STRINGSTRING
clpP clpP SES89273.1 SES89273.1 SET35724.1 SET35724.1 htpG htpG SET39894.1 SET39894.1 SET54812.1 SET54812.1 SET62623.1 SET62623.1 dnaJ dnaJ dnaK dnaK grpE grpE hrcA hrcA lon lon clpX clpX SET79072.1 SET79072.1 SET79094.1 SET79094.1 codY codY hslU hslU hslV hslV xerC xerC SET84509.1 SET84509.1 SET88860.1 SET88860.1 SET94037.1 SET94037.1 SET97889.1 SET97889.1 SEU00254.1 SEU00254.1 SEU00346.1 SEU00346.1 groS groS groL groL glyQS glyQS ftsH ftsH
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:
clpPATP-dependent Clp protease, protease 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)
SES89273.1Integrase/recombinase XerC/integrase/recombinase XerD; Belongs to the 'phage' integrase family. (299 aa)
SET35724.1ATP-dependent Clp protease ATP-binding subunit ClpE; Belongs to the ClpA/ClpB family. (710 aa)
htpGMolecular chaperone HtpG; Molecular chaperone. Has ATPase activity. (627 aa)
SET39894.1ATP-dependent protease ClpP, protease subunit. (251 aa)
SET54812.1HSP20 family protein; Belongs to the small heat shock protein (HSP20) family. (149 aa)
SET62623.1Rhomboid protease GluP. (520 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, [...] (377 aa)
dnaKMolecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. (614 aa)
grpEMolecular chaperone 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 [...] (196 aa)
hrcAHeat-inducible transcriptional repressor; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. (343 aa)
lonATP-dependent Lon protease; 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. (792 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. (425 aa)
SET79072.1Membrane protease subunit HflC; HflC and HflK could regulate a protease. (309 aa)
SET79094.1Membrane protease subunit HflK; HflC and HflK could encode or regulate a protease. (332 aa)
codYTranscriptional pleiotropic repressor; DNA-binding protein that represses the expression of many genes that are induced as cells make the transition from rapid exponential growth to stationary phase. It is a GTP-binding protein that senses the intracellular GTP concentration as an indicator of nutritional limitations. At low GTP concentration it no longer binds GTP and stop to act as a transcriptional repressor; Belongs to the CodY family. (258 aa)
hslUATP-dependent HslUV 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. (464 aa)
hslVATP-dependent HslUV protease, peptidase subunit HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. (181 aa)
xerCIntegrase/recombinase XerC; Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. The XerC- XerD complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids. (299 aa)
SET84509.1Ca2+-transporting ATPase. (886 aa)
SET88860.1Peptidyl-prolyl cis-trans isomerase B (cyclophilin B); PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. (143 aa)
SET94037.1Protein of unknown function. (77 aa)
SET97889.1Protein of unknown function. (77 aa)
SEU00254.1Putative Mg2+ transporter-C (MgtC) family protein. (230 aa)
SEU00346.1ATP-dependent Clp protease ATP-binding subunit ClpC; Belongs to the ClpA/ClpB family. (810 aa)
groSChaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. (94 aa)
groLChaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (545 aa)
glyQSglycyl-tRNA synthetase; Catalyzes the attachment of glycine to tRNA(Gly). Belongs to the class-II aminoacyl-tRNA synthetase family. (461 aa)
ftsHCell division protease 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. (666 aa)
Your Current Organism:
Salinibacillus kushneri
NCBI taxonomy Id: 237682
Other names: AS 1.3566, Bacillaceae bacterium 8-2, Bacillaceae bacterium W11-1, JCM 12390, S. kushneri, Salinibacillus kushneri Ren and Zhou 2005, strain 8-2
Server load: low (16%) [HD]