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
norVHypothetical protein; Anaerobic nitric oxide reductase; uses NADH to detoxify nitric oxide (NO), protecting several 4Fe-4S NO-sensitive enzymes. Has at least 2 reductase partners, only one of which (NorW, flavorubredoxin reductase) has been identified. NO probably binds to the di-iron center; electrons enter from the NorW at rubredoxin and are transferred sequentially to the FMN center and the di-iron center. Also able to function as an aerobic oxygen reductase; In the N-terminal section; belongs to the zinc metallo- hydrolase group 3 family. (482 aa)    
Predicted Functional Partners:
norW
Hypothetical protein; One of at least two accessory proteins for anaerobic nitric oxide (NO) reductase. Reduces the rubredoxin moiety of NO reductase.
   
 0.989
CKO_01293
Hypothetical protein; KEGG: eca:ECA2991 0. nasB; nitrite reductase [NAD(P)H] large subunit K00362; COG: COG2146 Ferredoxin subunits of nitrite reductase and ring-hydroxylating dioxygenases; Psort location: Cytoplasmic, score:9.26; Belongs to the nitrite and sulfite reductase 4Fe-4S domain family.
  
 
 0.977
CKO_04789
Hypothetical protein; KEGG: stm:STM3474 0. nirB; nitrite reductase, large subunit K00362; COG: COG1251 NAD(P)H-nitrite reductase; Psort location: Cytoplasmic, score:9.97; Belongs to the nitrite and sulfite reductase 4Fe-4S domain family.
 
 
 0.972
CKO_04391
Hypothetical protein; KEGG: sty:STY3321 1.0e-202 hyb0; hydrogenase small chain K06282; COG: COG1740 Ni,Fe-hydrogenase I small subunit; Psort location: Periplasmic, score:9.76.
  
 
 0.767
CKO_01425
Hypothetical protein; KEGG: ecp:ECP_1403 0. probable pyruvate-flavodoxin oxidoreductase K03737; COG: COG1013 Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, beta subunit.
 
  
 0.755
norR
Hypothetical protein; Required for the expression of anaerobic nitric oxide (NO) reductase, acts as a transcriptional activator for at least the norVW operon. Activation also requires sigma-54.
 
   
 0.753
CKO_01046
Hypothetical protein; Iron-storage protein.
 
  
 0.745
CKO_01042
Hypothetical protein; Iron-storage protein.
 
  
 0.736
hcp
Hypothetical protein; Catalyzes the reduction of hydroxylamine to form NH(3) and H(2)O.
 
   
 0.730
ytfE
Hypothetical protein; Di-iron-containing protein involved in the repair of iron- sulfur clusters damaged by oxidative and nitrosative stress conditions.
  
  
 0.644
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: medium (56%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.