STRINGSTRING
ispE protein (Bacillus cereus) - STRING interaction network
"ispE" - 4-diphosphocytidyl-2-C-methyl-D-erythritol kinase in Bacillus cereus
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:
some 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 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
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
ispE4-diphosphocytidyl-2-C-methyl-D-erythritol kinase; Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol (289 aa)    
Predicted Functional Partners:
ispF
2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase; Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4- diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP) (158 aa)
 
 
  0.992
ispD
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Catalyzes the formation of 4-diphosphocytidyl-2-C- methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4- phosphate (MEP) (226 aa)
 
 
  0.992
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 (292 aa)
   
  0.988
rnmV
Ribonuclease M5; Required for correct processing of both the 5’ and 3’ ends of 5S rRNA precursor. Cleaves both sides of a double-stranded region yielding mature 5S rRNA in one step (185 aa)
         
  0.949
ispG
4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase (flavodoxin); Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate; Belongs to the IspG family (370 aa)
   
 
  0.886
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)
 
   
  0.858
dxr
1-deoxy-D-xylulose 5-phosphate reductoisomerase; Catalyzes the NADP-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP); Belongs to the DXR family (380 aa)
   
     
  0.845
dxs
1-deoxy-D-xylulose-5-phosphate synthase; Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-xylulose-5-phosphate (DXP); Belongs to the transketolase family. DXPS subfamily (630 aa)
 
   
  0.839
purR
PurR- transcription regulator associated with purine metabolism; purR_Bsub- pur operon repressor PurR (282 aa)
   
   
  0.820
pth
Peptidyl-tRNA hydrolase; The natural substrate for this enzyme may be peptidyl- tRNAs which drop off the ribosome during protein synthesis; Belongs to the PTH family (186 aa)
 
        0.744
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
Server load: low (10%) [HD]