IED ID | IndEnz0001000185 |
Enzyme Type ID | amylase000185 |
Protein Name |
Catabolite control protein A Glucose-resistance amylase regulator |
Gene Name | ccpA alsA amyR graR BSU29740 |
Organism | Bacillus subtilis (strain 168) |
Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus Bacillus subtilis group Bacillus subtilis Bacillus subtilis subsp. subtilis Bacillus subtilis (strain 168) |
Enzyme Sequence | MSNITIYDVAREANVSMATVSRVVNGNPNVKPTTRKKVLEAIERLGYRPNAVARGLASKKTTTVGVIIPDISSIFYSELARGIEDIATMYKYNIILSNSDQNMEKELHLLNTMLGKQVDGIVFMGGNITDEHVAEFKRSPVPIVLAASVEEQEETPSVAIDYEQAIYDAVKLLVDKGHTDIAFVSGPMAEPINRSKKLQGYKRALEEANLPFNEQFVAEGDYTYDSGLEALQHLMSLDKKPTAILSATDEMALGIIHAAQDQGLSIPEDLDIIGFDNTRLSLMVRPQLSTVVQPTYDIGAVAMRLLTKLMNKEPVEEHIVELPHRIELRKSTKS |
Enzyme Length | 334 |
Uniprot Accession Number | P25144 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | DNA_BIND 6..25; /note=H-T-H motif; /evidence=ECO:0000255|PROSITE-ProRule:PRU00111 |
EC Number | |
Enzyme Function | FUNCTION: Global transcriptional regulator of carbon catabolite repression (CCR) and carbon catabolite activation (CCA), which ensures optimal energy usage under diverse conditions. Interacts with either P-Ser-HPr or P-Ser-Crh, leading to the formation of a complex that binds to DNA at the catabolite-response elements (cre). Binding to DNA allows activation or repression of many different genes and operons. {ECO:0000269|PubMed:10559165, ECO:0000269|PubMed:11557150, ECO:0000269|PubMed:1904524, ECO:0000269|PubMed:21106498, ECO:0000269|PubMed:7665492}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Beta strand (16); Chain (1); DNA binding (1); Domain (1); Helix (15); Turn (1) |
Keywords | 3D-structure;Activator;DNA-binding;Reference proteome;Repressor;Transcription;Transcription regulation |
Interact With | P39779; P08877; P20429 |
Induction | |
Subcellular Location | |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | X-ray crystallography (5) |
Cross Reference PDB | 1ZVV; 2FEP; 3OQM; 3OQN; 3OQO; |
Mapped Pubmed ID | 21630458; 22512862; |
Motif | |
Gene Encoded By | |
Mass | 36,940 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |