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cidA

Gene
cidA
Protein
Holin-like protein CidA
Organism
Staphylococcus aureus (strain Mu3 / ATCC 700698)
Length
131 amino acids
Function
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 CidAB proteins. When a cell is stressed by the addition of antibiotics or by other factors in the environment, the CidAB proteins possibly oligomerize 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 subsequent cell lysis by either allowing the murein hydrolases access to the cell wall substrate and/or regulating their activity by a possible change in the cell wall pH that results from loss of membrane potential.
Similarity
Belongs to the CidA/LrgA family. CidA subfamily.
Mass
14.73 kDa
Sequence
MHKVQLIIKLLLQLGIIIVITYIGTEIQKIFHLPLAGSIVGLFLFYLLLQFKIVPLTWVEDGANFLLKTMVFFFIPSVVGIMDVASEITLNYILFFAVIIIGTCIVALSSGYIAEKMSVKHKHRKGVDAYE

Gene
cidA
Protein
Holin-like protein CidA
Organism
Staphylococcus aureus (strain JH1)
Length
131 amino acids
Function
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 CidAB proteins. When a cell is stressed by the addition of antibiotics or by other factors in the environment, the CidAB proteins possibly oligomerize 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 subsequent cell lysis by either allowing the murein hydrolases access to the cell wall substrate and/or regulating their activity by a possible change in the cell wall pH that results from loss of membrane potential.
Similarity
Belongs to the CidA/LrgA family. CidA subfamily.
Mass
14.73 kDa
Sequence
MHKVQLIIKLLLQLGIIIVITYIGTEIQKIFHLPLAGSIVGLFLFYLLLQFKIVPLTWVEDGANFLLKTMVFFFIPSVVGIMDVASEITLNYILFFAVIIIGTCIVALSSGYIAEKMSVKHKHRKGVDAYE

Gene
cidA
Protein
Holin-like protein CidA
Organism
Staphylococcus aureus (strain USA300)
Length
131 amino acids
Function
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 CidAB proteins. When a cell is stressed by the addition of antibiotics or by other factors in the environment, the CidAB proteins possibly oligomerize 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 subsequent cell lysis by either allowing the murein hydrolases access to the cell wall substrate and/or regulating their activity by a possible change in the cell wall pH that results from loss of membrane potential.
Similarity
Belongs to the CidA/LrgA family. CidA subfamily.
Mass
14.73 kDa
Sequence
MHKVQLIIKLLLQLGIIIVITYIGTEIQKIFHLPLAGSIVGLFLFYLLLQFKIVPLTWVEDGANFLLKTMVFFFIPSVVGIMDVASEITLNYILFFAVIIIGTCIVALSSGYIAEKMSVKHKHRKGVDAYE

Gene
cidA
Protein
Holin-like protein CidA
Organism
Staphylococcus aureus (strain NCTC 8325)
Length
131 amino acids
Function
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 CidAB proteins. When a cell is stressed by the addition of antibiotics or by other factors in the environment, the CidAB proteins possibly oligomerize 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 subsequent cell lysis by either allowing the murein hydrolases access to the cell wall substrate and/or regulating their activity by a possible change in the cell wall pH that results from loss of membrane potential.
Similarity
Belongs to the CidA/LrgA family. CidA subfamily.
Mass
14.73 kDa
Sequence
MHKVQLIIKLLLQLGIIIVITYIGTEIQKIFHLPLAGSIVGLFLFYLLLQFKIVPLTWVEDGANFLLKTMVFFFIPSVVGIMDVASEITLNYILFFAVIIIGTCIVALSSGYIAEKMSVKHKHRKGVDAYE

Gene
cidA
Protein
Holin-like protein CidA
Organism
Staphylococcus aureus (strain JH9)
Length
131 amino acids
Function
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 CidAB proteins. When a cell is stressed by the addition of antibiotics or by other factors in the environment, the CidAB proteins possibly oligomerize 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 subsequent cell lysis by either allowing the murein hydrolases access to the cell wall substrate and/or regulating their activity by a possible change in the cell wall pH that results from loss of membrane potential.
Similarity
Belongs to the CidA/LrgA family. CidA subfamily.
Mass
14.73 kDa
Sequence
MHKVQLIIKLLLQLGIIIVITYIGTEIQKIFHLPLAGSIVGLFLFYLLLQFKIVPLTWVEDGANFLLKTMVFFFIPSVVGIMDVASEITLNYILFFAVIIIGTCIVALSSGYIAEKMSVKHKHRKGVDAYE

Gene
cidA
Protein
Holin-like protein CidA
Organism
Staphylococcus aureus (strain COL)
Length
131 amino acids
Function
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 CidAB proteins. When a cell is stressed by the addition of antibiotics or by other factors in the environment, the CidAB proteins possibly oligomerize 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 subsequent cell lysis by either allowing the murein hydrolases access to the cell wall substrate and/or regulating their activity by a possible change in the cell wall pH that results from loss of membrane potential.
Similarity
Belongs to the CidA/LrgA family. CidA subfamily.
Mass
14.73 kDa
Sequence
MHKVQLIIKLLLQLGIIIVITYIGTEIQKIFHLPLAGSIVGLFLFYLLLQFKIVPLTWVEDGANFLLKTMVFFFIPSVVGIMDVASEITLNYILFFAVIIIGTCIVALSSGYIAEKMSVKHKHRKGVDAYE

