STRINGSTRING
clpB-2 clpB-2 clpC clpC CT0265 CT0265 clpX clpX groES-1 groES-1 groEL groEL groES-2 groES-2 dnaK dnaK CT0644 CT0644 CT0645 CT0645 bcp-1 bcp-1 htpG htpG trx-2 trx-2 trxB trxB dsbD dsbD CT1144 CT1144 hslU hslU hslV hslV sodB sodB msrA msrA dnaJ dnaJ grpE grpE hrcA hrcA CT1492 CT1492 CT1500 CT1500 clpP clpP bcp-2 bcp-2 CT2233 CT2233 CT2237 CT2237 clpB-1 clpB-1
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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
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textmining
co-expression
protein homology
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clpB-2ATP-dependent Clp protease, ATP-binding subunit 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. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Belongs to [...] (438 aa)
clpCATP-dependent Clp protease, ATP-binding subunit ClpC; Identified by match to protein family HMM PF00004; match to protein family HMM PF02151; match to protein family HMM PF02861; match to protein family HMM PF07724; Belongs to the ClpA/ClpB family. (854 aa)
CT0265Conserved hypothetical protein; Identified by similarity to EGAD:103492; match to protein family HMM PF02151; match to protein family HMM PF02577. (204 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. (439 aa)
groES-1Chaperonin, 10 kDa; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. (95 aa)
groELChaperonin, 60 kDa; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (545 aa)
groES-2Chaperonin, 10 kDa; Identified by match to protein family HMM PF00166. (131 aa)
dnaKdnaK protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. (633 aa)
CT0644Heat shock protein, HSP20 family; Identified by match to protein family HMM PF00011; Belongs to the small heat shock protein (HSP20) family. (132 aa)
CT0645Hypothetical protein; Identified by Glimmer2; putative. (36 aa)
bcp-1Bacterioferritin comigratory protein, thiol peroxidase, putative; Identified by similarity to EGAD:18740; match to protein family HMM PF00578. (156 aa)
htpGHeat shock protein HtpG; Molecular chaperone. Has ATPase activity. (629 aa)
trx-2Thioredoxin; Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. (109 aa)
trxBThioredoxin reductase; Identified by similarity to EGAD:15213; match to protein family HMM PF00070; match to protein family HMM PF07992; match to protein family HMM TIGR01292. (311 aa)
dsbDThiol:disulfide interchange protein DsbD; Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm. This transfer involves a cascade of disulfide bond formation and reduction steps. Belongs to the thioredoxin family. DsbD subfamily. (607 aa)
CT1144Na+/H+ antiporter, putative; Identified by similarity to EGAD:6297; match to protein family HMM PF00999. (784 aa)
hslUHeat shock protein 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. (491 aa)
hslVHeat shock protein HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. (181 aa)
sodBSuperoxide dismutase; Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Belongs to the iron/manganese superoxide dismutase family. (200 aa)
msrAPeptide methionine 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. (284 aa)
dnaJdnaJ protein; 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, DnaK and Gr [...] (403 aa)
grpEgrpE protein; 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 [...] (194 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. (356 aa)
CT1492Thiolredoxin peroxidase; Identified by similarity to GP:3328221; match to protein family HMM PF00578. (195 aa)
CT1500Transcriptional regulator, MerR family; Identified by similarity to EGAD:17737; match to protein family HMM PF00376. (134 aa)
clpPATP-dependent Clp protease, proteolytic subunit ClpP; 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. (225 aa)
bcp-2Bacterioferritin comigratory protein, thiol peroxidase, putative; Identified by similarity to EGAD:18740; match to protein family HMM PF00578. (148 aa)
CT2233Thiol:disulfide interchange protein, thioredoxin family protein; Identified by similarity to EGAD:23849. (178 aa)
CT2237Hypothetical protein; Identified by Glimmer2; putative; Belongs to the ClpS family. (99 aa)
clpB-1ATP-dependent Clp protease, ATP-binding subunit 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. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Belongs to [...] (442 aa)
Your Current Organism:
Chlorobaculum tepidum
NCBI taxonomy Id: 194439
Other names: C. tepidum TLS, Chlorobaculum tepidum TLS, Chlorobium tepidum TLS
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