STRINGSTRING
msrA msrA dnaJ dnaJ dnaK dnaK EC1_09950 EC1_09950 EC1_10540 EC1_10540 EC1_10550 EC1_10550 EC1_11730 EC1_11730 EC1_13180 EC1_13180 groL groL EC1_14770 EC1_14770
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:
msrAmethionine-S-sulfoxide reductase; Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. (350 aa)
dnaJChaperone 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 [...] (372 aa)
dnaKChaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. (603 aa)
EC1_09950Plasmid segregation actin-type ATPase ParM. (281 aa)
EC1_10540Molecular chaperone, HSP90 family. (427 aa)
EC1_10550Molecular chaperone, HSP90 family. (198 aa)
EC1_11730Peptidyl-prolyl cis-trans isomerase (rotamase)-cyclophilin family. (51 aa)
EC1_13180Thioredoxin. (109 aa)
groLChaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (537 aa)
EC1_14770Co-chaperonin GroES (HSP10); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter; Belongs to the GroES chaperonin family. (86 aa)
Your Current Organism:
Faecalitalea cylindroides
NCBI taxonomy Id: 717960
Other names: Eubacterium cylindroides T2-87, F. cylindroides T2-87, Faecalitalea cylindroides T2-87
Server load: low (30%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.