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
mcsBArginine kinase; Catalyzes the specific phosphorylation of arginine residues in proteins; Belongs to the ATP:guanido phosphotransferase family. (340 aa)    
Predicted Functional Partners:
AGK99253.1
Hypothetical protein; PFAM: UvrB/uvrC motif.
 
  
 0.997
AGK99251.1
ATPase with chaperone activity, ATP-binding subunit; PFAM: AAA domain (Cdc48 subfamily); C-terminal, D2-small domain, of ClpB protein; Clp amino terminal domain; ATPase family associated with various cellular activities (AAA); UvrB/uvrC motif; Belongs to the ClpA/ClpB family.
 
 
 0.971
AGK99254.1
PFAM: Firmicute transcriptional repressor of class III stress genes (CtsR); Belongs to the CtsR family.
 
  
 0.954
radA
DNA repair protein RadA; DNA-dependent ATPase involved in processing of recombination intermediates, plays a role in repairing DNA breaks. Stimulates the branch migration of RecA-mediated strand transfer reactions, allowing the 3' invading strand to extend heteroduplex DNA faster. Binds ssDNA in the presence of ADP but not other nucleotides, has ATPase activity that is stimulated by ssDNA and various branched DNA structures, but inhibited by SSB. Does not have RecA's homology-searching function.
  
    0.792
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.
  
 
 0.783
AGK96531.1
ATP-dependent Clp protease ATP-binding subunit clpA; PFAM: AAA domain (Cdc48 subfamily); C-terminal, D2-small domain, of ClpB protein; Clp amino terminal domain; ATPase family associated with various cellular activities (AAA); TIGRFAM: ATP-dependent Clp protease ATP-binding subunit clpA; Belongs to the ClpA/ClpB family.
  
 
 0.771
disA
Putative nucleic-acid-binding protein (contains the HHH domain); Has also diadenylate cyclase activity, catalyzing the condensation of 2 ATP molecules into cyclic di-AMP (c-di-AMP). c-di-AMP acts as a signaling molecule that couples DNA integrity with progression of sporulation. The rise in c-di-AMP level generated by DisA while scanning the chromosome, operates as a positive signal that advances sporulation; upon encountering a lesion, the DisA focus arrests at the damaged site and halts c-di-AMP synthesis.
  
    0.712
AGK95446.1
Protein-tyrosine-phosphatase; PFAM: Low molecular weight phosphotyrosine protein phosphatase.
  
  
 0.674
AGK99255.1
Hypothetical protein.
       0.541
clpP
ATP-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.
   
  
 0.538
Your Current Organism:
Clostridium pasteurianum
NCBI taxonomy Id: 86416
Other names: C. pasteurianum BC1, Clostridia isolate BC1, Clostridium pasteurianum BC1, Clostridium pasteurianum str. BC1, Clostridium pasteurianum strain BC1, Clostridium sp. ATCC 53464, Clostridium sp. BC1
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.