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lrgA protein (Bacillus cereus) - STRING interaction network
"lrgA" - Antiholin-like protein LrgA in Bacillus cereus
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second shell of interactors
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proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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lrgAAntiholin-like protein LrgA; Inhibits the expression or activity of extracellular murein hydrolases by interacting, possibly with LrgB, with the holin-like protein CidA. The LrgAB and CidA proteins may affect the proton motive force of the membrane. May be involved in programmed cell death (PCD), possibly triggering PCD in response to antibiotics and environmental stresses (143 aa)    
Predicted Functional Partners:
lrgB
Antiholin-like protein LrgB; Inhibits the expression or activity of extracellular murein hydrolases by interacting, possibly with LrgA, with the holin-like protein CidA. The LrgAB and CidA proteins may affect the proton motive force of the membrane. May be involved in programmed cell death (PCD), possibly triggering PCD in response to antibiotics and environmental stresses (230 aa)
 
   
  0.990
cidA
Holin-like protein CidA; Increases the activity of extracellular murein hydrolases possibly by mediating their export via hole formation. Inhibited by the antiholin-like proteins LrgAB. In an unstressed cell, the LrgAB products probably inhibit the function of the CidA protein. When a cell is stressed by the addition of antibiotics or by other factors in the environment, CidA possibly oligomerizes within the bacterial cell membrane, creating lesions that disrupt the proton motive force, which in turn results in loss of cell viability. These lesions are also hypothesized to regulate the [...] (121 aa)
   
     
  0.952
ypdA_1
annotation not available (589 aa)
 
     
  0.889
yohK_1
annotation not available (225 aa)
 
   
  0.879
lytR_1
annotation not available (246 aa)
     
  0.873
cidB_1
annotation not available (230 aa)
   
  0.869
ksgA
Ribosomal RNA small subunit methyltransferase A; Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3’-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits (292 aa)
         
  0.631
lacD
lacD- tagatose 1,6-diphosphate aldolase (335 aa)
           
  0.619
cidA_1
annotation not available (122 aa)
   
          0.574
lytR
Polyisoprenyl-teichoic acid--peptidoglycan teichoic acid transferase TagU; May catalyze the final step in cell wall teichoic acid biosynthesis, the transfer of the anionic cell wall polymers (APs) from their lipid-linked precursor to the cell wall peptidoglycan (PG) (302 aa)
           
  0.543
Your Current Organism:
Bacillus cereus
NCBI taxonomy Id: 1396
Other names: ATCC 14579, B. cereus, BCRC 10603, Bacillus cereus, Bacillus endorhythmos, Bacillus medusa, Bacillus sp. 2479, Bacillus sp. BS2(2013b), Bacillus sp. BV4, Bacillus sp. JKR50, Bacillus sp. JKR62, Bacillus sp. JP44SK22, Bacillus sp. JP44SK37, Bacillus sp. JP44SK43, Bacillus sp. JP44SK45, Bacillus sp. JSG1(2014), Bacillus sp. KER 17, Bacillus sp. MZ-01, Bacillus sp. PXDK-1, Bacillus sp. Pf-1, Bacillus sp. V3, Bacillus sp. mmm86, CCM 2010, CCRC 10603, CCUG 7414, CIP 66.24, DSM 31, IAM 12605, IFO 15305, JCM 2152, LMG 6923, NBRC 15305, NCCB 75008, NCIMB 9373, NCTC 2599, NRRL B-3711, VKM B-504
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