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
Databases
Textmining
[Homology]
Score
dinBDNA polymerase IV; Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII. (376 aa)    
Predicted Functional Partners:
recA
Recombinase RecA; Can catalyze the hydrolysis of ATP in the presence of single- stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage; Belongs to the RecA family.
  
 0.894
lexA
Repressor LexA; Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
  
 
 0.874
dnaN
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 [...]
   
 0.869
APD13582.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+.
  
  
 0.867
AJC22649.1
Peptidase S24; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the peptidase S24 family.
  
 
 0.774
ftsW
Cell division protein FtsW; Peptidoglycan polymerase that is essential for cell division. Belongs to the SEDS family. FtsW subfamily.
  
 
 0.715
mrdB
Rod shape-determining protein RodA; Peptidoglycan polymerase that is essential for cell wall elongation; Belongs to the SEDS family. MrdB/RodA subfamily.
  
 
 0.710
sapB_1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.702
alkA_2
Adenosine deaminase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.696
dnaE_2
Error-prone DNA polymerase; DNA polymerase involved in damage-induced mutagenesis and translesion synthesis (TLS). It is not the major replicative DNA polymerase.
  
  
 0.690
Your Current Organism:
Pandoraea pulmonicola
NCBI taxonomy Id: 93221
Other names: ATCC BAA-62, ATCC:BAA:62, CCUG 38759, CIP 106625, DSM 16583, LMG 18106, LMG:18106, NCTC 13159, P. pulmonicola, Pandoraea pulmonicola Coenye et al. 2000
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