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dnaK dnaK surA surA clpB clpB yfgC yfgC ompC ompC yegD yegD ycdY ycdY ompA ompA ompF ompF lolA lolA ompX ompX tolB tolB htpG htpG ppiD ppiD clpX clpX phoE phoE secA secA djlA djlA dnaJ dnaJ ibpA ibpA lamB lamB ibpB ibpB secB secB cbpA cbpA groEL-2 groEL-2 grpE grpE tolB-2 tolB-2 tolC tolC hslO hslO yhgI yhgI
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:
dnaKMolecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. (638 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)
clpBATP-dependent protease, Hsp 100; 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. (857 aa)
yfgCHypothetical protein; Functions as both a chaperone and a metalloprotease. Maintains the integrity of the outer membrane by promoting either the assembly or the elimination of outer membrane proteins, depending on their folding state. (487 aa)
ompCOuter membrane pore protein 1b (Ib;c); Belongs to the Gram-negative porin family. (367 aa)
yegDPutative heat shock protein. (456 aa)
ycdYPutative oxidoreductase component. (184 aa)
ompAOuter membrane protein 3a (II*;G;d); Belongs to the outer membrane OOP (TC 1.B.6) superfamily. (356 aa)
ompFOuter membrane protein 1a. (308 aa)
lolAOuter-membrane lipoprotein carrier protein precursor; 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). (203 aa)
ompXOuter membrane protein X. (170 aa)
tolBTranslocation protein TolB precursor; Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity. TolB occupies a key intermediary position in the Tol-Pal system because it communicates directly with both membrane-embedded components, Pal in the outer membrane and TolA in the inner membrane. (418 aa)
htpGHeat shock protein 90; Molecular chaperone. Has ATPase activity. (624 aa)
ppiDPeptidyl-prolyl cis-trans isomerase D. (624 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)
phoEOuter membrane pore protein E (E,Ic,NmpAB); Belongs to the Gram-negative porin family. (342 aa)
secATranslocase; Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving both as a receptor for the preprotein-SecB complex and as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane. (901 aa)
djlADna-J like membrane chaperone protein; Regulatory DnaK co-chaperone. Direct interaction between DnaK and DjlA is needed for the induction of the wcaABCDE operon, involved in the synthesis of a colanic acid polysaccharide capsule, possibly through activation of the RcsB/RcsC phosphotransfer signaling pathway. The colanic acid capsule may help the bacterium survive conditions outside the host. (275 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)
ibpAHeat shock protein; Associates with aggregated proteins, together with IbpB, to stabilize and protect them from irreversible denaturation and extensive proteolysis during heat shock and oxidative stress. Aggregated proteins bound to the IbpAB complex are more efficiently refolded and reactivated by the ATP-dependent chaperone systems ClpB and DnaK/DnaJ/GrpE. Its activity is ATP-independent. (152 aa)
lamBMaltoporin precursor; Involved in the transport of maltose and maltodextrins. Belongs to the porin LamB (TC 1.B.3) family. (429 aa)
ibpBHeat shock protein; Associates with aggregated proteins, together with IbpA, to stabilize and protect them from irreversible denaturation and extensive proteolysis during heat shock and oxidative stress. Aggregated proteins bound to the IbpAB complex are more efficiently refolded and reactivated by the ATP-dependent chaperone systems ClpB and DnaK/DnaJ/GrpE. Its activity is ATP-independent. (142 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)
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)
grpEHsp 24 nucleotide exchange factor; 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 roun [...] (196 aa)
tolB-2Translocation protein TolB precursor. (391 aa)
tolCOuter membrane channel precursor protein. (492 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)
yhgIMembrane-bound protein in GNT I transport system; Involved in iron-sulfur cluster biogenesis. Binds a 4Fe-4S cluster, can transfer this cluster to apoproteins, and thereby intervenes in the maturation of Fe/S proteins. Could also act as a scaffold/chaperone for damaged Fe/S proteins. (191 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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