STRINGSTRING
dnaK dnaK dnaJ dnaJ fkpB fkpB surA surA djlA djlA KPN_00128 KPN_00128 hlpA hlpA stbE stbE stbB stbB KPN_00276 KPN_00276 yagY yagY tig tig clpX clpX htpG htpG ppiB ppiB KPN_00492 KPN_00492 dsbG dsbG spy spy KPN_01328 KPN_01328 ynfI ynfI KPN_01672 KPN_01672 dsbB dsbB yegD yegD yfgC yfgC hscA hscA hscB hscB clpB clpB grpE grpE fim fim fim-3 fim-3 KPN_03278 KPN_03278 fimC fimC dsbC dsbC scsC scsC fim-6 fim-6 fim-7 fim-7 fim-10 fim-10 ureE ureE fkpA fkpA KPN_04511 KPN_04511 cbpA cbpA groEL groEL KPN_04472 KPN_04472 cpxP cpxP secB secB hslO hslO ppiA ppiA slyD slyD fklB fklB KPN_04541 KPN_04541 groEL-2 groEL-2 groES groES
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)
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)
fkpBFKBP-type peptidyl-prolyl cis-trans isomerase (rotamase). (149 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)
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)
KPN_00128Hypothetical protein. (731 aa)
hlpAPeriplasmic molecular chaperone for outer membrane proteins; Belongs to the skp family. (148 aa)
stbEPutative fimbriae; chaparone. (244 aa)
stbBPutative fimbriae; chaparone. (252 aa)
KPN_00276Putative fimbrial chaparone. (232 aa)
yagYHypothetical protein; Part of the ecpRABCDE operon, which encodes the E.coli common pilus (ECP). ECP plays a dual role in early-stage biofilm development and host cell recognition (By similarity); Belongs to the EcpB/EcpE family. (222 aa)
tigTrigger 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. (432 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)
ppiBPeptidyl-prolyl cis-trans isomerase B (rotamase B); 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. (176 aa)
KPN_00492Probable pilin chaperone; Similar to PapD. (231 aa)
dsbGDisulfide isomerase, thiol-disulphide oxidase, periplasmic; Required for disulfide bond formation in some periplasmic proteins. Acts by transferring its disulfide bond to other proteins and is reduced in the process; Belongs to the thioredoxin family. DsbC subfamily. (206 aa)
spyPeriplasmic protein; Related to spheroblast formation. (161 aa)
KPN_01328Putative protease; Belongs to the ClpA/ClpB family. (866 aa)
ynfIPutative dimethyl sulfoxide reductase component; Required for biogenesis/assembly of DMSO reductase, but not for the interaction of the DmsA signal peptide with the Tat system. May be part of a chaperone cascade complex that facilitates a folding- maturation pathway for the substrate protein. (202 aa)
KPN_01672Putative fimbrial chaperone. (231 aa)
dsbBDisulfide bond formation protein B; Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein; Belongs to the DsbB family. (159 aa)
yegDPutative heat shock protein. (456 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)
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)
hscBCo-chaperone HscB; 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. (171 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)
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)
fimProbable pilin chaperone; Similar to PapD. (222 aa)
fim-3Putative chaperone. (220 aa)
KPN_03278Putative bacterial pili assembly chaperone. (233 aa)
fimCPeriplasmic chaperone; Required for type 1 fimbriae. (228 aa)
dsbCProtein disulfide isomerase II; Required for disulfide bond formation in some periplasmic proteins. Acts by transferring its disulfide bond to other proteins and is reduced in the process; Belongs to the thioredoxin family. DsbC subfamily. (237 aa)
scsCSuppression of copper sensitivity protein; Lipoprotein modification in lgt mutants of E. coli. (203 aa)
fim-6Putative bacterial pili assembly chaperone. (236 aa)
fim-7Putative fimbrial chaperone. (264 aa)
fim-10Putative fimbrial chaperone. (243 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)
fkpAFKBP-type peptidyl-prolyl cis-trans isomerase (rotamase). (276 aa)
KPN_04511Putative DSBA oxidoreductase. (261 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)
groELChaperonin GroEL. (318 aa)
KPN_04472Putative chaperone. (229 aa)
cpxPPeriplasmic repressor of cpx regulon by interaction with CpxA. (167 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)
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)
ppiAPeptidyl-prolyl cis-trans isomerase A (rotamase A); 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. (189 aa)
slyDFKBP-type peptidyl prolyl cis-trans isomerase (rotamase). (195 aa)
fklBFKBP-type 22KD peptidyl-prolyl cis-trans isomerase (rotamase). (226 aa)
KPN_04541Periplasmic chaperone, required for type 1 fimbriae. (228 aa)
groEL-2Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (548 aa)
groESCo-chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. (97 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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