STRINGSTRING
ABD29650.1 ABD29650.1 ctsR ctsR mcsA mcsA mcsB mcsB clpC clpC clpP clpP clpB clpB mecA mecA ABD30753.1 ABD30753.1 ABD30754.1 ABD30754.1 prmA prmA dnaJ dnaJ dnaK dnaK grpE grpE hrcA hrcA ABD30760.1 ABD30760.1 ABD30761.1 ABD30761.1 clpX clpX groL groL groS groS ABD31492.1 ABD31492.1 ABD31678.1 ABD31678.1 clpL clpL
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:
ABD29650.1Conserved hypothetical protein. (404 aa)
ctsRConserved hypothetical protein; Negative regulator of clpC, clpB and clpP transcription by binding directly and specifically to their promoter region. (153 aa)
mcsAUvrB/uvrC motif domain protein; Activates the phosphorylation activity of the protein- arginine kinase McsB (By similarity). May function as an important molecule for oxidative tolerance in various types of stress including that of heavy metals. Binds to Cu(2+), Zn(2+), Co(2+) and Cd(2+) via its CXXC metal binding motifs. (162 aa)
mcsBATP:guanido phosphotransferase, C-terminal catalytic domain protein; Catalyzes the specific phosphorylation of arginine residues in proteins (By similarity). Is required for stress tolerance and virulence in S.aureus. Acts as a modulator of the repressor activity of CtsR upon heavy metal and oxidative stress caused by these metal ions. (335 aa)
clpCEndopeptidase, putative; Required for growth at high temperatures, probably by acting as a chaperone during heat shock and targeting heat-denatured proteins for degradation by ClpP. Required for biofilm formation. May act as a chaperone regulating CtsR activity. (818 aa)
clpPATP-dependent Clp protease, proteolytic subunit ClpP; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. (195 aa)
clpBATP-dependent Clp protease, ATP-binding subunit ClpB; 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. (869 aa)
mecAConserved hypothetical protein; Enables the recognition and targeting of unfolded and aggregated proteins to the ClpC protease or to other proteins involved in proteolysis. (239 aa)
ABD30753.1Conserved hypothetical protein. (448 aa)
ABD30754.1Conserved hypothetical protein; Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit. (250 aa)
prmARibosomal protein L11 methyltransferase; Methylates ribosomal protein L11; Belongs to the methyltransferase superfamily. PrmA family. (312 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 [...] (379 aa)
dnaKDNAk protein, putative; Acts as a chaperone; Belongs to the heat shock protein 70 family. (610 aa)
grpECo-chaperone GrpE; 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-depend [...] (208 aa)
hrcAHeat-inducible transcription repressor HrcA; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. (325 aa)
ABD30760.1Conserved hypothetical protein; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. (374 aa)
ABD30761.1Conserved hypothetical protein. (42 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. (420 aa)
groLChaperonin, 60 kDa, GrpEL, putative; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (538 aa)
groSChaperonin, 10 kDa, GroES, putative; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. (94 aa)
ABD31492.1Conserved hypothetical protein. (378 aa)
ABD31678.1Conserved hypothetical protein; Belongs to the small heat shock protein (HSP20) family. (142 aa)
clpLATP-dependent Clp protease, ATP-binding subunit ClpC, putative; Required for the development of induced thermotolerance and intracellular multiplication within bovine mammary epithelial cells. (701 aa)
Your Current Organism:
Staphylococcus aureus
NCBI taxonomy Id: 93061
Other names: S. aureus subsp. aureus NCTC 8325, Staphylococcus aureus NCTC 8325, Staphylococcus aureus subsp. aureus NCTC 8325, Staphylococcus aureus subsp. aureus str. NCTC 8325, Staphylococcus aureus subsp. aureus strain NCTC 8325
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