STRINGSTRING
dnaK dnaK grpE grpE dnaJ dnaJ htpG htpG clpP clpP clpX clpX AMW77850.1 AMW77850.1 AMW77915.1 AMW77915.1 AMD27_04760 AMD27_04760 lon lon AMW78268.1 AMW78268.1 AMW78739.1 AMW78739.1 AMW80370.1 AMW80370.1 clpB clpB groEL groEL groS groS ftsH ftsH AMW79501.1 AMW79501.1
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:
dnaKMolecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. (646 aa)
grpENucleotide exchange factor 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 [...] (182 aa)
dnaJMolecular chaperone 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, [...] (373 aa)
htpGHypothetical protein; Molecular chaperone. Has ATPase activity. (639 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. (203 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. (436 aa)
AMW77850.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (250 aa)
AMW77915.1Heat-shock protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the small heat shock protein (HSP20) family. (152 aa)
AMD27_04760Peptidase M28; Internal stop; Derived by automated computational analysis using gene prediction method: Protein Homology. (126 aa)
lonEndopeptidase La; 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. (808 aa)
AMW78268.15-formyltetrahydrofolate cyclo-ligase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the 5-formyltetrahydrofolate cyclo-ligase family. (193 aa)
AMW78739.1Peptidase M16; Derived by automated computational analysis using gene prediction method: Protein Homology. (502 aa)
AMW80370.1Peptidase M16; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the peptidase M16 family. (456 aa)
clpBATP-dependent chaperone ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family. (859 aa)
groELMolecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (544 aa)
groSCo-chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. (96 aa)
ftsHCell division protein FtsH; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family. (633 aa)
AMW79501.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (284 aa)
Your Current Organism:
Acinetobacter sp. TGLY2
NCBI taxonomy Id: 1407071
Other names: A. sp. TGL-Y2, Acinetobacter sp. TGL-Y2
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