Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
S-adenosyl-L-methionine + protein L-glutamate | Thermotoga maritima | adaptation in bacterial chemotaxis involves reversible methylation of specific glutamate residues within the cytoplasmic domains of methyl-accepting chemotaxis proteins. Fifteen sites of methylation are identified within the cytoplasmic domains of four different chemoreceptors. The results establish a consensus sequence for chemoreceptor methylation sites in Thermotoga maritima that is distinct from the previously identified consensus sequence | S-adenosyl-L-homocysteine + protein L-glutamate methyl ester | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Thermotoga maritima | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
S-adenosyl-L-methionine + protein L-glutamate | adaptation in bacterial chemotaxis involves reversible methylation of specific glutamate residues within the cytoplasmic domains of methyl-accepting chemotaxis proteins. Fifteen sites of methylation are identified within the cytoplasmic domains of four different chemoreceptors. The results establish a consensus sequence for chemoreceptor methylation sites in Thermotoga maritima that is distinct from the previously identified consensus sequence | Thermotoga maritima | S-adenosyl-L-homocysteine + protein L-glutamate methyl ester | - |
? | |
S-adenosyl-L-methionine + protein L-glutamate | methylation of specific glutamate residues within the cytoplasmic domains of methyl-accepting chemotaxis proteins: TM0429fl, TM0429c, TM1143fl, TM1143c, TM1428fl, TM1428c | Thermotoga maritima | S-adenosyl-L-homocysteine + protein L-glutamate methyl ester | - |
? |