STRINGSTRING
ruvC ruvC ruvA ruvA ruvB ruvB polA polA AEF21502.1 AEF21502.1 recX recX tolB tolB AEF21124.1 AEF21124.1 def def AEF21506.1 AEF21506.1 AEF22300.1 AEF22300.1
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
ruvCCrossover junction endodeoxyribonuclease ruvC; Nuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves the cruciform structure in supercoiled DNA by nicking to strands with the same polarity at sites symmetrically opposed at the junction in the homologous arms and leaves a 5'-terminal phosphate and a 3'-terminal hydroxyl group. (174 aa)    
Predicted Functional Partners:
ruvA
Holliday junction ATP-dependent DNA helicase ruvA; 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. RuvA stimulates, in the presence of DNA, the weak ATPase activity of RuvB.
 
 0.996
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.
 
 
 0.980
polA
DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family.
 
   
 0.738
AEF21502.1
UPF0082 protein yeeN; TIGRFAM: Protein of unknown function DUF28; HAMAP: Protein of unknown function DUF28; KEGG: pmy:Pmen_1269 hypothetical protein; PFAM: Protein of unknown function DUF28.
 
  
 0.687
recX
Regulatory protein recX; Modulates RecA activity; Belongs to the RecX family.
  
  
 0.613
tolB
Protein tolB; Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity.
     
 0.570
AEF21124.1
KEGG: pmy:Pmen_3376 exonuclease RecJ; TIGRFAM: Bacterial RecJ exonuclease; PFAM: Phosphoesterase, RecJ-like; Phosphoesterase, DHHA1.
 
 
 
 0.564
def
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.
 
 
 
 0.559
AEF21506.1
KEGG: pmy:Pmen_1273 4-hydroxybenzoyl-CoA thioesterase; TIGRFAM: Tol-Pal system-associated acyl-CoA thioesterase; 4-hydroxybenzoyl-CoA thioesterase; PFAM: Thioesterase superfamily.
     
 0.555
AEF22300.1
KEGG: pen:PSEEN2212 cell division protein FtsK; PFAM: Cell divisionFtsK/SpoIIIE; DNA translocase FtsK gamma; SMART: DNA translocase FtsK gamma.
 
   
 0.548
Your Current Organism:
Pseudomonas fulva
NCBI taxonomy Id: 743720
Other names: P. fulva 12-X, Pseudomonas fulva 12-X, Pseudomonas fulva str. 12-X, Pseudomonas fulva strain 12-X
Server load: low (24%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.