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.
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 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 to each other.
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experimentally determined
co-expression
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codYGTP-sensing transcriptional pleiotropic repressor codY; DNA-binding protein that represses the expression of many genes that are induced as cells make the transition from rapid exponential growth to stationary phase. It is a GTP-binding protein that senses the intracellular GTP concentration as an indicator of nutritional limitations. At low GTP concentration it no longer binds GTP and stop to act as a transcriptional repressor; Belongs to the CodY family. (259 aa)    
Predicted Functional Partners:
SD78_2746
Catabolite control protein A.
    
 
 0.847
xerC
Site-specific tyrosine recombinase; Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. The XerC- XerD complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids.
  
  
 0.807
hslU
ATP-dependent hsl protease ATP-binding subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis.
  
    0.805
hslV
ATP-dependent protease HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
  
    0.778
SD78_1151
Transition state regulatory protein AbrB.
  
   
 0.758
SD78_3753
Flagellar basal-body rod protein FlgB; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body.
     
 0.729
SD78_2312
Stage 0 sporulation two-component response regulator (Spo0A); May play the central regulatory role in sporulation. It may be an element of the effector pathway responsible for the activation of sporulation genes in response to nutritional stress. Spo0A may act in concert with spo0H (a sigma factor) to control the expression of some genes that are critical to the sporulation process.
      
 0.707
sepF
FtsZ-interacting protein; Cell division protein that is part of the divisome complex and is recruited early to the Z-ring. Probably stimulates Z-ring formation, perhaps through the cross-linking of FtsZ protofilaments. Its function overlaps with FtsA.
   
  
 0.697
topA
DNA topoisomerase I; 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 removing DNA supe [...]
     
 0.695
fapR
Phosphate:acyl-ACP acyltransferase PlsX; Transcriptional factor involved in regulation of membrane lipid biosynthesis by repressing genes involved in fatty acid and phospholipid metabolism.
  
   
 0.668
Your Current Organism:
Bacillus badius
NCBI taxonomy Id: 1455
Other names: ATCC 14574, B. badius, Bacillus encimensis, Bacillus encimensis Dastager et al. 2015, Bacillus sp. SGD-V-25, CCUG 7412, CIP 58.52, DSM 23, DSM 28241 [[Bacillus encimensis]], IFO 15713, JCM 12228, LMG 7122, LMG:7122, NBRC 15713, NCIB 9364, NCIB:9364, NCIM 5513, NCTC 10333, NRRL NRS-663, VKM B-496, strain SGD-V-25 [[Bacillus encimensis]]
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