STRINGSTRING
htpG htpG dnaK dnaK grpE grpE AGP34356.1 AGP34356.1 dnaJ dnaJ ureD ureD ureE ureE ureF ureF ureG ureG yidC yidC groS groS groEL groEL tig tig clpX clpX lifO lifO AGP37109.1 AGP37109.1 clpA clpA rimM rimM AGP32621.1 AGP32621.1 AGP38489.1 AGP38489.1 dnaJ-2 dnaJ-2 groS-2 groS-2 groEL-2 groEL-2 groEL-3 groEL-3 AGP39939.1 AGP39939.1 AGP40341.1 AGP40341.1 hscB hscB hscA hscA AGP32888.1 AGP32888.1 clpB clpB clpA-2 clpA-2 dnaK-3 dnaK-3
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:
htpGHypothetical protein; Molecular chaperone. Has ATPase activity. (666 aa)
dnaKMolecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. (620 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 [...] (194 aa)
AGP34356.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. (338 aa)
dnaJHypothetical 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, Dna [...] (331 aa)
ureDHypothetical protein; Required for maturation of urease via the functional incorporation of the urease nickel metallocenter. (284 aa)
ureEHypothetical protein; Involved in urease metallocenter assembly. Binds nickel. Probably functions as a nickel donor during metallocenter assembly. Belongs to the UreE family. (192 aa)
ureFHypothetical protein; Required for maturation of urease via the functional incorporation of the urease nickel metallocenter. (226 aa)
ureGUrease accessory protein UreG; Facilitates the functional incorporation of the urease nickel metallocenter. This process requires GTP hydrolysis, probably effectuated by UreG. (214 aa)
yidCHypothetical protein; Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispanning membrane proteins. (614 aa)
groSMolecular chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. (98 aa)
groELMolecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (562 aa)
tigHypothetical protein; 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. (410 aa)
clpXATP-dependent protease; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. (418 aa)
lifOHypothetical protein; May be involved in the folding of the extracellular lipase during its passage through the periplasm; Belongs to the lipase chaperone family. (335 aa)
AGP37109.1Hypothetical protein; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. (414 aa)
clpAATP-dependent Clp protease ATP-binding protein; 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. (778 aa)
rimMRibosome maturation factor RimM; An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Probably interacts with S19. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes; Belongs to the RimM family. (170 aa)
AGP32621.1ATPase AAA; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the ClpA/ClpB family. (899 aa)
AGP38489.1Hypothetical protein; Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane). (229 aa)
dnaJ-2Hypothetical 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, Dna [...] (359 aa)
groS-2Molecular chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. (96 aa)
groEL-2Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (542 aa)
groEL-3Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (539 aa)
AGP39939.1Hypothetical protein; Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane). (192 aa)
AGP40341.1Hypothetical protein; Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane). (206 aa)
hscBHypothetical protein; 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. (178 aa)
hscAChaperone protein HscA; Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB. (669 aa)
AGP32888.1Protein disaggregation chaperone; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the ClpA/ClpB family. (870 aa)
clpBProtein disaggregation chaperone; 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. (869 aa)
clpA-2ATP-dependent Clp protease ATP-binding protein; 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. (916 aa)
dnaK-3Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. (638 aa)
Your Current Organism:
Sorangium cellulosum So01572
NCBI taxonomy Id: 1254432
Other names: S. cellulosum So0157-2, Sorangium cellulosum So0157-2
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