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_04374Hypothetical protein; KEGG: eci:UTI89_C3737 3.1e-11 yhdM; Zn(II)-responsive regulator of ZntA; COG: COG0789 Predicted transcriptional regulators; Psort location: Cytoplasmic, score:8.96. (141 aa)    
Predicted Functional Partners:
CKO_04614
Hypothetical protein; KEGG: sec:SC3266 0. arcB; aerobic respiration control sensor protein K07648; COG: COG0784 FOG: CheY-like receiver; Psort location: CytoplasmicMembrane, score:9.97.
   
 
 0.767
rpoD
Hypothetical protein; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is the primary sigma factor during exponential growth.
 
 
 0.720
cbpA
Hypothetical protein; DNA-binding protein that preferentially recognizes a curved DNA sequence. It is probably a functional analog of DnaJ; displays overlapping activities with DnaJ, but functions under different conditions, probably acting as a molecular chaperone in an adaptive response to environmental stresses other than heat shock. Lacks autonomous chaperone activity; binds native substrates and targets them for recognition by DnaK. Its activity is inhibited by the binding of CbpM.
  
 
 0.691
dnaJ
Hypothetical protein; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, Dna [...]
  
 
 0.691
rpoB
Hypothetical protein; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
    
 
 0.648
CKO_04820
Hypothetical protein; KEGG: sty:STY4302 1.0e-90 yrfE; putative NUDIX hydrolase K08312; COG: COG0494 NTP pyrophosphohydrolases including oxidative damage repair enzymes; Psort location: Cytoplasmic, score:8.96.
   
    0.619
rpoA
Hypothetical protein; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
   
 
 0.613
CKO_03140
Hypothetical protein; KEGG: sdy:SDY_3873 1.3e-250 glnA; glutamine synthetase K01915; COG: COG0174 Glutamine synthetase; Psort location: Cytoplasmic, score:9.97.
  
 
 0.608
rpoZ
Hypothetical protein; Promotes RNA polymerase assembly. Latches the N- and C- terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits.
   
 
 0.599
rpoC
Hypothetical protein; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
    
 
 0.598
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
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