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
prmCprotein-(glutamine-N5) methyltransferase, release factor-specific; 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. (281 aa)    
Predicted Functional Partners:
prfA
glutamyl-tRNA reductase; Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
 
 
 0.997
sirB2
Invasion protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
    0.845
atpH
ATP F0F1 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.
 
   0.707
atpG
ATP F0F1 synthase 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.
 
   0.686
atpE
ATP synthase F0F1 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.
  
   0.679
AMG31267.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.648
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.
  
   0.644
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.
  
   0.634
atpC
ATP synthase F0F1 subunit epsilon; Produces ATP from ADP in the presence of a proton gradient across the membrane.
  
   0.634
kdsA
2-dehydro-3-deoxyphosphooctonate aldolase; Catalyzes the formation of 2-dehydro-3-deoxy-D-octonate 8-phosphate from phosphoenolpyruvate and D-arabinose 5-phosphate in LPS biosynthesis; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the KdsA family.
       0.627
Your Current Organism:
Grimontia hollisae
NCBI taxonomy Id: 673
Other names: ATCC 33564, CAIM 625, CCUG 13625, CDC 0075-80, CIP 101886, DSM 15132, G. hollisae, IMET 12291, LMG 17719, LMG:17719, NCTC 11640, Special Bacteriology group EF-13, Vibrio hollisae
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