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
recJsingle-stranded-DNA exonuclease RecJ; Derived by automated computational analysis using gene prediction method: Protein Homology. (760 aa)    
Predicted Functional Partners:
AJC95780.1
single-stranded-DNA-specific exonuclease RecJ; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 
0.929
apt
Adenine phosphoribosyltransferase; Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
  
    0.878
secDF
Preprotein translocase subunit SecD/SecF; Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA; Belongs to the SecD/SecF family. SecD subfamily.
     
 0.829
recQ-1
ATP-dependent DNA helicase RecQ-1; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
 0.818
dtd
D-tyrosyl-tRNA(Tyr) deacylase; An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA- based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D- aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl- tRNA entities in vivo and helps enforce protein L-homochirality. Belongs to the DTD family.
 
     0.771
relA
GTP pyrophosphokinase; In eubacteria ppGpp (guanosine 3'-diphosphate 5-' diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance.
  
    0.761
AJC96023.1
N-acetylmuramoyl-L-alanine amidase; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.737
ruvB
Holliday junction ATP-dependent DNA helicase RuvB; The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing.
 
  
 0.687
priA
Primosomal protein N; Involved in the restart of stalled replication forks. Recognizes and binds the arrested nascent DNA chain at stalled replication forks. It can open the DNA duplex, via its helicase activity, and promote assembly of the primosome and loading of the major replicative helicase DnaB onto DNA; Belongs to the helicase family. PriA subfamily.
 
     0.680
xseA
Exodeoxyribonuclease VII large subunit; Bidirectionally degrades single-stranded DNA into large acid- insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides; Belongs to the XseA family.
  
  
 0.657
Your Current Organism:
Staphylococcus hyicus
NCBI taxonomy Id: 1284
Other names: ATCC 11249, CCM 2368, CCUG 6509, CIP 81.58, DSM 20459, JCM 2423, LMG 13352, LMG:13352, Micrococcus hyicus, NCTC 10350, S. hyicus, Staphylococcus hyicus hyicus, Staphylococcus hyicus subsp. hyicus
Server load: low (12%) [HD]