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
recADNA recombination/repair protein RecA; Can catalyze the hydrolysis of ATP in the presence of single- stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage; Belongs to the RecA family. (346 aa)    
Predicted Functional Partners:
polA
DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity.
 
 0.986
lexA
Repressor LexA; Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
  
 
 0.937
cinA
Competence/damage-inducible protein A; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the CinA family.
  
  
 0.927
AND73330.1
Snf2 family helicase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.901
AND72788.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+.
  
 
 0.884
AND72685.1
Pyruvate:ferredoxin (flavodoxin) oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.868
AND71318.1
DNA polymerase III subunit beta; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of [...]
 
 0.847
recX
Recombination regulator RecX; Modulates RecA activity; Belongs to the RecX family.
  
 
 0.815
frr
Ribosome recycling factor; Responsible for the release of ribosomes from messenger RNA at the termination of protein biosynthesis. May increase the efficiency of translation by recycling ribosomes from one round of translation to another; Belongs to the RRF family.
 
   
 0.797
rpoB
DNA-directed RNA polymerase subunit beta; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
 
 0.795
Your Current Organism:
Enterococcus hirae
NCBI taxonomy Id: 1354
Other names: ATCC 8043, ATCC 9790, CCM 2423, CCUG 18659, CCUG 19917, CFBP 4250, CIP 53.48, DSM 20160, E. hirae, HAMBI 644, IFO 3181, JCM 8729, LMG 6399, LMG:6399, NBRC 3181, NCCB 46070, NCCB 58005, NCIMB 6459, NCTC 12367, strain E.E. Snell strain R
Server load: low (32%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.