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dnaK dnaK dnaJ dnaJ surA surA hlpA hlpA clpX clpX htpG htpG spy spy narW narW narJ narJ hscA hscA ureE ureE hdeB-2 hdeB-2 KPN_03534 KPN_03534 hslO hslO secB secB cpxP cpxP groEL groEL cbpA cbpA groEL-2 groEL-2
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:
dnaKMolecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. (638 aa)
dnaJChaperone with DnaK; 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 [...] (377 aa)
surAPeptidyl-prolyl cis-trans isomerase (PPIase); 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. (428 aa)
hlpAPeriplasmic molecular chaperone for outer membrane proteins; Belongs to the skp family. (148 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. (424 aa)
htpGHeat shock protein 90; Molecular chaperone. Has ATPase activity. (624 aa)
spyPeriplasmic protein; Related to spheroblast formation. (161 aa)
narWCryptic nitrate reductase 2 delta subunit. (231 aa)
narJNitrate reductase 1, delta subunit, assembly function. (236 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. Involved in the maturation of IscU. (616 aa)
ureEUrease accessory protein ureE; Involved in urease metallocenter assembly. Binds nickel. Probably functions as a nickel donor during metallocenter assembly. Belongs to the UreE family. (158 aa)
hdeB-2Hypothetical protein; Required for optimal acid stress protection, which is important for survival of enteric bacteria in the acidic environment of the host stomach. Exhibits a chaperone-like activity at acidic pH by preventing the aggregation of many different periplasmic proteins. Belongs to the HdeB family. (101 aa)
KPN_03534Periplasmic protein; Related to spheroblast formation. (136 aa)
hslOHsp33-like chaperonin; 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. (294 aa)
secBExport 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. (155 aa)
cpxPPeriplasmic repressor of cpx regulon by interaction with CpxA. (167 aa)
groELChaperonin GroEL. (318 aa)
cbpAPutative chaperone DnaJ; DNA-binding protein that preferentially recognizes a curved DNA sequence. It is probably a functional analog of DnaJ; displays overlapping activities with DnaJ, but functions under different conditions, probably acting as a molecular chaperone in an adaptive response to environmental stresses other than heat shock. Lacks autonomous chaperone activity; binds native substrates and targets them for recognition by DnaK. Its activity is inhibited by the binding of CbpM. (305 aa)
groEL-2Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (548 aa)
Your Current Organism:
Klebsiella pneumoniae MGH78578
NCBI taxonomy Id: 272620
Other names: K. pneumoniae subsp. pneumoniae MGH 78578, Klebsiella pneumoniae MCG 78578, Klebsiella pneumoniae str. MCG 78578, Klebsiella pneumoniae subsp. pneumoniae ATCC 700721, Klebsiella pneumoniae subsp. pneumoniae MGH 78578, Klebsiella pneumoniae subsp. pneumoniae str. MGH 78578, Klebsiella pneumoniae subsp. pneumoniae strain MGH 78578
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