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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
ychFHypothetical protein; ATPase that binds to both the 70S ribosome and the 50S ribosomal subunit in a nucleotide-independent manner. (363 aa)    
Predicted Functional Partners:
pth
Hypothetical protein; The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis. Belongs to the PTH family.
 
  
 0.963
prfA
Hypothetical protein; Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
 
  
 0.911
pheT
Hypothetical protein; KEGG: ecp:ECP_1661 0. phenylalanyl-tRNA synthetase beta chain K01890; COG: COG0073 EMAP domain; Psort location: Cytoplasmic, score:9.97.
  
  
 0.897
guaA
Hypothetical protein; Catalyzes the synthesis of GMP from XMP.
  
  
 0.892
argS
Hypothetical protein; KEGG: eco:b1876 1.0e-296 argS, lov; arginine tRNA synthetase K01887; COG: COG0018 Arginyl-tRNA synthetase; Psort location: Cytoplasmic, score:9.97.
  
  
 0.875
lepA
Hypothetical protein; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre- translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP- dependent manner.
 
  
 0.860
metG
Hypothetical protein; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.
  
  
 0.818
rpsG
Hypothetical protein; One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center, probably blocks exit of the E-site tRNA; Belongs to the universal ribosomal protein uS7 family.
  
 
 0.770
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.
 
 
 0.734
prs
Hypothetical protein; Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib- 5-P); Belongs to the ribose-phosphate pyrophosphokinase family. Class I subfamily.
 
    0.716
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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