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hscA protein (Methylobacillus flagellatus) - STRING interaction network
"hscA" - Fe-S protein assembly chaperone HscA in Methylobacillus flagellatus
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second shell of interactors
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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hscAFe-S protein assembly chaperone HscA; Chaperone involved in the maturation of iron-sulfur cluster-containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB (622 aa)    
Predicted Functional Partners:
dnaJ
Chaperone protein DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, D [...] (373 aa)
 
  0.998
hscB
Co-chaperone Hsc20; Co-chaperone involved in the maturation of iron-sulfur cluster-containing proteins. Seems to help targeting proteins to be folded toward HscA (177 aa)
 
  0.995
grpE
GrpE protein; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP- dependent [...] (184 aa)
 
  0.992
Mfla_0803
Ferredoxin, 2Fe-2S type (113 aa)
 
 
  0.991
groL
Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (544 aa)
 
  0.988
Mfla_0807
Scaffold protein; A scaffold on which IscS assembles Fe-S clusters. It is likely that Fe-S cluster coordination is flexible as the role of this complex is to build and then hand off Fe-S clusters (133 aa)
 
 
  0.979
Mfla_0806
Iron-sulfur cluster assembly protein IscA (107 aa)
 
 
  0.962
iscS
Cysteine desulfurase IscS; 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 (405 aa)
 
 
  0.950
Mfla_0809
Aminotransferase, class V (382 aa)
 
 
  0.933
fusA
Elongation factor G; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post- translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (697 aa)
 
  0.933
Your Current Organism:
Methylobacillus flagellatus
NCBI taxonomy Id: 265072
Other names: M. flagellatus, M. flagellatus KT, Methylobacillus, Methylobacillus flagellatus, Methylobacillus flagellatus KT, Methylobacillus flagellatus str. KT, Methylobacillus flagellatus strain KT
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