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
APR07146.1Amidase. (113 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.
    
  0.903
gatB
Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatB/GatE family. GatB subfamily.
  
 
 0.896
gatC
Glutamyl-tRNA(Gln) amidotransferase subunit C; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatC family.
  
 
 0.799
aspS
Aspartate--tRNA ligase; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
  
 
 0.569
gltX
Glutamate--tRNA ligase; Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily.
  
 
 0.553
APR07148.1
6-aminohexanoate-cyclic-dimer hydrolase.
 
      0.533
APR07907.1
CamS sex pheromone cAM373 precursor.
  
    0.519
ftsZ
Cell division protein FtsZ; Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity.
   
    0.485
guaA
GMP synthase [glutamine-hydrolyzing]; Catalyzes the synthesis of GMP from XMP.
  
  
 0.484
asnS
Asparagine--tRNA ligase.
   
 
 0.459
Your Current Organism:
Lactobacillus parabuchneri
NCBI taxonomy Id: 152331
Other names: ATCC 49374, CCUG 32261, CIP 103368, CIP 106749 [[Lactobacillus ferintoshensis Simpson et al. 2002]], DSM 5707, JCM 12493, JCM 12511 [[Lactobacillus ferintoshensis Simpson et al. 2002]], L. parabuchneri, LMG 11457, LMG:11457, Lactobacillus ferintoshensis, Lactobacillus ferintoshensis Simpson et al. 2002, NBRC 107865, NCDO 2748, NCIMB 8838, strain R7-84 [[Lactobacillus ferintoshensis Simpson et al. 2002]], strain R7-84(T) [[Lactobacillus ferintoshensis Simpson et al. 2002]]
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