pseudomonas stanieri, strain 146
Server load: low (22%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.