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lrpC protein (Bacillus subtilis 168) - STRING interaction network
"lrpC" - AsnC family transcriptional regulator in Bacillus subtilis 168
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second shell of interactors
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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lrpCAsnC family transcriptional regulator; Transcriptional regulator with a possible role in regulation of amino acid metabolism. Plays a role in the growth phase transition (180 aa)    
Predicted Functional Partners:
yugG
AsnC family transcriptional regulator (166 aa)
           
  0.868
prcR
Hypothetical protein; Activates transcription of the putBCP operon. Requires proline as a coactivator (411 aa)
           
  0.792
ydzA
Membrane protein (96 aa)
         
  0.739
yqiR
Sigma L-dependent transcriptional regulator YqiR (692 aa)
           
  0.729
topB
DNA topoisomerase 3 (EC-5.99.1.2); Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5’-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3’-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus remo [...] (727 aa)
         
  0.670
yydG
Peptide biosynthesis protein YydG (EC-1.-.-.-); Required for production of the modified peptide YydF (Probable). May activate a metalloenzyme (Potential) (319 aa)
   
 
  0.613
albA
Antilisterial bacteriocin subtilosin biosynthesis protein AlbA; Catalyzes the formation of 3 thioether bonds during production of the sactipeptide subtilosin from SboA. In vitro the thioether bonds cannot be made in the absence of the SboA propeptide, suggesting this is the first reaction in subtilosin maturation (PubMed-22366720). In vitro, in the absence of a second substrate, cleaves S-adenosyl-L-methionine into Met and 5’-dA (PubMed-22366720) (448 aa)
   
 
  0.613
skfB
Hypothetical protein; Catalyzes the formation of the thioether bond required for production of the sporulation killing factor (SKF) from SkfA (PubMed-12817086). Forms the cysteine-methionine thioether bond found in SKF; the acceptor amino acid can be hydrophobic, aromatic or a small hydrophilic amino acid but not a larger hydrophilic amino acid, i.e. Met=Ala, Phe, Leu, Tyr>Asn, Ser>>Gln, Glu, Lys (PubMed-23282011). The relative position of Cys and Met in the substrate cannot be inverted, in vitro the thioether bond cannot be made in the absence of the SkfA propeptide, suggesting this i [...] (410 aa)
   
 
  0.613
nasF
Uroporphyrinogen-iii C-methyltransferase (EC-2.1.1.107) (481 aa)
   
   
  0.596
hbs
DNA-binding protein HU 1; Histone-like DNA-binding protein which is capable of wrapping DNA to stabilize it, and thus to prevent its denaturation under extreme environmental conditions (92 aa)
     
 
  0.547
Your Current Organism:
Bacillus subtilis 168
NCBI taxonomy Id: 224308
Other names: B. subtilis, B. subtilis subsp. subtilis, B. subtilis subsp. subtilis str. 168, Bacillus globigii, Bacillus natto, Bacillus sp. 15:2, Bacillus sp. RSP-GLU, Bacillus sp. S2 BC-1, Bacillus subtilis, Bacillus subtilis 168, Bacillus subtilis subsp. subtilis, Bacillus subtilis subsp. subtilis 168, Bacillus subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis str. BGSC 1A700, Bacillus subtilis/Bacillus globigii, Bacillus uniflagellatus, Vibrio subtilis
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