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.
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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:
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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
CKO_04756Hypothetical protein; KEGG: stm:STM3455 1.3e-99 slyD; FKBP-type peptidyl prolyl cis-trans isomerase (rotamase) K03775; COG: COG1047 FKBP-type peptidyl-prolyl cis-trans isomerases 2; Psort location: Cytoplasmic, score:8.96. (195 aa)    
Predicted Functional Partners:
CKO_04076
Hypothetical protein; KEGG: eci:UTI89_C3084 0. hycE; formate hydrogenlyase subunit 5 precursor; COG: COG3261 Ni,Fe-hydrogenase III large subunit; Psort location: Cytoplasmic, score:8.96.
   
 
 0.897
CKO_04083
Hypothetical protein; KEGG: reh:H16_A1087 9.9e-14 ureG; UreA amidohydrolase (urease) regulatory and maturation protein UreG; COG: COG0378 Ni2+-binding GTPase involved in regulation of expression and maturation of urease and hydrogenase; Psort location: Cytoplasmic, score:9.97.
    
 
 0.895
ureG
Hypothetical protein; Facilitates the functional incorporation of the urease nickel metallocenter. This process requires GTP hydrolysis, probably effectuated by UreG.
    
 
 0.846
nuoC
Hypothetical protein; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; In the N-terminal section; belongs to the complex I 30 kDa subunit family.
   
 
 0.690
rpsJ
Hypothetical protein; Involved in the binding of tRNA to the ribosomes. Belongs to the universal ribosomal protein uS10 family.
   
  
 0.590
CKO_01835
Hypothetical protein; KEGG: stm:STM1238 5.2e-222 icdA; isocitrate dehydrogenase K00031; COG: COG0538 Isocitrate dehydrogenases; Psort location: Cytoplasmic, score:9.97.
  
    0.538
CKO_00123
Hypothetical protein; KEGG: eci:UTI89_C4335 4.1e-55 trxA; thioredoxin 1 K03671; COG: COG0526 Thiol-disulfide isomerase and thioredoxins; Psort location: Cytoplasmic, score:9.26; Belongs to the thioredoxin family.
   
   0.528
fusA
Hypothetical protein; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily.
   
  
 0.467
CKO_01946
Hypothetical protein; KEGG: eci:UTI89_C1237 3.3e-220 ndh; NADH dehydrogenase K03885; COG: COG1252 NADH dehydrogenase, FAD-containing subunit.
  
    0.461
CKO_04950
Hypothetical protein; KEGG: pfo:Pfl_2451 9.2e-122 FAD-dependent pyridine nucleotide-disulphide oxidoreductase K03885; COG: COG1252 NADH dehydrogenase, FAD-containing subunit; Psort location: Cytoplasmic, score:8.96.
  
    0.461
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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