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dbpA protein (Bacillus cereus) - STRING interaction network
"dbpA" - ATP-dependent RNA helicase DbpA in Bacillus cereus
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second shell of interactors
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proteins of unknown 3D structure
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some 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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dbpAATP-dependent RNA helicase DbpA; DEAD-box RNA helicase involved in the assembly of the 50S ribosomal subunit. Has an RNA-dependent ATPase activity, which is specific for 23S rRNA, and a 3’ to 5’ RNA helicase activity that uses the energy of ATP hydrolysis to destabilize and unwind short rRNA duplexes (481 aa)    
Predicted Functional Partners:
cshA
DEAD-box ATP-dependent RNA helicase CshA; DEAD-box RNA helicase possibly involved in RNA degradation. Unwinds dsRNA in both 5’- and 3’-directions, has RNA- dependent ATPase activity; Belongs to the DEAD box helicase family. CshA subfamily (525 aa)
   
   
0.825
cshA_1
DEAD-box ATP-dependent RNA helicase CshA; SNF2 family N-terminal domain protein (454 aa)
   
   
 
0.821
ppiB
Peptidyl-prolyl cis-trans isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (145 aa)
 
 
 
  0.503
sun
Ribosomal RNA small subunit methyltransferase B; Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA (444 aa)
   
 
  0.467
pnp
Polyribonucleotide nucleotidyltransferase; Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3’- to 5’-direction (712 aa)
   
 
  0.467
rraA
4-hydroxy-4-methyl-2-oxoglutarate aldolase; Catalyzes the aldol cleavage of 4-hydroxy-4-methyl-2- oxoglutarate (HMG) into 2 molecules of pyruvate. Also contains a secondary oxaloacetate (OAA) decarboxylase activity due to the common pyruvate enolate transition state formed following C-C bond cleavage in the retro-aldol and decarboxylation reactions (159 aa)
       
 
  0.441
truB
tRNA pseudouridine synthase B; Responsible for synthesis of pseudouridine from uracil- 55 in the psi GC loop of transfer RNAs (307 aa)
   
 
  0.419
fusA
Elongation factor G; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post- translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (692 aa)
   
 
  0.400
tetO
Tetracycline resistance protein TetO; small_GTP- small GTP-binding domain protein (647 aa)
   
 
  0.400
Your Current Organism:
Bacillus cereus
NCBI taxonomy Id: 1396
Other names: ATCC 14579, B. cereus, BCRC 10603, Bacillus cereus, Bacillus endorhythmos, Bacillus medusa, Bacillus sp. 2479, Bacillus sp. BS2(2013b), Bacillus sp. BV4, Bacillus sp. JKR50, Bacillus sp. JKR62, Bacillus sp. JP44SK22, Bacillus sp. JP44SK37, Bacillus sp. JP44SK43, Bacillus sp. JP44SK45, Bacillus sp. JSG1(2014), Bacillus sp. KER 17, Bacillus sp. MZ-01, Bacillus sp. PXDK-1, Bacillus sp. Pf-1, Bacillus sp. V3, Bacillus sp. mmm86, CCM 2010, CCRC 10603, CCUG 7414, CIP 66.24, DSM 31, IAM 12605, IFO 15305, JCM 2152, LMG 6923, NBRC 15305, NCCB 75008, NCIMB 9373, NCTC 2599, NRRL B-3711, VKM B-504
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