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_01011Hypothetical protein; KEGG: ecj:JW1912 4.7e-260 amyA; cytoplasmic alpha-amylase K01176; COG: COG0366 Glycosidases; Psort location: Cytoplasmic, score:9.97. (495 aa)    
Predicted Functional Partners:
CKO_05029
Hypothetical protein; KEGG: eci:UTI89_C4113 0. malS; alpha-amylase precursor K01176; COG: COG0366 Glycosidases; Psort location: Periplasmic, score:10.00.
 
   
  0.956
glgX
Hypothetical protein; Removes maltotriose and maltotetraose chains that are attached by 1,6-alpha-linkage to the limit dextrin main chain, generating a debranched limit dextrin.
  
 
 0.944
glgB
Hypothetical protein; Catalyzes the formation of the alpha-1,6-glucosidic linkages in glycogen by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position; Belongs to the glycosyl hydrolase 13 family. GlgB subfamily.
  
 
 0.942
CKO_04838
Hypothetical protein; Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties.
  
 0.938
CKO_04847
Hypothetical protein; Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties.
  
 0.936
CKO_04837
Hypothetical protein; KEGG: eco:b3416 0. malQ; 4-alpha-glucanotransferase (amylomaltase) K00705; COG: COG1640 4-alpha-glucanotransferase; Psort location: Cytoplasmic, score:9.97.
  
 
 0.923
CKO_02297
Hypothetical protein; KEGG: ssn:SSO_0800 0. putative glucosidase K01187; COG: COG1501 Alpha-glucosidases, family 31 of glycosyl hydrolases; Belongs to the glycosyl hydrolase 31 family.
  
 
 0.906
CKO_02764
Hypothetical protein; KEGG: ecj:JW0393 0. malZ; maltodextrin glucosidase K01187; COG: COG0366 Glycosidases; Psort location: Cytoplasmic, score:9.97; Belongs to the glycosyl hydrolase 13 family.
     
 0.905
CKO_02485
Hypothetical protein; KEGG: spt:SPA2056 0. nagE; pts system, N-acetylglucosamine-specific IIABC component K02802:K02803:K02804; COG: COG2190 Phosphotransferase system IIA components; Psort location: CytoplasmicMembrane, score:10.00.
  
  
 0.673
fliT
Hypothetical protein; Dual-function protein that regulates the transcription of class 2 flagellar operons and that also acts as an export chaperone for the filament-capping protein FliD. As a transcriptional regulator, acts as an anti-FlhDC factor; it directly binds FlhC, thus inhibiting the binding of the FlhC/FlhD complex to class 2 promoters, resulting in decreased expression of class 2 flagellar operons. As a chaperone, effects FliD transition to the membrane by preventing its premature polymerization, and by directing it to the export apparatus.
       0.627
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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