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:
some 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
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
iscSBCysteine desulfurase iscs 2; Catalyzes the removal of elemental sulfur from cysteine to produce alanine (381 aa)    
Predicted Functional Partners:
thiI
Putative persulfide atp pyrophosphatase involved in thiamine biosynthesis and trna modification; Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS
 0.995
sufU
Nitrogen fixation protein nifu and related proteins; Its function is controversial. Has been generally assumed to be an iron-sulfur cluster assembly scaffold protein but more recent evidence suggest it is a sulfurtransferase rather than a scaffold assembly protein . Has been shown to bind low levels of a labile, air- sensitive Fe-S cluster; this can be assembled under anaerobic conditions from FeCl(3) and Li(2)S. Has been shown to be able to transfer this Fe-S cluster to an acceptor protein. Stimulates the cysteine desulfurase activity of SufS, for which it acts as a second substrate. [...]
 0.979
yrkF
Putative rhodanese-related sulfur transferase; Belongs to the sulfur carrier protein TusA family
   
 
 0.976
moeB
Molybdopterin biosynthesis adenylyltransferase; Catalyzes the adenylation by ATP of the carboxyl group of the C-terminal glycine of sulfur carrier protein MoaD
  
 0.888
nifS
Putative desulfurase involved in iron-sulfur clusters for nad biosynthesis; Catalyzes the removal of elemental sulfur from cysteine to produce alanine (By similarity). Seems to be required for NAD biosynthesis
  
  
 
0.835
iscSA
Cysteine desulfurase involved in trna thiolation; Catalyzes the removal of elemental sulfur from cysteine to produce alanine
  
  
 
0.820
cysE
Serine o-acetyltransferase; Catalyzes the acetylation of serine by acetyl-CoA to produce O-acetylserine (OAS)
 
   
 0.770
moeA
Molybdene to molybdopterin ligation enzyme; Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP
  
  
 0.638
sspA
Small acid-soluble spore protein a (major alpha-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
       0.613
gcvPB
Glycine decarboxylase (subunit 2) (glycine cleavage system protein p); The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein (By similarity)
      
 0.598
Your Current Organism:
Bacillus subtilis
NCBI taxonomy Id: 224308
Other names: B. subtilis subsp. subtilis str. 168, Bacillus subtilis 168, Bacillus subtilis subsp. subtilis 168, Bacillus subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis str. BGSC 1A700
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