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DJ87_5398 protein (Bacillus cereus) - STRING interaction network
"DJ87_5398" - met_pdase_I: methionine aminopeptidase, type I in Bacillus cereus
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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DJ87_5398met_pdase_I- methionine aminopeptidase, type I (248 aa)    
Predicted Functional Partners:
def2
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 (184 aa)
   
   
  0.712
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)
   
   
  0.688
rplB
50S ribosomal protein L2; One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome (276 aa)
 
 
  0.640
rplD
50S ribosomal protein L4; Forms part of the polypeptide exit tunnel (207 aa)
 
 
  0.622
dat_2
D-alanine aminotransferase; Acts on the D-isomers of alanine, leucine, aspartate, glutamate, aminobutyrate, norvaline and asparagine. The enzyme transfers an amino group from a substrate D-amino acid to the pyridoxal phosphate cofactor to form pyridoxamine and an alpha- keto acid in the first half-reaction (290 aa)
     
   
  0.599
dat_3
D-alanine aminotransferase; Acts on the D-isomers of alanine, leucine, aspartate, glutamate, aminobutyrate, norvaline and asparagine. The enzyme transfers an amino group from a substrate D-amino acid to the pyridoxal phosphate cofactor to form pyridoxamine and an alpha- keto acid in the first half-reaction (291 aa)
     
   
  0.599
pbuE
annotation not available (394 aa)
     
   
  0.599
uppP_2
Undecaprenyl-diphosphatase; Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin; Belongs to the UppP family (270 aa)
         
  0.594
uppP
Undecaprenyl-diphosphatase; Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin; Belongs to the UppP family (263 aa)
         
  0.594
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)
 
 
  0.591
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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