STRINGSTRING
hslV hslV hslU hslU dnaK dnaK dnaJ dnaJ hrcA hrcA grpE grpE hslO hslO groEL groEL groS groS AIL98723.1 AIL98723.1 AIL98857.1 AIL98857.1 groEL-2 groEL-2 clpP clpP clpX clpX lon lon clpS-2 clpS-2 clpA clpA AIL99771.1 AIL99771.1 clpP-2 clpP-2 clpB clpB trxA-2 trxA-2
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:
hslVPeptidase; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. (185 aa)
hslUATP-dependent protease; 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. (435 aa)
dnaKMolecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. (641 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, [...] (379 aa)
hrcAHeat-inducible transcription repressor; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. (359 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 [...] (208 aa)
hslOHsp33-like chaperonin; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family. (330 aa)
groELMolecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (545 aa)
groSMolecular chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. (98 aa)
AIL98723.1Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method: Protein Homology. (351 aa)
AIL98857.1Molecular chaperone Hsp70; Derived by automated computational analysis using gene prediction method: Protein Homology. (429 aa)
groEL-2Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (542 aa)
clpPClp protease; 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. (208 aa)
clpXClp protease ATP-binding protein; 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)
lonDNA-binding protein; 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. (806 aa)
clpS-2Clp protease ClpS; Involved in the modulation of the specificity of the ClpAP- mediated ATP-dependent protein degradation; Belongs to the ClpS family. (117 aa)
clpAClp protease ClpX; ATPase and specificity subunit of the ClpA-ClpP ATP dependent serine protease; directs protease to specific substrates; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the ClpA/ClpB family. (838 aa)
AIL99771.1Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method: Protein Homology. (205 aa)
clpP-2Clp protease; 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)
clpBATPase AAA; 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. (868 aa)
trxA-2Thioredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. (330 aa)
Your Current Organism:
Sinorhizobium meliloti
NCBI taxonomy Id: 382
Other names: ATCC 9930, CCUG 27879, CFBP 5561, DSM 30135, Ensifer meliloti, Ensifer sp. AC50a, Ensifer sp. AC50e, HAMBI 2148, IAM 12611, ICMP 12623, IFO 14782, JCM 20682, LMG 6133, LMG:6133, NBRC 14782, NCAIM B.01520, NRRL L-45, NZP 4027, Rhizobium meliloti, Rhizobium meliloti (megaplasmid pRME41B SYM), Rhizobium meliloti (plasmid pRmeGR4b), Rhizobium meliloti plasmid pRmeGR4b, Rhizobium sp. AC50e, S. meliloti
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