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
APR07513.1Exodeoxyribonuclease. (252 aa)    
Predicted Functional Partners:
birA
Bifunctional ligase/repressor BirA; Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a repressor; Belongs to the biotin--protein ligase family.
  
    0.704
polA
DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity.
  
 0.693
APR07226.1
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 [...]
   
 0.631
APR08554.1
Ribosomal large subunit pseudouridine synthase B; Belongs to the pseudouridine synthase RsuA family.
  
    0.616
nfo
Putative endonuclease 4; Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic sites (AP sites) to produce new 5'-ends that are base-free deoxyribose 5-phosphate residues. It preferentially attacks modified AP sites created by bleomycin and neocarzinostatin.
    
 
 0.575
APR07512.1
Hypothetical protein.
       0.553
APR08490.1
Putative A/G-specific adenine glycosylase YfhQ; Adenine glycosylase active on G-A mispairs.
    
 0.532
APR07142.1
Succinyl-diaminopimelate desuccinylase.
      0.519
topA
DNA topoisomerase 1; Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA- (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supe [...]
  
  
 0.494
metG
Methionine--tRNA ligase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation; Belongs to the class-I aminoacyl-tRNA synthetase family. MetG type 2B subfamily.
  
  
 0.408
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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