close STRING v12.5 is now available!
The next version of STRING is ready for use in your analyses: updated networks across STRING • newly available directed regulatory networks • a new typed view showing functional, physical, and regulatory edges in one network • new clustering options and cluster-based layouts • … and much more!
Explore STRING v12.5 →
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
CKO_02519Hypothetical protein; KEGG: stm:STM0643 3.9e-91 cobC; alpha ribazole-5'-P phosphatase in cobalamin synthesis K02226; COG: COG0406 Fructose-2,6-bisphosphatase; Belongs to the phosphoglycerate mutase family. (203 aa)    
Predicted Functional Partners:
cobS
Hypothetical protein; Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'- phosphate; Belongs to the CobS family.
 
 
 0.976
cobT
Hypothetical protein; Catalyzes the synthesis of alpha-ribazole-5'-phosphate from nicotinate mononucleotide (NAMN) and 5,6-dimethylbenzimidazole (DMB).
 
 
 0.968
CKO_02518
Hypothetical protein; KEGG: stt:t2223 1.6e-149 cobD; threonine-phosphate decarboxylase K04720; COG: COG0079 Histidinol-phosphate/aromatic aminotransferase and cobyric acid decarboxylase; Psort location: Cytoplasmic, score:8.96.
 
  
 0.770
CKO_00820
Hypothetical protein; Catalyzes ATP-dependent phosphorylation of adenosylcobinamide and addition of GMP to adenosylcobinamide phosphate.
 
  
 0.746
cobQ
Hypothetical protein; Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation. Belongs to the CobB/CobQ family. CobQ subfamily.
 
  
 0.723
cobD
Hypothetical protein; Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group.
 
  
 0.498
rsfS
Hypothetical protein; Functions as a ribosomal silencing factor. Interacts with ribosomal protein L14 (rplN), blocking formation of intersubunit bridge B8. Prevents association of the 30S and 50S ribosomal subunits and the formation of functional ribosomes, thus repressing translation.
  
    0.492
rlmH
Hypothetical protein; Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA; Belongs to the RNA methyltransferase RlmH family.
       0.487
cbiA
Hypothetical protein; Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source; Belongs to the CobB/CbiA family.
 
  
 0.478
CKO_00812
Hypothetical protein; KEGG: stm:STM2026 1.0e-113 cbiJ; precorrin-6X reductase K03397; COG: COG2099 Precorrin-6x reductase; Psort location: Cytoplasmic, score:8.96.
 
  
 0.478
Your Current Organism:
Citrobacter koseri
NCBI taxonomy Id: 290338
Other names: C. koseri ATCC BAA-895, Citrobacter (diversus) koseri ATCC BAA-895, Citrobacter koseri ATCC BAA-895, Citrobacter koseri str. ATCC BAA-895, Citrobacter koseri strain ATCC BAA-895
Server load: low (22%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.