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:
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Gene Fusion
Cooccurrence
Coexpression
Experiments
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[Homology]
Score
clpP-2Protease subunit of ATP-dependent protease; 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. (200 aa)    
Predicted Functional Partners:
clpX
Endopeptidase Clp ATP-binding regulatory 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.
 
 0.943
AFY96180.1
ATPase with chaperone activity, ATP-binding subunit; PFAM: AAA domain (Cdc48 subfamily); Clp amino terminal domain; C-terminal, D2-small domain, of ClpB protein; ATPase family associated with various cellular activities (AAA); UvrB/uvrC motif; Belongs to the ClpA/ClpB family.
   
 
 0.630
clpB
ATP-dependent chaperone 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.
   
 
 0.629
clpB-2
ATP-dependent chaperone 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.
   
 
 0.600
hrcA
Heat shock gene repressor HrcA; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons.
   
  
 0.564
clpP
Protease subunit of ATP-dependent protease; 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.
 
    
0.515
AFY93995.1
PFAM: Clp protease; TIGRFAM: ATP-dependent Clp protease, proteolytic subunit ClpP; Belongs to the peptidase S14 family.
 
    
0.466
ribBA
GTP cyclohydrolase II/3,4-dihydroxy-2-butanone 4-phosphate synthase; Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate; In the C-terminal section; belongs to the GTP cyclohydrolase II family.
   
 
 0.466
def-2
Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
 
  
 0.449
AFY92157.1
PAS domain S-box; PFAM: CBS domain; Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; GAF domain; Response regulator receiver domain; His Kinase A (phosphoacceptor) domain; PAS fold; TIGRFAM: PAS domain S-box.
  
 
 0.420
Your Current Organism:
Chamaesiphon minutus
NCBI taxonomy Id: 1173020
Other names: C. minutus PCC 6605, Chamaesiphon minutus PCC 6605, Chamaesiphon sp. ACMM 446, Chamaesiphon sp. ATCC 27169, Chamaesiphon sp. PCC 6605
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