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
ADO47181.1Pitrilysin; KEGG: cko:CKO_04186 hypothetical protein; PFAM: peptidase M16 domain protein. (962 aa)    
Predicted Functional Partners:
recD
Exodeoxyribonuclease V, alpha subunit; A helicase/nuclease that prepares dsDNA breaks (DSB) for recombinational DNA repair. Binds to DSBs and unwinds DNA via a highly rapid and processive ATP-dependent bidirectional helicase activity. Unwinds dsDNA until it encounters a Chi (crossover hotspot instigator) sequence from the 3' direction. Cuts ssDNA a few nucleotides 3' to the Chi site. The properties and activities of the enzyme are changed at Chi. The Chi-altered holoenzyme produces a long 3'-ssDNA overhang and facilitates RecA-binding to the ssDNA for homologous DNA recombination and r [...]
  
  
 0.838
recB
Exodeoxyribonuclease V, beta subunit; A helicase/nuclease that prepares dsDNA breaks (DSB) for recombinational DNA repair. Binds to DSBs and unwinds DNA via a highly rapid and processive ATP-dependent bidirectional helicase activity. Unwinds dsDNA until it encounters a Chi (crossover hotspot instigator) sequence from the 3' direction. Cuts ssDNA a few nucleotides 3' to the Chi site. The properties and activities of the enzyme are changed at Chi. The Chi-altered holoenzyme produces a long 3'-ssDNA overhang and facilitates RecA-binding to the ssDNA for homologous DNA recombination and re [...]
  
  
 0.827
wzzE
Lipopolysaccharide biosynthesis protein; Modulates the polysaccharide chain length of enterobacterial common antigen (ECA); Belongs to the WzzB/Cld/Rol family.
  
     0.740
recC
Exodeoxyribonuclease V, gamma subunit; A helicase/nuclease that prepares dsDNA breaks (DSB) for recombinational DNA repair. Binds to DSBs and unwinds DNA via a highly rapid and processive ATP-dependent bidirectional helicase activity. Unwinds dsDNA until it encounters a Chi (crossover hotspot instigator) sequence from the 3' direction. Cuts ssDNA a few nucleotides 3' to the Chi site. The properties and activities of the enzyme are changed at Chi. The Chi-altered holoenzyme produces a long 3'-ssDNA overhang and facilitates RecA-binding to the ssDNA for homologous DNA recombination and r [...]
     
 0.628
ADO48459.1
PFAM: Haemolysin expression modulating family protein; KEGG: ctu:Ctu_20090 OriC-binding nucleoid-associated protein.
  
     0.611
ADO46747.1
PFAM: Barstar (barnase inhibitor); KEGG: sdy:SDY_3415 hypothetical protein.
  
     0.596
ADO47783.1
KEGG: kva:Kvar_1446 hypothetical protein.
  
     0.581
wzyE
WzyE family protein; Probably involved in the polymerization of enterobacterial common antigen (ECA) trisaccharide repeat units; Belongs to the WzyE family.
  
     0.536
ADO50577.1
PFAM: protein of unknown function Spy-related; KEGG: sew:SeSA_A4277 periplasmic repressor CpxP.
  
     0.535
ADO47177.1
KEGG: kpe:KPK_0881 hypothetical protein.
       0.532
Your Current Organism:
Enterobacter lignolyticus
NCBI taxonomy Id: 701347
Other names: Enterobacter lignolyticus SCF1, [. lignolyticus SCF1, [Enterobacter] lignolyticus SCF1
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.