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
HA50_08635Fe-S cluster assembly scaffold SufA; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the HesB/IscA family. (124 aa)    
Predicted Functional Partners:
HA50_08640
Fe-S cluster assembly protein SufB; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.975
HA50_22120
Fe-S cluster assembly protein NifU; May be involved in the formation or repair of [Fe-S] clusters present in iron-sulfur proteins.
  
  
 0.945
HA50_08645
Fe-S cluster assembly ATPase SufC; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.923
HA50_08650
FeS cluster assembly protein SufD; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.916
HA50_08655
Bifunctional cysteine desulfurase/selenocysteine lyase; Cysteine desulfurases mobilize the sulfur from L-cysteine to yield L-alanine, an essential step in sulfur metabolism for biosynthesis of a variety of sulfur-containing biomolecules. Component of the suf operon, which is activated and required under specific conditions such as oxidative stress and iron limitation. Acts as a potent selenocysteine lyase in vitro, that mobilizes selenium from L- selenocysteine. Selenocysteine lyase activity is however unsure in vivo.
  
 0.841
iscS
IscS subfamily cysteine desulfurase; Master enzyme that delivers sulfur to a number of partners involved in Fe-S cluster assembly, tRNA modification or cofactor biosynthesis. Catalyzes the removal of elemental sulfur atoms from cysteine to produce alanine. Functions as a sulfur delivery protein for Fe-S cluster synthesis onto IscU, an Fe-S scaffold assembly protein, as well as other S acceptor proteins.
 
 
 0.821
HA50_27895
IscS subfamily cysteine desulfurase; Catalyzes the removal of elemental sulfur from cysteine to produce alanine; involved in NAD biosynthesis; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.814
HA50_22115
Cysteine desulfurase NifS; Catalyzes the removal of elemental sulfur atoms from cysteine to produce alanine.
 
 
 0.785
djlA
Molecular chaperone DjlA; Regulatory DnaK co-chaperone. Direct interaction between DnaK and DjlA is needed for the induction of the wcaABCDE operon, involved in the synthesis of a colanic acid polysaccharide capsule, possibly through activation of the RcsB/RcsC phosphotransfer signaling pathway. The colanic acid capsule may help the bacterium survive conditions outside the host.
  
 
 0.774
iscR
Fe-S cluster assembly transcriptional regulator IscR; Regulates the transcription of several operons and genes involved in the biogenesis of Fe-S clusters and Fe-S-containing proteins.
  
  
 0.772
Your Current Organism:
Pantoea cypripedii
NCBI taxonomy Id: 55209
Other names: ATCC 29267, Bacillus cypripedii, CFBP 3613, CIP 105195, DSM 3873, Erwinia carotovora var. cypripedii, Erwinia cypripedii, Erwinia cyrpipedii, LMG 2655, LMG 2657, LMG:2655, LMG:2657, NCPPB 3004, P. cypripedii, Pectobacterium cypripedii
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