STRINGSTRING
AEI13833.1 AEI13833.1 clpP clpP clpX clpX lon lon AEI13875.1 AEI13875.1 AEI14265.1 AEI14265.1 AEI14560.1 AEI14560.1 AEI14663.1 AEI14663.1 AEI14891.1 AEI14891.1 AEI15143.1 AEI15143.1 AEI15532.1 AEI15532.1 AEI15642.1 AEI15642.1 msrB msrB hslU hslU hslV hslV htpG htpG AEI15888.1 AEI15888.1 AEI15923.1 AEI15923.1 groL groL groS groS dnaJ-2 dnaJ-2 dnaK dnaK grpE grpE hrcA hrcA
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:
AEI13833.1Rhodanese-like protein. (402 aa)
clpPATP-dependent Clp protease proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. (195 aa)
clpXATP-dependent Clp protease ATP-binding subunit clpX; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. (413 aa)
lonAnti-sigma H sporulation factor, LonB; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. (777 aa)
AEI13875.1Cytochrome c biogenesis protein transmembrane region. (244 aa)
AEI14265.1Alkyl hydroperoxide reductase/ Thiol specific antioxidant/ Mal allergen. (161 aa)
AEI14560.1Thioredoxin; Belongs to the thioredoxin family. (105 aa)
AEI14663.1Thioredoxin reductase. (318 aa)
AEI14891.1Alkyl hydroperoxide reductase/ Thiol specific antioxidant/ Mal allergen. (145 aa)
AEI15143.1Heat shock protein Hsp20; Belongs to the small heat shock protein (HSP20) family. (151 aa)
AEI15532.1Heat shock protein DnaJ domain protein. (219 aa)
AEI15642.1Alkyl hydroperoxide reductase/ Thiol specific antioxidant/ Mal allergen. (174 aa)
msrBPeptide methionine sulfoxide reductase msrB; 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. (336 aa)
hslUATP-dependent hsl protease ATP-binding subunit hslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. (440 aa)
hslVATP-dependent protease hslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. (175 aa)
htpGChaperone protein htpG; Molecular chaperone. Has ATPase activity. (626 aa)
AEI15888.1Redox-active disulfide protein 2. (81 aa)
AEI15923.1Peroxiredoxin. (197 aa)
groL60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (549 aa)
groS10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. (96 aa)
dnaJ-2Chaperone 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 [...] (378 aa)
dnaKChaperone protein dnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. (653 aa)
grpEProtein grpE; 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 i [...] (216 aa)
hrcAHeat-inducible transcription repressor HrcA; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. (349 aa)
Your Current Organism:
Flexistipes sinusarabici
NCBI taxonomy Id: 717231
Other names: F. sinusarabici DSM 4947, Flexistipes sinusarabici DSM 4947, Flexistipes sinusarabici str. DSM 4947, Flexistipes sinusarabici strain DSM 4947
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