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STRINGSTRING
STRING protein interaction network
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:
a 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 to 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
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
DJ90_1972Hypothetical protein; Cobalamin synthesis cobW C-terminal domain protein. (355 aa)    
Predicted Functional Partners:
rpsN2
Alternate 30S ribosomal protein S14; Binds 16S rRNA, required for the assembly of 30S particles and may also be responsible for determining the conformation of the 16S rRNA at the A site; Belongs to the universal ribosomal protein uS14 family.
  
 
 0.494
troA
Periplasmic zinc-binding protein troA; Belongs to the bacterial solute-binding protein 9 family.
 
  
 0.461
folE2
GTP cyclohydrolase folE2; Converts GTP to 7,8-dihydroneopterin triphosphate.
  
  
 0.455
DJ90_722
bacill_yteA: regulatory, yteA family protein.
  
  
 0.449
map
Methionine aminopeptidase, type I; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.
    
   0.442
map-2
Methionine aminopeptidase, type I; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.
    
   0.442
map-3
Methionine aminopeptidase, type I; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.
    
   0.442
map-4
Methionine aminopeptidase, type I; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.
    
   0.442
rpmB
L28: ribosomal protein L28; Belongs to the bacterial ribosomal protein bL28 family.
  
  
 0.438
hisE
histidine_hisI: phosphoribosyl-ATP diphosphatase; In the N-terminal section; belongs to the PRA-CH family.
     
 0.422
Your Current Organism:
Paenibacillus macerans
NCBI taxonomy Id: 44252
Other names: ATCC 8244, Aerobacillus macerans, BCRC 14680, Bacillus macerans, Bactrillum macerans, CCM 2012, CCRC 14680, CCRC:14680, CCUG 7423, CFBP 4253, CIP 66.19, DSM 24, HAMBI 636, IAM 12467, IFO 15307, JCM 2500, LMG 13281, LMG 6324, LMG:13281, LMG:6324, NBRC 15307, NCCB 48019, NCIB 9368, NCIMB 9368, NCTC 6355, NRRL B-172, NRRL B-394, NRRL B-4267, P. macerans, VKM B-506, Zymobacillus macerans
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