IED ID | IndEnz0002008965 |
Enzyme Type ID | protease008965 |
Protein Name |
Small, acid-soluble spore protein C SASP |
Gene Name | sspC BSU19950 |
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 | MAQQSRSRSNNNNDLLIPQAASAIEQMKLEIASEFGVQLGAETTSRANGSVGGEITKRLVRLAQQNMGGQFH |
Enzyme Length | 72 |
Uniprot Accession Number | P02958 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | |
Enzyme Function | FUNCTION: SASP are bound to spore DNA. They are double-stranded DNA-binding proteins that cause DNA to change to an a-like conformation. They protect the DNA backbone from chemical and enzymatic cleavage and are thus involved in dormant spore's high resistance to UV light. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Chain (1); Helix (3); Site (1) |
Keywords | 3D-structure;DNA-binding;Reference proteome;Sporulation |
Interact With | |
Induction | |
Subcellular Location | |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | X-ray crystallography (1) |
Cross Reference PDB | 2Z3X; |
Mapped Pubmed ID | 18287075; |
Motif | |
Gene Encoded By | |
Mass | 7,758 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |