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cshB protein (Bacillus cereus) - STRING interaction network
"cshB" - DEAD-box ATP-dependent RNA helicase CshB in Bacillus cereus
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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
filled nodes:
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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Cooccurence
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[Homology]
Score
cshBDEAD-box ATP-dependent RNA helicase CshB; Probable DEAD-box RNA helicase. May work in conjunction with the cold shock proteins to ensure proper initiation of transcription at low and optimal temperatures (436 aa)    
Predicted Functional Partners:
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)
       
 
  0.761
rnpA
Ribonuclease P protein component; RNaseP catalyzes the removal of the 5’-leader sequence from pre-tRNA to produce the mature 5’-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5’-leader sequence and broadening the substrate specificity of the ribozyme (115 aa)
     
 
  0.713
nfo
Probable endonuclease 4; Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic sites (AP sites) to produce new 5’-ends that are base-free deoxyribose 5-phosphate residues. It preferentially attacks modified AP sites created by bleomycin and neocarzinostatin (298 aa)
         
  0.707
ispH
4-hydroxy-3-methylbut-2-enyl diphosphate reductase; Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)- butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis; Belongs to the IspH family (316 aa)
   
        0.596
cat
annotation not available (185 aa)
           
  0.590
sun
Ribosomal RNA small subunit methyltransferase B; Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA (444 aa)
 
 
  0.546
DJ87_577
annotation not available (139 aa)
              0.545
DJ87_576
annotation not available (101 aa)
              0.522
truB
tRNA pseudouridine synthase B; Responsible for synthesis of pseudouridine from uracil- 55 in the psi GC loop of transfer RNAs (307 aa)
 
 
  0.511
yqeH
GTPase_YqeH- ribosome biogenesis GTPase YqeH (368 aa)
 
      0.497
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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