Gene
cidA
Protein
Holin-like protein CidA
Organism
Staphylococcus aureus (strain Newman)
Length
131 amino acids
Function
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 CidAB proteins. When a cell is stressed by the addition of antibiotics or by other factors in the environment, the CidAB proteins possibly oligomerize 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 subsequent cell lysis by either allowing the murein hydrolases access to the cell wall substrate and/or regulating their activity by a possible change in the cell wall pH that results from loss of membrane potential.
Similarity
Belongs to the CidA/LrgA family. CidA subfamily.
Mass
14.73 kDa
Sequence
MHKVQLIIKLLLQLGIIIVITYIGTEIQKIFHLPLAGSIVGLFLFYLLLQFKIVPLTWVEDGANFLLKTMVFFFIPSVVGIMDVASEITLNYILFFAVIIIGTCIVALSSGYIAEKMSVKHKHRKGVDAYE

Gene
cidA
Protein
Holin-like protein CidA
Organism
Staphylococcus aureus (strain Mu50 / ATCC 700699)
Length
131 amino acids
Function
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 CidAB proteins. When a cell is stressed by the addition of antibiotics or by other factors in the environment, the CidAB proteins possibly oligomerize 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 subsequent cell lysis by either allowing the murein hydrolases access to the cell wall substrate and/or regulating their activity by a possible change in the cell wall pH that results from loss of membrane potential.
Similarity
Belongs to the CidA/LrgA family. CidA subfamily.
Mass
14.73 kDa
Sequence
MHKVQLIIKLLLQLGIIIVITYIGTEIQKIFHLPLAGSIVGLFLFYLLLQFKIVPLTWVEDGANFLLKTMVFFFIPSVVGIMDVASEITLNYILFFAVIIIGTCIVALSSGYIAEKMSVKHKHRKGVDAYE

Gene
cidA
Protein
Holin-like protein CidA
Organism
Staphylococcus aureus (strain N315)
Length
131 amino acids
Function
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 CidAB proteins. When a cell is stressed by the addition of antibiotics or by other factors in the environment, the CidAB proteins possibly oligomerize 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 subsequent cell lysis by either allowing the murein hydrolases access to the cell wall substrate and/or regulating their activity by a possible change in the cell wall pH that results from loss of membrane potential.
Similarity
Belongs to the CidA/LrgA family. CidA subfamily.
Mass
14.73 kDa
Sequence
MHKVQLIIKLLLQLGIIIVITYIGTEIQKIFHLPLAGSIVGLFLFYLLLQFKIVPLTWVEDGANFLLKTMVFFFIPSVVGIMDVASEITLNYILFFAVIIIGTCIVALSSGYIAEKMSVKHKHRKGVDAYE

Gene
cidA
Protein
Holin-like protein CidA
Organism
Staphylococcus aureus (strain MRSA252)
Length
131 amino acids
Function
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 CidAB proteins. When a cell is stressed by the addition of antibiotics or by other factors in the environment, the CidAB proteins possibly oligomerize 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 subsequent cell lysis by either allowing the murein hydrolases access to the cell wall substrate and/or regulating their activity by a possible change in the cell wall pH that results from loss of membrane potential.
Similarity
Belongs to the CidA/LrgA family. CidA subfamily.
Mass
14.735 kDa
Sequence
MHKVQLIIKLLLQLGIIIVITYIGTEIQKIFHLPLAGSIVGLFLFYLLLQFKIVPLTWVEDGANFLLKTMVFFFIPSVVGIMDVASEITLNYILFFAVIIIGTCIVALSSGYIAEKMSVKHKQRKGIDAYE

Gene
cidA
Protein
Holin-like protein CidA
Organism
Staphylococcus aureus (strain MSSA476)
Length
131 amino acids
Function
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 CidAB proteins. When a cell is stressed by the addition of antibiotics or by other factors in the environment, the CidAB proteins possibly oligomerize 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 subsequent cell lysis by either allowing the murein hydrolases access to the cell wall substrate and/or regulating their activity by a possible change in the cell wall pH that results from loss of membrane potential.
Similarity
Belongs to the CidA/LrgA family. CidA subfamily.
Mass
14.73 kDa
Sequence
MHKVQLIIKLLLQLGIIIVITYIGTEIQKIFHLPLAGSIVGLFLFYLLLQFKIVPLTWVEDGANFLLKTMVFFFIPSVVGIMDVASEITLNYILFFAVIIIGTCIVALSSGYIAEKMSVKHKHRKGVDAYE

