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coaBC protein (Bacillus cereus) - STRING interaction network
"coaBC" - Coenzyme A biosynthesis bifunctional protein CoaBC in Bacillus cereus
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second shell of interactors
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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coaBCCoenzyme A biosynthesis bifunctional protein CoaBC; Catalyzes two steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4’-phosphopantothenate to form 4-phosphopantothenoylcysteine, in the latter compound is decarboxylated to form 4’-phosphopantotheine; In the C-terminal section; belongs to the PPC synthetase family (401 aa)    
Predicted Functional Partners:
coaD
Phosphopantetheine adenylyltransferase; Reversibly transfers an adenylyl group from ATP to 4’- phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate; Belongs to the bacterial CoaD family (163 aa)
 
 
  0.983
coaX
Type III pantothenate kinase; Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis (247 aa)
 
 
  0.982
dut
Dut- dUTP diphosphatase family protein (148 aa)
 
   
  0.911
sun
Ribosomal RNA small subunit methyltransferase B; Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA (444 aa)
 
 
  0.906
priA
Primosomal protein N; Involved in the restart of stalled replication forks. Recognizes and binds the arrested nascent DNA chain at stalled replication forks. It can open the DNA duplex, via its helicase activity, and promote assembly of the primosome and loading of the major replicative helicase DnaB onto DNA (801 aa)
              0.903
panC
Pantothenate synthetase; Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate; Belongs to the pantothenate synthetase family (282 aa)
 
 
  0.901
def1_1
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 (156 aa)
   
        0.894
stp
annotation not available (250 aa)
   
 
  0.876
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 (314 aa)
   
        0.849
prkC
annotation not available (657 aa)
              0.844
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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