STRINGSTRING
dnaK dnaK ACS20678.1 ACS20678.1 ACS20646.1 ACS20646.1 ACS20068.1 ACS20068.1 ACS20055.1 ACS20055.1 ACS19892.1 ACS19892.1 ACS19854.1 ACS19854.1 ACS19712.1 ACS19712.1 ACS19711.1 ACS19711.1 dsbB dsbB ACS19233.1 ACS19233.1 clpX clpX tig tig hscA hscA hscB hscB ACS18569.1 ACS18569.1 clpB clpB ACS18364.1 ACS18364.1 grpE grpE dnaJ dnaJ ACS18060.1 ACS18060.1 groS groS groL groL ACS17193.1 ACS17193.1 ACS16863.1 ACS16863.1 secB secB ACS20776.1 ACS20776.1 ureE ureE ACS21249.1 ACS21249.1 htpG htpG ACS21848.1 ACS21848.1 surA surA
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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.
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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
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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
Others
textmining
co-expression
protein homology
Your Input:
dnaKChaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. (645 aa)
ACS20678.1PFAM: cytoplasmic chaperone TorD family protein; KEGG: pol:Bpro_0935 cytoplasmic chaperone TorD. (205 aa)
ACS20646.1PFAM: peptidylprolyl isomerase FKBP-type; KEGG: aav:Aave_3772 peptidylprolyl isomerase, FKBP-type. (147 aa)
ACS20068.1Hsp33 protein; 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. (335 aa)
ACS20055.1KEGG: dia:Dtpsy_0919 fkbp-type peptidyl-prolyl cis-trans isomerase. (174 aa)
ACS19892.1PFAM: peptidylprolyl isomerase FKBP-type; KEGG: dia:Dtpsy_1738 peptidylprolyl isomerase. (142 aa)
ACS19854.1PFAM: heat shock protein DnaJ domain protein; chaperone DnaJ domain protein; SMART: heat shock protein DnaJ domain protein; KEGG: bav:BAV0873 curved DNA-binding protein. (320 aa)
ACS19712.1Peptidyl-prolyl cis-trans isomerase cyclophilin type; 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. (170 aa)
ACS19711.1Peptidyl-prolyl cis-trans isomerase cyclophilin type; 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. (199 aa)
dsbBDisulphide bond formation protein DsbB; Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein; Belongs to the DsbB family. (171 aa)
ACS19233.1PFAM: outer membrane chaperone Skp (OmpH); KEGG: vei:Veis_1447 outer membrane chaperone Skp (OmpH); Belongs to the skp family. (180 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. (421 aa)
tigTrigger factor; 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. (437 aa)
hscAFe-S protein assembly chaperone HscA; Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB. (618 aa)
hscBCo-chaperone Hsc20; Co-chaperone involved in the maturation of iron-sulfur cluster-containing proteins. Seems to help targeting proteins to be folded toward HscA; Belongs to the HscB family. (172 aa)
ACS18569.1KEGG: pcr:Pcryo_1830 P pilus assembly protein chaperone PapD-like. (242 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. (873 aa)
ACS18364.1PFAM: peptidylprolyl isomerase FKBP-type; KEGG: aav:Aave_1387 peptidylprolyl isomerase. (116 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 [...] (179 aa)
dnaJChaperone 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 [...] (378 aa)
ACS18060.1KEGG: dac:Daci_1060 molecular chaperone, HSP70 class. (420 aa)
groSChaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. (96 aa)
groLChaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (550 aa)
ACS17193.1Type VI secretion ATPase, ClpV1 family; KEGG: azo:azo3903 putative ATP-dependent Clp protease, ATP-binding subunit ClpB; TIGRFAM: type VI secretion ATPase, ClpV1 family; PFAM: ATPase AAA-2 domain protein; AAA ATPase central domain protein; Clp domain protein; SMART: AAA ATPase; Belongs to the ClpA/ClpB family. (909 aa)
ACS16863.1Type VI secretion ATPase, ClpV1 family; KEGG: bpt:Bpet4107 putative ATPase with chaperone activity; TIGRFAM: type VI secretion ATPase, ClpV1 family; PFAM: ATPase AAA-2 domain protein; AAA ATPase central domain protein; ATPase associated with various cellular activities AAA_5; Clp domain protein; SMART: AAA ATPase; Belongs to the ClpA/ClpB family. (908 aa)
secBProtein-export protein SecB; One of the proteins required for the normal export of preproteins out of the cell cytoplasm. It is a molecular chaperone that binds to a subset of precursor proteins, maintaining them in a translocation-competent state. It also specifically binds to its receptor SecA. (154 aa)
ACS20776.1KEGG: bac:BamMC406_2972 hypothetical protein. (92 aa)
ureEUreE urease accessory domain protein; Involved in urease metallocenter assembly. Binds nickel. Probably functions as a nickel donor during metallocenter assembly. Belongs to the UreE family. (193 aa)
ACS21249.1Thiol:disulfide interchange protein DsbC; Required for disulfide bond formation in some periplasmic proteins. Acts by transferring its disulfide bond to other proteins and is reduced in the process; Belongs to the thioredoxin family. DsbC subfamily. (240 aa)
htpGHeat shock protein Hsp90; Molecular chaperone. Has ATPase activity. (678 aa)
ACS21848.1KEGG: pol:Bpro_4719 peptidylprolyl isomerase, FKBP-type. (158 aa)
surASurA domain protein; Chaperone involved in the correct folding and assembly of outer membrane proteins. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associated steps of protein maturation. (469 aa)
Your Current Organism:
Variovorax paradoxus S110
NCBI taxonomy Id: 543728
Other names: V. paradoxus S110, Variovorax paradoxus str. S110, Variovorax paradoxus strain S110
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