Gene
cidA
Protein
Holin-like protein CidA
Organism
Staphylococcus aureus (strain USA300 / TCH1516)
Length
131 amino acids
Function
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 CidAB proteins. When a cell is stressed by the addition of antibiotics or by other factors in the environment, the CidAB proteins possibly oligomerize 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 subsequent cell lysis by either allowing the murein hydrolases access to the cell wall substrate and/or regulating their activity by a possible change in the cell wall pH that results from loss of membrane potential.
Similarity
Belongs to the CidA/LrgA family. CidA subfamily.
Mass
14.73 kDa
Sequence
MHKVQLIIKLLLQLGIIIVITYIGTEIQKIFHLPLAGSIVGLFLFYLLLQFKIVPLTWVEDGANFLLKTMVFFFIPSVVGIMDVASEITLNYILFFAVIIIGTCIVALSSGYIAEKMSVKHKHRKGVDAYE

Gene
cidA
Protein
Holin-like protein CidA
Organism
Staphylococcus aureus (strain MW2)
Length
131 amino acids
Function
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 CidAB proteins. When a cell is stressed by the addition of antibiotics or by other factors in the environment, the CidAB proteins possibly oligomerize 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 subsequent cell lysis by either allowing the murein hydrolases access to the cell wall substrate and/or regulating their activity by a possible change in the cell wall pH that results from loss of membrane potential.
Similarity
Belongs to the CidA/LrgA family. CidA subfamily.
Mass
14.73 kDa
Sequence
MHKVQLIIKLLLQLGIIIVITYIGTEIQKIFHLPLAGSIVGLFLFYLLLQFKIVPLTWVEDGANFLLKTMVFFFIPSVVGIMDVASEITLNYILFFAVIIIGTCIVALSSGYIAEKMSVKHKHRKGVDAYE

Gene
cidA
Protein
Holin-like protein CidA
Organism
Staphylococcus epidermidis (strain ATCC 35984 / RP62A)
Length
130 amino acids
Function
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 CidAB proteins. When a cell is stressed by the addition of antibiotics or by other factors in the environment, the CidAB proteins possibly oligomerize 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 subsequent cell lysis by either allowing the murein hydrolases access to the cell wall substrate and/or regulating their activity by a possible change in the cell wall pH that results from loss of membrane potential.
Similarity
Belongs to the CidA/LrgA family. CidA subfamily.
Mass
14.514 kDa
Sequence
MEKAKFVIKLILQLALIMLITFIGTEVQKLLHIPLAGSIVGLMLFFLLLQFKIVPESWINVGADFLLKTMVFFFIPSVVGIMDVASNITMNYILFFIVIIIGTCLVALSSGYIAEKMLEKSNTRKGTDHS

Gene
cidA
Protein
Holin-like protein CidA
Organism
Staphylococcus epidermidis (strain ATCC 12228)
Length
130 amino acids
Function
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 CidAB proteins. When a cell is stressed by the addition of antibiotics or by other factors in the environment, the CidAB proteins possibly oligomerize 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 subsequent cell lysis by either allowing the murein hydrolases access to the cell wall substrate and/or regulating their activity by a possible change in the cell wall pH that results from loss of membrane potential.
Similarity
Belongs to the CidA/LrgA family. CidA subfamily.
Mass
14.514 kDa
Sequence
MEKAKFVIKLILQLALIMLITFIGTEVQKLLHIPLAGSIVGLMLFFLLLQFKIVPESWINVGADFLLKTMVFFFIPSVVGIMDVASNITMNYILFFIVIIIGTCLVALSSGYIAEKMLEKSNTRKGTDHS

Gene
cidA
Protein
Holin-like protein CidA
Organism
Bacillus subtilis (strain 168)
Length
128 amino acids
Function
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 subsequent cell lysis by either allowing the murein hydrolases access to the cell wall substrate and/or regulating their activity by a possible change in the cell wall pH that results from loss of membrane potential.
Similarity
Belongs to the CidA/LrgA family. CidA subfamily.
Mass
14.261 kDa
Sequence
MKKLLLTVIQIALLFIFARLINWVTALLHINIPGSIIGIVILFTLLHFNIIKLEWIELGAAWLLGELLLFFIPSAVGVIEYGDIMSKFGVSILLVVIISTFVVMVSTGTLTQLIAKRKEKKHTCSSEL

Gene
cidA
Protein
Holin-like protein CidA
Organism
Bacillus velezensis (strain DSM 23117 / BGSC 10A6 / FZB42)
Length
128 amino acids
Function
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 subsequent cell lysis by either allowing the murein hydrolases access to the cell wall substrate and/or regulating their activity by a possible change in the cell wall pH that results from loss of membrane potential.
Similarity
Belongs to the CidA/LrgA family. CidA subfamily.
Mass
14.184 kDa
Sequence
MKKLLLTVIQIALLFIFARLINWVTAALHINIPGSIIGIVILFTLLHFKIIKLEWIELGAAWLLGELLLFFIPSAVGVIEYGDIMSKFGVSILLVVVISTFVVMVSTGTLTQLIAKRKEKKQTCSSES