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cpn10 cpn10 htpG htpG secB secB cbpA cbpA clpB clpB fkpB fkpB fliT fliT dsbB dsbB BP1428 BP1428 BP1471 BP1471 BP1525 BP1525 tig tig clpX clpX hscB hscB hscA hscA fimB fimB ppiB ppiB hslO hslO dnaJ dnaJ dnaK dnaK grpE grpE ureE ureE dsbC dsbC surA surA cpn60 cpn60
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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:
cpn1010 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. (95 aa)
htpGtRNA-Leu; Molecular chaperone. Has ATPase activity. (635 aa)
secBProtein-export protein; 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. (175 aa)
cbpASimilar to Escherichia coli curved DNA-binding protein CbpA or B1000 SW:CBPA_ECOLI (P36659) (306 aa) fasta scores: E(): 2.9e-26, 41.772% id in 316 aa, and to Caulobacter crescentus DnaJ family protein cc2772 TR:Q9A4Q8 (EMBL:AE005942) (314 aa) fasta scores: E(): 4.2e-31, 41.742% id in 333 aa. (312 aa)
clpBATP-dependent protease, ATPase subunit; 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. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Belongs to the ClpA/ClpB [...] (865 aa)
fkpBSimilar to Escherichia coli, and FkbP-type 16 kDa peptidyl-prolyl cis-trans isomerase FkbP or SlpA or B0028 or Z0033 or Ecs0031 SW:FKBX_ECOLI (P22563) (148 aa) fasta scores: E(): 5.9e-11, 33.56% id in 146 aa, and to Vibrio cholerae peptidyl-prolyl cis-trans isomerase, FkbP-type Vc0684 TR:Q9KU45 (EMBL:AE004154) (144 aa) fasta scores: E(): 5.4e-14, 38.35% id in 146 aa. (151 aa)
fliTHypothetical protein (Pseudogene); (CCAA)2 in pertussis; (CCAA)1 in parapertussis. (116 aa)
dsbBSimilar to Escherichia coli disulfide bond formation protein B DsbB or RoxB or B1185 or Z1948 or Ecs1680 SW:DSBB_ECOLI (P30018) (176 aa) fasta scores: E(): 3.1e-05, 28.47% id in 144 aa, and to Pseudomonas aeruginosa disulfide bond formation protein B 1 DsbB1 or Pa5256 SW:DSB1_PSEAE (P21482) (163 aa) fasta scores: E(): 8.3e-08, 30.57% id in 157 aa. (158 aa)
BP1428Similar to Salmonella typhimurium outer membrane protein OmpH precursor OmpH SW:OMPH_SALTY (P16974) (161 aa) fasta scores: E(): 3.6e-06, 28.84% id in 156 aa, and to Neisseria meningitidis putative outer membrane protein Nma0086 TR:Q9JX30 (EMBL:AL162752) (166 aa) fasta scores: E(): 8.9e-13, 39.63% id in 164 aa; Belongs to the skp family. (187 aa)
BP1471Conserved hypothetical protein; Similar to Vibrio cholerae chaperone, formate dehydrogenase-specific, putative Vc1515 TR:Q9KRW9 (EMBL:AE004230) (218 aa) fasta scores: E(): 1.1e-21, 43.54% id in 186 aa, and to Vibrio cholerae TorD protein Vc1720 TR:Q9KRC2 (EMBL:AE004250) (220 aa) fasta scores: E(): 0.0061, 25% id in 204 aa. (209 aa)
BP1525Putative membrane protein; Similar to Agrobacterium tumefaciens Agr_l_2587p TR:AAK89860 (EMBL:AE008329) (171 aa) fasta scores: E(): 0.96, 29.03% id in 155 aa. (159 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. (436 aa)
clpXATP-dependent Clp 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. (434 aa)
hscBChaperone 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. (170 aa)
hscAChaperone protein; Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB. (620 aa)
fimBFimbrial protein (pseudogene); Required for the biogenesis of the filamentous hemagglutinin and the fimbria; Belongs to the periplasmic pilus chaperone family. (244 aa)
ppiBPeptidyl-prolyl cis-trans isomerase 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. (169 aa)
hslOPutative 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. (304 aa)
dnaJMolecular chaperone; 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 [...] (385 aa)
dnaKMolecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. (641 aa)
grpEPutative GrpE chaperone; 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- [...] (184 aa)
ureEUrease accessory protein (Pseudogene); Involved in urease metallocenter assembly. Binds nickel. Probably functions as a nickel donor during metallocenter assembly. Belongs to the UreE family. (204 aa)
dsbCPutative thiol:disulphide interchange protein (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 (By similarity). Necessary for extracellular secretion of the pertussis toxin (PTX); Belongs to the thioredoxin family. DsbC subfamily. (279 aa)
surAPutative peptidyl-prolyl cis-trans isomerase; 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. (519 aa)
cpn6060 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (547 aa)
Your Current Organism:
Bordetella pertussis
NCBI taxonomy Id: 257313
Other names: B. pertussis Tohama I, Bordetella pertussis Tohama I
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