Detail Information for IndEnz0002005272
IED ID IndEnz0002005272
Enzyme Type ID protease005272
Protein Name DNA-binding transcriptional repressor ScoC
HTH-type transcriptional regulator Hpr
Protease production regulatory protein Hpr
Gene Name hpr catA scoC BSU09990
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 MNRVEPPYDVKEALVFTQKMAQLSKALWKSIEKDWQQWLKPYDLNINEHHILWIAYQLNGASISEIAKFGVMHVSTAFNFSKKLEERGYLRFSKRLNDKRNTYVQLTEEGTEVFWSLLEEFDPTRNAVFKGSQPLYHLFGKFPEVAEMMCMIRHIYGDDFMEIFETSLTNIDNDFESVNGKLKKKAKDSAADEPAEELEPVNS
Enzyme Length 203
Uniprot Accession Number P11065
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding DNA_BIND 63..86; /note=H-T-H motif; /evidence=ECO:0000255|HAMAP-Rule:MF_01911
EC Number
Enzyme Function FUNCTION: Negative regulator of protease production and sporulation. Acts by binding directly to the promoter of protease genes (aprE and nprE), and by repressing oligopeptide permease operons (appABCDF and oppABCDF), thereby preventing uptake of oligopeptides required for initiation of sporulation. Acts with SinR as a corepressor of epr expression. Binds to non-m6A-5-methylated 5'-GACGAG-3' sites, tested with scpA; when the target is methylated by DnmA, this repressor no longer binds and transcription is up-regulated (PubMed:32324221). {ECO:0000255|HAMAP-Rule:MF_01911, ECO:0000269|PubMed:10383984, ECO:0000269|PubMed:16923912, ECO:0000269|PubMed:1906467, ECO:0000269|PubMed:32324221}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Beta strand (5); Chain (1); DNA binding (1); Domain (1); Helix (11); Region (1); Turn (1)
Keywords 3D-structure;DNA-binding;Direct protein sequencing;Reference proteome;Repressor;Sporulation;Transcription;Transcription regulation
Interact With O34483
Induction INDUCTION: Negatively regulated by the Mrp homolog protein SalA and by SenS. {ECO:0000269|PubMed:15126467, ECO:0000269|PubMed:16321961}.
Subcellular Location
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D X-ray crystallography (1)
Cross Reference PDB 2FXA;
Mapped Pubmed ID 25278935;
Motif
Gene Encoded By
Mass 23,713
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda