STRINGSTRING
dnaJ dnaJ groL1 groL1 groS groS SYN_00029 SYN_00029 SYN_00030 SYN_00030 SYN_00031 SYN_00031 SYN_00045 SYN_00045 groS-2 groS-2 SYN_00110 SYN_00110 SYN_00143 SYN_00143 SYN_00338 SYN_00338 lon lon SYN_00784 SYN_00784 SYN_00894 SYN_00894 msrB msrB SYN_01288 SYN_01288 SYN_01289 SYN_01289 SYN_01290 SYN_01290 SYN_01439 SYN_01439 SYN_01815 SYN_01815 dnaJ-2 dnaJ-2 SYN_01907 SYN_01907 groS-3 groS-3 groL3 groL3 grpE grpE dnaK dnaK SYN_02089 SYN_02089 hslV hslV hslU hslU SYN_02351 SYN_02351 clpS clpS SYN_02378 SYN_02378 aat aat clpB clpB tig tig clpP clpP clpX clpX lon-2 lon-2 groL2 groL2 htpX-2 htpX-2 SYN_03787 SYN_03787
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:
dnaJChaperone 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 a [...] (373 aa)
groL1Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (544 aa)
groSCo-chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. (96 aa)
SYN_00029Molecular chaperone; Small heat shock protein; Belongs to the small heat shock protein (HSP20) family. (168 aa)
SYN_00030Molecular chaperone; Small heat shock protein; Belongs to the small heat shock protein (HSP20) family. (134 aa)
SYN_00031Molecular chaperone; Small heat shock protein; Belongs to the small heat shock protein (HSP20) family. (147 aa)
SYN_00045Thioredoxin; Belongs to the thioredoxin family. (110 aa)
groS-2Co-chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. (96 aa)
SYN_00110Chaperone protein dnaJ. (270 aa)
SYN_00143Rhodanese-related sulfurtransferase. (307 aa)
SYN_00338Glutaredoxin-like protein. (81 aa)
lonATP-dependent protease 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. (790 aa)
SYN_00784Small heat shock protein; Belongs to the small heat shock protein (HSP20) family. (153 aa)
SYN_00894Chaperone protein. (315 aa)
msrBPeptide 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. (362 aa)
SYN_01288Hypothetical cytosolic protein. (79 aa)
SYN_01289Copper chaperone copZ. (58 aa)
SYN_01290Copper-exporting ATPase. (826 aa)
SYN_01439Thioredoxin reductase. (324 aa)
SYN_01815Thiol:disulfide interchange protein. (238 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 [...] (377 aa)
SYN_01907Small heat shock protein; Belongs to the small heat shock protein (HSP20) family. (163 aa)
groS-3Co-chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. (98 aa)
groL3Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (542 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 [...] (213 aa)
dnaKChaperone protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. (637 aa)
SYN_02089Thioredoxin. (214 aa)
hslVATP-dependent endopeptidase hsl proteolytic subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. (212 aa)
hslUATP-dependent endopeptidase hsl ATP-binding subunit; 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. (460 aa)
SYN_02351Cation transport ATPase. (809 aa)
clpSATP-dependent Clp protease adaptor protein; Involved in the modulation of the specificity of the ClpAP- mediated ATP-dependent protein degradation; Belongs to the ClpS family. (107 aa)
SYN_02378ATPase clp protease ATP binding subunit; Belongs to the ClpA/ClpB family. (768 aa)
aatleu/phe-tRNA-protein transferase; Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl- tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine. (239 aa)
clpBclpB protein; 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. (874 aa)
tigTrigger factor, ppiase; Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase; Belongs to the FKBP-type PPIase family. Tig subfamily. (443 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. (194 aa)
clpXATP-dependent clp protease ATP-binding subunit; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. (420 aa)
lon-2ATP-dependent protease 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. (812 aa)
groL2Chaperonin GroEL, truncated; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (545 aa)
htpX-2Endopeptidase htpX; Belongs to the peptidase M48B family. (284 aa)
SYN_03787Thioredoxin-like protein. (90 aa)
Your Current Organism:
Syntrophus aciditrophicus
NCBI taxonomy Id: 56780
Other names: S. aciditrophicus SB, Syntrophus aciditrophicus SB, Syntrophus aciditrophicus str. SB, Syntrophus aciditrophicus strain SB
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