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rsmB rsmB fmt fmt rlmN rlmN prpC prpC thiI thiI defA defA truB truB rsmE rsmE rbgA rbgA rpe rpe cpgA cpgA
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
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Predicted Interactions
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gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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rsmBRNA-binding Sun protein; Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA. (447 aa)    
Predicted Functional Partners:
fmt
methionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family.
 
  
 0.999
rlmN
23S rRNA m2A2503 methyltransferase; Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs; Belongs to the radical SAM superfamily. RlmN family.
  
  
 0.990
prpC
Phosphorylated protein phosphatase; Protein phosphatase that dephosphorylates PrkC and EF-G (elongation factor G, fusA). prpC and prkC are cotranscribed, which suggests that they form a functional couple in vivo, PrpC's primary role being possibly to counter the action of PrkC. May be involved in sporulation and biofilm formation. Does not seem to be involved in stress response. Dephosphorylates phosphorylated CgsA, EF-Tu and YezB.
 
 
 0.989
thiI
Putative persulfide ATP pyrophosphatase involved in thiamine biosynthesis and tRNA modification; Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS.
   
    0.945
defA
Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions (By similarity).
  
  
 0.938
truB
tRNA pseudouridine 55 synthase; Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs; Belongs to the pseudouridine synthase TruB family. Type 1 subfamily.
 
 
 0.934
rsmE
Methylase of U1498 in 16S rRNA; Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit (By similarity).
 
  
 0.924
rbgA
Ribosome biogenesis GTPase A; Essential protein that is required for a late step of 50S ribosomal subunit assembly. Has GTPase activity that is stimulated by interaction with the immature 50S ribosome subunit. Binds to the 23S rRNA. Required for the association of ribosomal proteins RplP and RpmA with the large subunit.
 
 
 0.919
rpe
Ribulose-5-phosphate 3-epimerase; Catalyzes the reversible epimerization of D-ribulose 5- phosphate to D-xylulose 5-phosphate; Belongs to the ribulose-phosphate 3-epimerase family.
 
 
 0.911
cpgA
GTPase involved in ribosome and sacculus morphogenesis; One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Helps release RbfA from mature subunits. May play a role in the assembly of ribosomal proteins into the subunit. Circularly permuted GTPase with a low level of activity and slow catalytic turnover, does not act on ATP. GTPase activity is stimulated by the presence of 30S or 70S ribosomes, phosphorylation increases stimulation. Depletion results in increased sensitivity to protein synthesis inhibitors that block the [...]
  
  
 0.907
Your Current Organism:
Bacillus subtilis 168
NCBI taxonomy Id: 224308
Other names: B. subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis 168, Bacillus subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis str. BGSC 1A700
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