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
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[Homology]
Score
iscSACysteine desulfurase involved in tRNA thiolation; Catalyzes the removal of elemental sulfur from cysteine to produce alanine. (379 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.
 
 0.996
sufU
Iron-sulfur cluster assembly scaffold protein; 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. Alkyl [...]
 
 0.991
mnmA
tRNA 2-thiouridylase; Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
 
  
 0.990
moeB
Molybdopterin biosynthesis adenylyltransferase; Catalyzes the adenylation by ATP of the carboxyl group of the C-terminal glycine of sulfur carrier protein MoaD.
  
 0.948
iscSB
Cysteine desulfurase; Catalyzes the removal of elemental sulfur from cysteine to produce alanine.
  
 
0.924
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.
  
  
0.916
cymR
Transcriptional regulator of cysteine biosynthesis; Master repressor of cysteine metabolism in B.subtilis. Controls the expression of genes involved either in cysteine synthesis from sulfide (cysK), sulfonates (ssu), or methionine (mccAB) or in cystine uptake (tcyP). Activity of CymR is positively regulated by CysK in response to cysteine availability. When cysteine is present, the pool of O-acetylserine (OAS) is low, which leads to the formation of a CymR-CysK complex and transcriptional repression of the CymR regulon occurs. In the absence of cysteine, the OAS pool is high and the Cy [...]
  
  
 0.912
yrkF
Putative rhodanese-related sulfur transferase; 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 sulfur carrier protein TusA family.
   
 
 0.907
miaB
Enzyme for ms(2)i(6)A formation for tRNA modification; Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6- (dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine.
  
  
 0.752
mtaB
tRNA N(6)-threonylcarbamoyladenosine (t(6)A) methylthiotransferase; Catalyzes the methylthiolation of N6- threonylcarbamoyladenosine (t(6)A), leading to the formation of 2- methylthio-N6-threonylcarbamoyladenosine (ms(2)t(6)A) at position 37 in tRNAs that read codons beginning with adenine. Belongs to the methylthiotransferase family. MtaB subfamily.
  
  
 0.751
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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