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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene Fusion
Co-occurrence
Co-expression
Experiments
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[Homology]
Score
recRRecombination protein RecR; May play a role in DNA repair. It seems to be involved in an RecBC-independent recombinational process of DNA repair. It may act with RecF and RecO. (190 aa)    
Predicted Functional Partners:
Cla_0113
Conserved hypothetical protein (DUF149 domain protein); Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection.
  
  
 0.911
racR
Two-component response regulator; Pfam matches to PF00072.15 Response_reg, and to PF00486.19 Trans_reg_C.
       0.825
racS
Two-component sensor histidine kinase; Pfam match to PF02518.17 HATPase_c.
       0.825
Cla_0208
Conserved hypothetical protein.
   
 
 0.791
dnaJ
Co-chaperone and heat shock protein; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions be [...]
     
 0.713
por
Pyruvate ferredoxin/flavodoxin oxidoreductase; Pfam matches to PF01855.10 POR_N, and to PF01558.9 POR.
  
 
 0.689
dnaA
Chromosomal replication initiator protein DnaA; Plays an important role in the initiation and regulation of chromosomal replication. Binds to the origin of replication; it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'- TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids. Belongs to the DnaA family.
  
   
 0.614
ftsK
DNA segregation ATPase FtsK/SpoIIIE; Contains possible alternative start; Pfam matches to PF01580.9 FtsK_SpoIIIE, and to PF09397.1 Ftsk_gamma; Belongs to the FtsK/SpoIIIE/SftA family.
 
   
 0.590
dnaX
DNA polymerase III, gamma and tau subunits; DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity.
 
  
 0.563
topA
DNA topoisomerase I; 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 [...]
 
   
 0.562
Your Current Organism:
Campylobacter lari
NCBI taxonomy Id: 306263
Other names: C. lari RM2100, Campylobacter lari RM2100, Campylobacter lari str. RM2100, Campylobacter lari strain RM2100
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.