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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
ybbRConserved hypothetical protein; Upon coexpression in E.coli stimulates the diadenylate cyclase activity of CdaA about 20-fold. In B.subtilis c-di-AMP is a second messenger that mediates growth, DNA repair and cell wall homeostasis; it is toxic when present in excess. (483 aa)    
Predicted Functional Partners:
ybbP
Putative enzyme with DAC domain protein; One of 3 paralogous diadenylate cyclases (DAC) in this bacteria, catalyzing the condensation of 2 ATP molecules into cyclic di-AMP (c-di-AMP) (Probable). Upon expression in E.coli leads to c-di- AMP synthesis. Probably the main producer of c-di-AMP for the cell; is probably implicated in control of peptidogylcan synthesis. In B.subtilis c-di-AMP is a second messenger that mediates growth, DNA repair and cell wall homeostasis; it is toxic when present in excess.
 
  
 0.996
glmM
Phosphoglucosamine mutase; Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate (By similarity). Glucosamine-1-phosphate is used for cell wall biosynthesis (Probable); Belongs to the phosphohexose mutase family.
  
  
 0.985
cdnD
Phosphodiesterase acting on cyclic dinucleotides; Has phosphodiesterase (PDE) activity against cyclic-di-AMP (c-di-AMP) and to a much lesser extent against cyclic-di-GMP (c-di-GMP) in the DHH/DHHA1 domains. Also has ATPase activity, probably via the GGDEF domain. Overexpression leads to increased sensitivity to methyl methanesulfonate (MMS) and H(2)O(2). Overexpression leads to extreme sensitivity to the beta-lactam antibiotic cefuroxime (CEF), probably dependent on PDE activity. May monitor cellular heme or NO levels. In B.subtilis c-di-AMP is a second messenger that mediates growth, [...]
  
  
 0.941
yqfF
Putative membrane associate hydrolase; Probably has phosphodiesterase (PDE) activity against cyclic- di-AMP (c-di-AMP); may be the major c-di-AMP PDE in the cell. In B.subtilis c-di-AMP is a second messenger that mediates growth, DNA repair and cell wall homeostasis; it is toxic when present in excess.
   
  
 0.912
yojJ
Putative enzyme with DAC domain; One of 3 paralogous diadenylate cyclases (DAC) in this bacteria, catalyzing the condensation of 2 ATP molecules into cyclic di-AMP (c-di-AMP) (Probable). Upon expression in E.coli leads to c-di- AMP synthesis. Overexpression of the hyperactive mutant (L44F) in the absence of c-di-AMP phosphodiesterase GdpP leads to growth defects in log phase (long curly cell filaments) that disappear upon sporulation; spore formation is normal, showing sporulation is insensitive to the excess c-di-AMP. In B.subtilis c-di-AMP is a second messenger that mediates growth, [...]
 
  
 0.886
rsiW
anti-sigma(W) factor; The anti-sigma factor for extracytoplasmic function (ECF) sigma factor sigma-W (SigW). Holds SigW, its cognate ECF sigma factor, in an inactive form until released by regulated intramembrane proteolysis (RIP). SigW and RsiW mediate cell response to cell wall stress. RIP occurs when an extracytoplasmic signal triggers a concerted proteolytic cascade to transmit information and elicit cellular responses. The membrane-spanning regulatory substrate protein is first cut periplasmically (site-1 protease, S1P, PrsW) , then within the membrane itself (site-2 protease, S2P [...]
  
  
 0.690
priA
Primosomal replication factor Y (primosomal protein N'); Involved in the restart of stalled replication forks. Recognizes and binds the arrested nascent DNA chain at stalled replication forks. It can open the DNA duplex, via its helicase activity, and promote assembly of the primosome and loading of the major replicative helicase DnaB onto DNA; Belongs to the helicase family. PriA subfamily.
  
  
 0.671
sigW
RNA polymerase ECF(extracytoplasmic function)-type sigma factor W; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. Sigma-W controls genes involved in response to cell envelope stress such as antimicrobial peptides , alkaline pH , transport processes and detoxification.
  
  
 0.662
pbpB
Penicillin-binding protein 2B; Penicillin-binding proteins (PBPs) function in the late steps of murein biosynthesis. PBP-2B is required for vegetative cell division and sporulation septation. Beta-lactamase inactivates the PBPs by acylating an essential serine residue in the active site of these proteins, thereby interrupting normal cell wall synthesis; Belongs to the transpeptidase family.
 
    0.584
divIB
Cell-division initiation protein; Cell division protein that may be involved in stabilizing or promoting the assembly of the division complex. Plays an essential role in division at high temperatures, maybe by protecting FtsL from degradation or by promoting formation of the FtsL-DivIC complex. May modulate the transpeptidase activity of PBP-2B. Also required for efficient sporulation at all temperatures. Could be directly involved in the engulfment process or be required to form a sporulation septum competent for engulfment. Influences the Spo0J/Soj system of chromosome segregation. B [...]
  
    0.545
Your Current Organism:
Bacillus subtilis 168
NCBI taxonomy Id: 224308
Other names: B. subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis 168, Bacillus subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis str. BGSC 1A700
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