STRINGSTRING
clpX clpX hslV hslV hslU hslU htpG htpG lon lon groEL groEL groES groES KGL13142.1 KGL13142.1 KGL13253.1 KGL13253.1 cbpA cbpA hspR hspR KGL12835.1 KGL12835.1 KGL12930.1 KGL12930.1 KGL12969.1 KGL12969.1 clpP clpP dnaJ dnaJ hrcA hrcA grpE grpE dnaK dnaK KGL12669.1 KGL12669.1 groEL-2 groEL-2 KGL12675.1 KGL12675.1 KGL12716.1 KGL12716.1
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:
clpXClp protease 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. (426 aa)
hslVPeptidase; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. (182 aa)
hslUATP-dependent protease; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. (445 aa)
htpGMolecular chaperone Hsp90; Molecular chaperone. Has ATPase activity. (613 aa)
lonLon protease; 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. (865 aa)
groELMolecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (545 aa)
groESMolecular chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. (89 aa)
KGL13142.1Amino acid permease; Derived by automated computational analysis using gene prediction method: Protein Homology. (417 aa)
KGL13253.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (120 aa)
cbpACobalamin ABC transporter permease; Derived by automated computational analysis using gene prediction method: Protein Homology. (163 aa)
hspRMerR family transcriptional regulator; Derived by automated computational analysis using gene prediction method: Protein Homology. (122 aa)
KGL12835.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (260 aa)
KGL12930.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (400 aa)
KGL12969.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (837 aa)
clpPClp protease; 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. (193 aa)
dnaJMolecular chaperone 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, [...] (366 aa)
hrcAHypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (273 aa)
grpEHeat shock protein 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- [...] (180 aa)
dnaKMolecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. (629 aa)
KGL12669.1Molecular chaperone GroES; Derived by automated computational analysis using gene prediction method: Protein Homology. (89 aa)
groEL-2Molecular chaperone GroEL; 60 kDa chaperone family; promotes refolding of misfolded polypeptides especially under stressful conditions; forms two stacked rings of heptamers to form a barrel-shaped 14mer; ends can be capped by GroES; misfolded proteins enter the barrel where they are refolded when GroES binds; many bacteria have multiple copies of the groEL gene which are active under different environmental conditions; the B.japonicum protein in this cluster is expressed constitutively; in Rhodobacter, Corynebacterium and Rhizobium this protein is essential for growth; Derived by autom [...] (545 aa)
KGL12675.1Lon protease; Derived by automated computational analysis using gene prediction method: Protein Homology. (865 aa)
KGL12716.1Molecular chaperone Hsp90; Derived by automated computational analysis using gene prediction method: Protein Homology. (613 aa)
Your Current Organism:
Helicobacter muridarum
NCBI taxonomy Id: 216
Other names: ATCC 49282, CCUG 29262, CIP 104248, DSM 22221, H. muridarum, LMG 13646, LMG:13646, NCTC 12714, strain ST1
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