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:
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Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
sufCSulfur mobilizing ABC protein, ATPase; Evidence 2b: Function of strongly homologous gene; enzyme; Belongs to the ABC transporter superfamily. Ycf16 family. (261 aa)    
Predicted Functional Partners:
sufB
FeS cluster formation protein; The SufBCD complex acts synergistically with SufE to stimulate the cysteine desulfurase activity of SufS. The SufBCD complex contributes to the assembly or repair of oxygen-labile iron-sulfur clusters under oxidative stress. May facilitate iron uptake from extracellular iron chelators under iron limitation (By similarity). Belongs to the UPF0051 (ycf24) family.
 
 0.999
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 [...]
 
  
 0.999
sufS
Cysteine desulfurase; Enzyme able to deliver sulfur to partners involved in Fe-S cluster assembly. Catalyzes the removal of elemental sulfur atoms from L-cysteine to produce L-alanine. Activity is stimulated 40- to 100-fold by SufU, which acts as a second substrate for this enzyme following release of Ala, and generating SufU.S. A mixture of SufS, SufU, Fra and L-cysteine is able to reconstitute Fe-S clusters on apo-aconitase (citB), reconstituting aconitase activity.
  
 0.999
sufD
FeS assembly protein SufD; The SufBCD complex acts synergistically with SufE to stimulate the cysteine desulfurase activity of SufS. The SufBCD complex contributes to the assembly or repair of oxygen-labile iron-sulfur clusters under oxidative stress. May facilitate iron uptake from extracellular iron chelators under iron limitation (By similarity). Belongs to the UPF0051 (ycf24) family.
 
 0.999
ycbU
Putative cysteine desulfurase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme.
 
  
 0.856
yitW
Conserved hypothetical protein; Involved in the maturation of iron-sulfur (Fe-S) proteins. May function as a Fe-S cluster carrier.
 
  
 0.840
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.
  
  
 0.744
sufA
Chaperone involved in Fe-S cluster assembly; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; factor.
  
 
 0.705
yutI
Putative iron-sulfur scaffold protein; May be involved in the formation or repair of [Fe-S] clusters present in iron-sulfur proteins.
     
 0.678
ccpA
Transcriptional regulator (Lacl family); Global transcriptional regulator of carbon catabolite repression (CCR) and carbon catabolite activation (CCA), which ensures optimal energy usage under diverse conditions. Interacts with either P- Ser-HPr or P-Ser-Crh, leading to the formation of a complex that binds to DNA at the catabolite-response elements (cre). Binding to DNA allows activation or repression of many different genes and operons.
    
   0.570
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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