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
recArecA protein; 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. (362 aa)    
Predicted Functional Partners:
polA
DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family.
 
 0.993
Deba_2577
Helicase domain protein; COGs: COG0553 Superfamily II DNA/RNA helicase SNF2 family; InterPro IPR014001:IPR001650:IPR000330:IPR014021; KEGG: sfu:Sfum_3846 helicase domain-containing protein; PFAM: helicase domain protein; SNF2-related protein; SMART: DEAD-like helicase; helicase domain protein; SPTR: A0LQ13 Helicase domain protein; manually curated; PFAM: Helicase conserved C-terminal domain; SNF2 family N-terminal domain.
  
 
 0.962
lexA
Transcriptional repressor, LexA family; 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.
  
 
 0.945
Deba_1516
Peptidase S24/S26A/S26B, conserved region; Represses a number of genes involved in the response to DNA damage (SOS response).
  
 
 0.945
Deba_1841
Transcriptional repressor, LexA family; Represses a number of genes involved in the response to DNA damage (SOS response).
  
 
 0.945
Deba_1143
Competence/damage-inducible protein CinA; COGs: COG1546 Uncharacterized protein (competence- and mitomycin-induced); InterPro IPR001453:IPR008136:IPR008135; KEGG: gme:Gmet_0196 competence/damage-inducible protein CinA; PFAM: CinA domain protein; molybdopterin binding domain; SPTR: C8QYB6 Competence/damage-inducible protein CinA; TIGRFAM: competence/damage-inducible protein CinA; PFAM: Probable molybdopterin binding domain; Competence-damaged protein; TIGRFAM: competence/damage-inducible protein CinA N-terminal domain; competence/damage-inducible protein CinA C-terminal domain; molybden [...]
  
  
 0.930
Deba_0246
DNA polymerase III, beta subunit; 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 [...]
  
 0.914
dinB
DNA-directed DNA polymerase; 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.
  
 0.907
Deba_0816
UvrD/REP helicase; COGs: COG0210 Superfamily I DNA and RNA helicase; InterPro IPR014016:IPR014017:IPR000212; KEGG: dma:DMR_07030 ATP-dependent DNA helicase; PFAM: UvrD/REP helicase; SPTR: Q1NUA0 UvrD/REP helicase; PFAM: UvrD/REP helicase.
 
 
 0.858
Deba_1832
ERCC4 domain protein; COGs: COG1948 ERCC4-type nuclease; InterPro IPR006166:IPR011335:IPR020819; KEGG: sfu:Sfum_3788 ERCC4 domain-containing protein; PFAM: ERCC4 domain protein; SMART: ERCC4 domain protein; SPTR: C6MK29 ERCC4 domain protein.
   
 0.852
Your Current Organism:
Desulfarculus baarsii
NCBI taxonomy Id: 644282
Other names: D. baarsii DSM 2075, Desulfarculus baarsii 2st 14, Desulfarculus baarsii DSM 2075, Desulfarculus baarsii str. DSM 2075, Desulfarculus baarsii strain DSM 2075
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