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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene Fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
yqfOConserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function. (373 aa)    
Predicted Functional Partners:
trmK
tRNA (adenine(22)-N(1))-methyltransferase; Catalyzes the S-adenosyl-L-methionine-dependent formation of N(1)-methyladenine at position 22 (m1A22) in tRNA.
  
 0.997
hisC
Histidinol-phosphate aminotransferase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily.
  
  
 0.871
ylxR
Putative RNA binding protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pf: putative factor.
   
  
 0.748
tsaD
tRNA(NNU) t(6)A37 threonylcarbamoyladenosine modification; Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB; this reaction does not require ATP in vitro. TsaD likely plays a direct catalytic role in this reaction. Belongs to the KAE1 / TsaD family.
  
  
 0.721
cshA
ATP-dependent RNA helicase; The most abundant DEAD-box RNA helicase. An ATP-dependent RNA helicase with RNA-dependent ATPase activity. May work in conjunction with the cold shock proteins to ensure proper initiation of transcription at low and optimal temperatures. In vitro, unwinds dsRNA in both 5'- and 3'- directions. Plays a role in ribosomal 50S subunit assembly. Its deletion leads to changes in mRNA levels for over 200 transcripts.
  
 
 0.658
ccpN
Negative regulator of gluconeogenesis; Transcription repressor that binds to the promoter of gapB and pckA genes, preventing their expression. Acts as a regulator for catabolite repression of gluconeogenic genes.
 
    0.640
tilS
tRNAile lysidine synthetase; Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine. Belongs to the tRNA(Ile)-lysidine synthase family.
 
  
 0.611
sigA
RNA polymerase major sigma-43 factor (sigma-A); 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; Belongs to the sigma-70 factor family. RpoD/SigA subfamily.
  
  
 0.610
dnaG
DNA primase; RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.
 
  
 0.606
recO
DNA double strand break repair and homologous recombination factor; Plays a role in DNA double-stranded break repair. It seems to be involved in an RecBC-independent recombinational process of DNA repair. It may act with RecF and RecR. Is recruited to repair centers, foci that are the site of double-strand break(s) after RecN and before RecF; may actively recruit RecF.
 
     0.605
Your Current Organism:
Bacillus subtilis 168
NCBI taxonomy Id: 224308
Other names: B. subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis 168, Bacillus subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis str. BGSC 1A700
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