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
rsmIMethylase; Catalyzes the 2'-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA. (292 aa)    
Predicted Functional Partners:
mraW
S-adenosyl-L-methionine-dependent methyltransferase mraW; Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
  
   
 0.809
ksgA
Ribosomal RNA small subunit methyltransferase A; Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
     
 0.735
tatD
DNase; TatD like proteins; E.coli TatD is a cytoplasmic protein, shown to have magnesium dependent DNase activity.
  
    0.682
nifJ1
Oxidoreductase required for the transfer of electrons from pyruvate to flavodoxin, which reduces nitrogenase, Pyruvate + CoA + oxidized flavodoxin = acetyl-CoA + CO2 + reduced flavodoxin.
   
   0.607
greA
Transcription elongation factor GreA; Necessary for efficient RNA polymerase transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by cleavage factors such as GreA or GreB allows the resumption of elongation from the new 3'terminus. GreA releases sequences of 2 to 3 nucleotides.
  
  
 0.599
ftsZ
Cell division protein FtsZ; Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity.
  
   
 0.576
mesJ
CMP/dCMP deaminase, zinc-binding; Catalyzes the deamination of adenosine to inosine at the wobble position 34 of tRNA(Arg2); Belongs to the cytidine and deoxycytidylate deaminase family.
 
    0.572
CBL57259.1
5.2 Protein of unknown function similar to proteins from other organisms.
       0.551
ispE
4-diphosphocytidyl-2-C-methyl-D-erythritol kinase; Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
       0.548
gidB
Methyltransferase gidB (Glucose-inhibited division protein B); Specifically methylates the N7 position of a guanine in 16S rRNA; Belongs to the methyltransferase superfamily. RNA methyltransferase RsmG family.
 
   
 0.544
Your Current Organism:
Propionibacterium freudenreichii
NCBI taxonomy Id: 754252
Other names: P. freudenreichii subsp. shermanii CIRM-BIA1, Propionibacterium freudenreichii subsp. shermanii ATCC 9614, Propionibacterium freudenreichii subsp. shermanii CIP 103027, Propionibacterium freudenreichii subsp. shermanii CIRM-BIA1, Propionibacterium freudenreichii subsp. shermanii str. CIRM-BIA1, Propionibacterium freudenreichii subsp. shermanii strain CIRM-BIA1
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.