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
ylzJConserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function. (70 aa)    
Predicted Functional Partners:
tepA
Protein export-enhancing factor; Required for efficient translocation of pre-proteins across the membrane; Belongs to the peptidase S14 family. TepA subfamily.
  
  
 0.986
spoIIIE
Spore DNA translocase; Plays an essential role during sporulation. Required for the translocation of the chromosomal DNA from mother cell into the forespore during polar septation, for the final steps of compartmentalization in the presence of trapped DNA, and for the final steps of engulfment. The N-terminus mediates localization to the division septum and is required for both septal membrane fusion and engulfment membrane fusion. May form DNA-conducting channels across the two lipid bilayers of the septum after cell division. The C-terminus functions as a DNA motor that exports DNA i [...]
       0.560
rnjB
Ribonuclease J2; Endonucleolytically cleaves the 5'-leader sequence of certain mRNAs. Endonuclease digestion by the RNase J1/J2 complex occurs at a different site and in some cases more efficiently than J1 or J2 alone. The exonuclease activity of the J1/J2 complex is highly processive on substrates longer than 5 nucleotides, on shorter substrates is distributive. Plays a role in mRNA maturation and stability. Appears to have a limited effect on 16S rRNA maturation, despite its similarity to RNase J1. This subunit alone has very poor 5'-3' exonuclease activity. Belongs to the metallo-be [...]
       0.543
spoVT
Transcriptional regulator; Transcriptional factor that regulates positively or negatively the expression of a large number of forespore-specific sigma G-dependent genes. May provide a mechanism of feedback control that is important for forespore development. SpoVT levels during spore formation have a major impact on the germination and the resistance of the resultant spores. To B.subtilis AbrB and Abh.
      
 0.483
sspB
Small acid-soluble spore protein (beta-type SASP); SASP are bound to spore DNA. They are double-stranded DNA- binding proteins that cause DNA to change to an a-like conformation. They protect the DNA backbone from chemical and enzymatic cleavage and are thus involved in dormant spore's high resistance to UV light.
   
  
 0.422
sacA
Sucrase-6-phosphate hydrolase; Evidence 2b: Function of strongly homologous gene; Product type e: enzyme; Belongs to the glycosyl hydrolase 32 family.
      
 0.420
ymfC
Putative transcriptional regulator (GntR family); Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pr: putative regulator.
       0.419
dapA
Dihydrodipicolinate synthase; Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
       0.414
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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