Cloned (Comment) | Organism |
---|---|
gene kamA, DNA and amino acid sequence determination and analysis, sequence analysis of the kam locus, genetic organization, the kam locus forms two operons: yodT (yodT-yodS-yodR-yodQ-yodPkamR) and kamA (kamA-yokU-yozE). The transcriptional start sites (TSSs) of the kamA gene were determined using 5' rapid amplification of cDNA ends (RACE). A typical -12/-24 sigma54 binding site is identified in the promoter PkamA, which is located upstream of the kamA gene TSS. PkamA, which directs the transcription of the kamA operon, is controlled by the sigma54 factor and is activated through the sigma54-dependent transcriptional regulator KamR. The kamA operon is also controlled by sigmaK and regulated by the GerE protein in the late stage of sporulation | Bacillus thuringiensis serovar kurstaki |
Protein Variants | Comment | Organism |
---|---|---|
additional information | generation of kamR and kamA mutants by homologous recombination to examine the role of the kam locus. The results show that the sporulation rate in Bacillus thuringiensis mutant strain HD (DELTAkamR) is slightly decreased compared to that in wild-type strain HD73, whereas that in strain HD (DELTAkamA) it is similar to that in strain HD73. Other genes regulated by KamR are important for sporulation. Construction of yodT and kamA promoter fusions with lacZ | Bacillus thuringiensis serovar kurstaki |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-lysine | Bacillus thuringiensis serovar kurstaki | - |
L-beta-lysine | - |
r | |
L-lysine | Bacillus thuringiensis serovar kurstaki HD73 | - |
L-beta-lysine | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus thuringiensis serovar kurstaki | A0A0K0QCW0 | - |
- |
Bacillus thuringiensis serovar kurstaki HD73 | A0A0K0QCW0 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-lysine | - |
Bacillus thuringiensis serovar kurstaki | L-beta-lysine | - |
r | |
L-lysine | - |
Bacillus thuringiensis serovar kurstaki HD73 | L-beta-lysine | - |
r |
Synonyms | Comment | Organism |
---|---|---|
AblA | - |
Bacillus thuringiensis serovar kurstaki |
HD73_2540 | locus name | Bacillus thuringiensis serovar kurstaki |
KAM | - |
Bacillus thuringiensis serovar kurstaki |
kamA | - |
Bacillus thuringiensis serovar kurstaki |
lysine-2,3-aminomutase | - |
Bacillus thuringiensis serovar kurstaki |
General Information | Comment | Organism |
---|---|---|
metabolism | L-lysine is first converted to L-beta-lysine by a lysine-2,3-aminomutase in the lysine degradation pathway, and this intermediate is then acetylated to Nepsilon-acetyl-beta-lysine by the action of an acetyltransferase. The L-lysine degradation pathway in strain HD73, overview | Bacillus thuringiensis serovar kurstaki |
physiological function | lysine 2,3-aminomutase catalyzes the interconversion of L-lysine and L-beta-lysine. Analysis of the transcription and regulation of the kam locus, including lysine-2,3-aminomutase-encoding genes, in Bacillus thuringiensis, overview. Transcription of the lysine-2,3-aminomutase gene in the kam locus of Bacillus thuringiensis subsp. kurstaki strain HD73 is controlled by both sigma54 and sigmaK factors | Bacillus thuringiensis serovar kurstaki |