STRINGSTRING
DJ87_1933 protein (Bacillus cereus) - STRING interaction network
"DJ87_1933" - annotation not available in Bacillus cereus
Nodes:
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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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
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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
DJ87_1933annotation not available (412 aa)    
Predicted Functional Partners:
comEA
annotation not available (199 aa)
   
   
  0.690
mtnA_1
Methylthioribose-1-phosphate isomerase; Catalyzes the interconversion of methylthioribose-1- phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1- P); Belongs to the EIF-2B alpha/beta/delta subunits family. MtnA subfamily (351 aa)
         
  0.605
mtnA_2
Methylthioribose-1-phosphate isomerase; Catalyzes the interconversion of methylthioribose-1- phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1- P); Belongs to the EIF-2B alpha/beta/delta subunits family. MtnA subfamily (347 aa)
         
  0.605
mtnK_1
Methylthioribose kinase; Catalyzes the phosphorylation of methylthioribose into methylthioribose-1-phosphate (393 aa)
           
  0.592
mtnK_2
Methylthioribose kinase; Catalyzes the phosphorylation of methylthioribose into methylthioribose-1-phosphate (409 aa)
           
  0.592
cinA
cinA_cterm- competence/damage-inducible CinA C-terminal domain protein; Belongs to the CinA family (412 aa)
           
  0.537
ligA
DNA ligase; DNA ligase that catalyzes the formation of phosphodiester linkages between 5’-phosphoryl and 3’-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA; Belongs to the NAD-dependent DNA ligase family. LigA subfamily (669 aa)
         
  0.478
mtnX
2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase; Dephosphorylates 2-hydroxy-3-keto-5-methylthiopentenyl- 1-phosphate (HK-MTPenyl-1-P) yielding 1,2-dihydroxy-3-keto-5- methylthiopentene (DHK-MTPene) (219 aa)
           
  0.451
mtnW
2,3-diketo-5-methylthiopentyl-1-phosphate enolase; Catalyzes the enolization of 2,3-diketo-5- methylthiopentyl-1-phosphate (DK-MTP-1-P) into 2-hydroxy-3-keto-5- methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P); Belongs to the RuBisCO large chain family. Type IV subfamily (414 aa)
           
  0.418
mtnD
Acireductone dioxygenase; Catalyzes 2 different reactions between oxygene and the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene) depending upon the metal bound in the active site. Fe-containing acireductone dioxygenase (Fe-ARD) produces formate and 2-keto-4- methylthiobutyrate (KMTB), the alpha-ketoacid precursor of methionine in the methionine recycle pathway. Ni-containing acireductone dioxygenase (Ni-ARD) produces methylthiopropionate, carbon monoxide and formate, and does not lie on the methionine recycle pathway (170 aa)
           
  0.403
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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