STRINGSTRING
dnaK dnaK groEL groEL ilvN ilvN clpX clpX ftsZ ftsZ tuf tuf fabH fabH glgA glgA folB folB rbcL rbcL dnaJ dnaJ soxB soxB apsA apsA
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
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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:
dnaKdnaK protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. (633 aa)
groELChaperonin, 60 kDa; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (545 aa)
ilvNAcetolactate synthase, small subunit; Identified by similarity to GP:5733116; match to protein family HMM PF01842; match to protein family HMM TIGR00119. (159 aa)
clpXATP-dependent Clp protease, ATP-binding subunit 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. (439 aa)
ftsZCell division protein FtsZ; Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity. (434 aa)
tufTranslation elongation factor TU; This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis. (393 aa)
fabH3-oxoacyl-(acyl-carrier-protein) synthase III; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids; Belongs to the thiolase-like superfamily. FabH family. (329 aa)
glgAGlycogen synthase; Synthesizes alpha-1,4-glucan chains using ADP-glucose. (488 aa)
folBDihydroneopterin aldolase; Catalyzes the conversion of 7,8-dihydroneopterin to 6- hydroxymethyl-7,8-dihydropterin. (126 aa)
rbcLRibulose bisphosphate carboxylase, large subunit; May be involved in sulfur metabolism and oxidative stress response. Does not show RuBisCO activity; Belongs to the RuBisCO large chain family. Type IV subfamily. (435 aa)
dnaJdnaJ protein; 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 and Gr [...] (403 aa)
soxBSulfur oxidation protein SoxB; Identified by similarity to EGAD:41987; match to protein family HMM PF02872; match to protein family HMM TIGR01409; Belongs to the 5'-nucleotidase family. (616 aa)
apsAAdenylylsulfate reductase, alpha subunit; Identified by similarity to EGAD:41238; match to protein family HMM PF00890; match to protein family HMM TIGR02061. (658 aa)
Your Current Organism:
Chlorobaculum tepidum
NCBI taxonomy Id: 194439
Other names: C. tepidum TLS, Chlorobaculum tepidum TLS, Chlorobium tepidum TLS
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