STRINGSTRING
TMO_0337 TMO_0337 groL groL groS groS ureE ureE TMO_1773 TMO_1773 surA surA clpX clpX tig tig ppi ppi TMO_2108 TMO_2108 cbpA cbpA htpG htpG TMO_3180 TMO_3180 hslO hslO clpB clpB yegD yegD secB secB grpE grpE dnaK dnaK dnaJ dnaJ TMO_0576 TMO_0576 TMO_0588 TMO_0588 TMO_0986 TMO_0986
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.
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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
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:
TMO_0337Heat shock protein DnaJ. (203 aa)
groLGroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (548 aa)
groSChaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. (96 aa)
ureEUrease accessory protein; Involved in urease metallocenter assembly. Binds nickel. Probably functions as a nickel donor during metallocenter assembly. Belongs to the UreE family. (281 aa)
TMO_1773Outer membrane protein. (195 aa)
surAParvulin-like peptidyl-prolyl isomerase. (426 aa)
clpXATP-dependent 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. (422 aa)
tigFKBP-type peptidyl-prolyl cis-trans isomerase (trigger 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. (452 aa)
ppiPeptidyl-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. (191 aa)
TMO_2108Peptidyl-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. (159 aa)
cbpACurved DNA-binding protein. (332 aa)
htpGChaperone protein htpG; Molecular chaperone. Has ATPase activity. (648 aa)
TMO_3180Disulfide bond formation protein, DsbB family. (181 aa)
hslOMolecular chaperone Hsp33; 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. (328 aa)
clpBATP-dependent Clp protease ATP-binding subunit; 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. (865 aa)
yegDChaperone protein yegD. (432 aa)
secBPreprotein translocase subunit 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. (160 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 [...] (206 aa)
dnaKMolecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. (642 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 [...] (393 aa)
TMO_0576Heat shock protein DnaJ-like protein. (258 aa)
TMO_0588ATP-dependent Clp protease ATP-binding subunit ClpA; Belongs to the ClpA/ClpB family. (801 aa)
TMO_0986Curved DNA-binding protein. (298 aa)
Your Current Organism:
Tistrella mobilis
NCBI taxonomy Id: 1110502
Other names: T. mobilis KA081020-065, Tistrella mobilis KA081020-065, Tistrella mobilis str. KA081020-065, Tistrella mobilis strain KA081020-065
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