Detail Information for IndEnz0002008244
IED ID IndEnz0002008244
Enzyme Type ID protease008244
Protein Name HTH-type transcriptional regulator SinR
Gene Name sinR flaD sin BSU24610
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 MIGQRIKQYRKEKGYSLSELAEKAGVAKSYLSSIERNLQTNPSIQFLEKVSAVLDVSVHTLLDEKHETEYDGQLDSEWEKLVRDAMTSGVSKKQFREFLDYQKWRKSQKEE
Enzyme Length 111
Uniprot Accession Number P06533
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding DNA_BIND 17..36; /note=H-T-H motif; /evidence=ECO:0000255|PROSITE-ProRule:PRU00257
EC Number
Enzyme Function FUNCTION: Negative as well as positive regulator of alternate developmental processes that are induced at the end of vegetative growth in response to nutrient depletion. Binds to the alkaline protease (aprE) gene at two sites. Also acts as a repressor of the key sporulation gene spo0A. Negatively regulates transcription of the eps operon, which is responsible for the biosynthesis of an exopolysaccharide involved in biofilm formation; therefore it could govern the transition between a state in which bacteria swim or swarm and a state in which bacteria assemble into multicellular communities. Acts with Hpr as a corepressor of epr expression. Also negatively regulates transcription of the lutABC operon, which is required for lactate utilization. Repressor activity is regulated by SinI. {ECO:0000269|PubMed:15661000, ECO:0000269|PubMed:16923912, ECO:0000269|PubMed:1898931, ECO:0000269|PubMed:7642487}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Beta strand (1); Chain (1); DNA binding (1); Domain (2); Helix (7)
Keywords 3D-structure;Activator;DNA-binding;Reference proteome;Repressor;Sporulation;Transcription;Transcription regulation
Interact With
Induction
Subcellular Location
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D NMR spectroscopy (2); X-ray crystallography (4)
Cross Reference PDB 1B0N; 2YAL; 3QQ6; 3ZKC; 5TN0; 5TN2;
Mapped Pubmed ID 21708175; 23430750; 31493408;
Motif
Gene Encoded By
Mass 12,989
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda