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
efeNPeroxidase converting ferric iron into ferrous iron; Involved in the recovery of exogenous heme iron. Extracts iron from heme while preserving the tetrapyrrol ring intact (By similarity). (416 aa)    
Predicted Functional Partners:
efeM
Lipoprotein binding ferrous or ferric iron for transport; Involved in iron uptake; Belongs to the EfeM/EfeO family.
 
  
 0.999
efeU
Ferrous ion permease; Uptake of Fe(2+) ions across the membrane.
 
  
 0.998
ycnJ
Putative copper import protein; Involved in uptake of extracellular oxidized copper under copper-limiting conditions; In the N-terminal section; belongs to the CopC family.
 
  
 0.932
phoD
Alkaline phosphatase D; Evidence 1a: Function experimentally demonstrated in the studied strain; enzyme.
      
 0.909
tatCD
Component of the twin-arginine pre-protein translocation pathway; Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin- arginine motif in their signal peptide across membranes. Required for PhoD secretion. TatCd promotes membrane localization of TatAd via domain specific interactions. TatCd is required for stabile production of TatAd as well as for its maintenance; Belongs to the TatC family.
 
   
 0.826
tatAC
Component of the twin-arginine pre-protein translocation pathway; Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin- arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system.
  
  
 0.816
tatAY
Component of the twin-arginine pre-protein translocation pathway; Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin- arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system. Required for YwbN secretion; Belongs to the TatA/E family.
     
 0.814
yvgO
Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function; PubMedId: 11988534.
      
 0.750
ykuE
Putative metallophosphoesterase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the metallophosphoesterase superfamily.
      
 0.742
wapA
Cell wall-associated protein precursor; Toxic component of a toxin-immunity protein module, which functions as a cellular contact-dependent growth inhibition (CDI) system. A site-specific general tRNA nuclease, the C-terminus (residues 2201-2334) removes 2 or 4 nucleotides from the 3' end of at least 4 tRNAs (upon expression in E.coli), possibly endonucleolytically. The nuclease activity is neutralized by expression of the cognate immunity protein WapI from the same strain, but not its homolog from 2 other B.subtilis strains. The C-terminus cannot be expressed on its own in E.coli, how [...]
   
  
 0.719
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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