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
mobBMobilization protein MobB; Relaxases/mobilisation proteins are required for the horizontal transfer of genetic information contained on plasmids that occurs during bacterial conjugation; Localized in the cytoplasm; Family membership. (283 aa)    
Predicted Functional Partners:
traP
TraP is part of a conjugative transposon ans is predicted as a transfer primase. Contains an N-terminal CHC2 (CycHisCysCys type) zinc finger domain suggesting that this protein binds to substrates as DNA, RNA. Localized in the cytoplasm; Function unclear.
 
  
 0.952
traA
TraA is part of a conjugative transposon and is predicted to be involved in its transfer. Belongs to the CobQ/CobB/MinD/ParA nucleotide binding protein family. Localized in the cytoplasm; Function unclear.
 
   
 0.812
CAZ96857.1
Conserved hypothetical protein; Localized in the cytoplasm.
       0.790
CAZ96855.1
Hypothetical membrane protein; Contains a transmembrane helix; Localized in the cytoplasmic membrane; Hypothetical protein.
       0.773
dnaN
DNA polymerase III, beta chain; 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 r [...]
  
 
 0.635
CAZ96853.1
Conserved protein adopting a a ribbon-helix-helix core topology consisting of four helices in an open array of two hairpins. Such domains are found in several bacterial and phage repressors. Localized in the cytoplasm; Family membership.
       0.618
recB
Exodeoxyribonuclease V, beta chain; The Exonuclease V is a multifunctional nuclease required for efficient DNA repair. It catalyzes the unwinding of double-stranded DNA and the cleavage of single-stranded DNA and it stimulates local genetic recombination. All of these activities require concomitant hydrolysis of ATP; Belongs to the helicase family, UvrD subfamily; Localized in the cytoplasm; High confidence in function and specificity.
  
 
 0.610
CAZ96859.1
Hypothetical protein; Localized in the cytoplasm.
       0.578
CAZ96860.1
Hypothetical protein; Localized in the cytoplasm.
       0.578
truB
tRNA pseudouridine synthase B; Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs; Belongs to the pseudouridine synthase TruB family. Type 1 subfamily.
   
 
  0.554
Your Current Organism:
Zobellia galactanivorans
NCBI taxonomy Id: 63186
Other names: CCUG 47099, CIP 106680, Cytophaga drobachiensis, DSM 12802, Flavobacterium droebachense, Pseudomonas droebachense, Z. galactanivorans, Zobellia galactanivorans corrig. Barbeyron et al. 2001, Zobellia galactanovorans, strain Dsij
Server load: low (22%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.