Detail Information for IndEnz0001000185
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