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cidA protein (Bacillus cereus) - STRING interaction network
"cidA" - Holin-like protein CidA 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
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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cidAHolin-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)    
Predicted Functional Partners:
yohK_1
annotation not available (225 aa)
 
   
  0.979
lrgA
Antiholin-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)
   
     
  0.952
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)
 
   
  0.944
cidB_1
annotation not available (230 aa)
 
   
  0.870
benM
annotation not available (301 aa)
              0.672
mraY
Phospho-N-acetylmuramoyl-pentapeptide-transferase; First step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan; Belongs to the glycosyltransferase 4 family. MraY subfamily (324 aa)
         
  0.466
pbpB_2
annotation not available (712 aa)
           
  0.459
pbpB_1
annotation not available (699 aa)
           
  0.459
glgD
Glycogen biosynthesis protein GlgD; glgD- glucose-1-phosphate adenylyltransferase, GlgD subunit (344 aa)
           
  0.459
kdgK_1
annotation not available (338 aa)
           
  0.459
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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