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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
yqeIRNA-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (97 aa)    
Predicted Functional Partners:
aroE
Shikimate dehydrogenase; Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).
 
    0.979
nadD
Nicotinic acid mononucleotide adenylyltransferase; Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
  
  
 0.904
yqeM
SAM-dependent methyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.875
rsfS
Ribosome silencing factor; Functions as a ribosomal silencing factor. Interacts with ribosomal protein L14 (rplN), blocking formation of intersubunit bridge B8. Prevents association of the 30S and 50S ribosomal subunits and the formation of functional ribosomes, thus repressing translation.
  
  
 0.852
yqeH
Ribosome biogenesis GTPase YqeH; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.843
yqeK
Phosphohydrolase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
    0.836
ODJ57729.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.821
BFR44_10715
ComE operon protein 2; Incomplete; partial in the middle of a contig; missing stop; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.469
topB
DNA topoisomerase III; Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA- (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA su [...]
     
 0.462
topA
DNA topoisomerase I; Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA- (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supe [...]
     
 0.462
Your Current Organism:
Brochothrix thermosphacta
NCBI taxonomy Id: 2756
Other names: ATCC 11509, B. thermosphacta, CCUG 35132, CIP 103251, DSM 20171, IFO 12167, JCM 20628, LMG 17208, LMG:17208, Microbacterium thermosphactum, NBRC 12167, NCIB 10018, NCIB:10018, NCTC 10822
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