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
ydzAConserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function. (96 aa)    
Predicted Functional Partners:
ydbA
Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function.
      
 0.884
lrpC
Transcriptional regulator (Lrp/AsnC family); Transcriptional regulator with a possible role in regulation of amino acid metabolism. Plays a role in the growth phase transition.
     
 0.728
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 [...]
     
 0.696
ctaA
heme-A synthase; Catalyzes the oxidation of the C8 methyl side group on heme O porphyrin ring into a formyl group. Also involved in the sporulation.
   
    0.529
yozB
Putative integral inner membrane protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pm: putative membrane component.
  
    0.498
ppsD
Plipastatin synthetase; This protein is a multifunctional enzyme, able to activate and polymerize the amino acids Pro, Gln and Tyr as part of the biosynthesis of the lipopeptide antibiotic plipastatin. The Tyr residue is further epimerized to the D-isomer form. The activation sites for these amino acids consist of individual domains. Belongs to the ATP-dependent AMP-binding enzyme family.
   
  
 0.483
ppsC
Plipastatin synthetase; This protein is a multifunctional enzyme, able to activate and polymerize the amino acids Glu and Ala/Val as part of the biosynthesis of the lipopeptide antibiotic plipastatin. The Ala/Val residue is further epimerized to the D-isomer form. The activation sites for these amino acids consist of individual domains. Belongs to the ATP-dependent AMP-binding enzyme family.
   
  
 0.482
ywcI
Hypothetical protein; Evidence 5: No homology to any previously reported sequences.
      
 0.481
oxdC
Oxalate decarboxylase; Converts oxalate to formate and CO(2) in an O(2)-dependent reaction. Can also catalyze minor side reactions: oxalate oxidation to produce H(2)O(2), and oxalate-dependent, H(2)O(2)-independent dye oxidations.
   
  
 0.432
rnmV
Ribonuclease M5; Required for correct processing of both the 5' and 3' ends of 5S rRNA precursor. Cleaves both sides of a double-stranded region yielding mature 5S rRNA in one step. Releases 5'-phosphoryl and 3'- hydroxy termini.
      
 0.426
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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