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dinB protein (Methylobacter tundripaludum) - STRING interaction network
"dinB" - DNA polymerase IV in Methylobacter tundripaludum
Nodes:
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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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 each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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[Homology]
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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 (367 aa)    
Predicted Functional Partners:
Mettu_1953
Beta sliding clamp; 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 replication as [...] (366 aa)
     
  0.968
lexA
LexA repressor; 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 (211 aa)
   
  0.934
polA
DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5’-3’ exonuclease activity (930 aa)
   
  0.929
recA
Protein 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 (345 aa)
   
  0.918
Mettu_4109
Acylphosphatase; KEGG- acp-A2cp1_0730 acylphosphatase; HAMAP- Acylphosphatase; PFAM- Acylphosphatase-like; Belongs to the acylphosphatase family (89 aa)
       
  0.762
groL
60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (550 aa)
       
 
  0.753
Mettu_2681
SNF2-related protein; KEGG- hch-HCH_06999 SNF2 family DNA/RNA helicase; PFAM- SNF2-related; Zinc finger, SWIM-type; DNA/RNA helicase, C-terminal; SMART- DEAD-like helicase, N-terminal; DNA/RNA helicase, C-terminal (1083 aa)
   
  0.752
Mettu_3480
Pyruvate-flavodoxin oxidoreductase; Oxidoreductase required for the transfer of electrons from pyruvate to flavodoxin (1212 aa)
     
 
  0.749
nusA
Transcription termination/antitermination protein NusA; Participates in both transcription termination and antitermination (505 aa)
       
 
  0.725
Mettu_2713
PFAM- Ankyrin repeat; KEGG- sdy-SDY_P106 hypothetical protein (938 aa)
   
  0.718
Your Current Organism:
Methylobacter tundripaludum
NCBI taxonomy Id: 697282
Other names: M. tundripaludum SV96, Methylobacter sp. SV96, Methylobacter tundripaludum, Methylobacter tundripaludum DSM 17260, Methylobacter tundripaludum SV96, Methylobacter tundripaludum str. SV96, Methylobacter tundripaludum strain SV96
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