STRINGSTRING
STRING protein interaction network
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:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
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. (416 aa)    
Predicted Functional Partners:
clpP1
ATP-dependent Clp protease proteolytic subunit 1; 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.
 
 0.997
clpP2
ATP-dependent Clp protease proteolytic subunit 2 (Endopeptidase Clp 2); 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.
 
 0.991
tig
Trigger factor (TF); 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.
 
  
 0.898
tepA
Protein export-enhancing factor; Experimentally verified as part of mature spore proteome PMID:19542279; Belongs to the peptidase S14 family.
  
 
 0.893
atpD1
ATP synthase subunit beta (ATPase subunit beta) (ATP synthase F1 sector subunit beta); Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits; Belongs to the ATPase alpha/beta chains family.
 
    
 0.861
msrAB
Peptide methionine sulfoxide reductase MsrA/MsrB; Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
  
 
 0.852
lon
ATP-dependent protease La, S16 peptidase family; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner.
 
 
 0.828
hfq
Hfq-like RNA chaperone; RNA chaperone that binds small regulatory RNA (sRNAs) and mRNAs to facilitate mRNA translational regulation in response to envelope stress, environmental stress and changes in metabolite concentrations. Also binds with high specificity to tRNAs. Belongs to the Hfq family.
   
  
 0.786
groL
60 kDa chaperonin (Protein Cpn60) (GroEL protein); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 
 0.758
clpB
Chaperone protein; 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.
  
 
 0.758
Your Current Organism:
Clostridioides difficile
NCBI taxonomy Id: 272563
Other names: C. difficile 630, Clostridioides difficile 630, Clostridium difficile 630, Clostridium difficile 630 (epidemic type X), Clostridium difficile str. 630, Clostridium difficile strain 630, Peptoclostridium difficile 630
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