IED ID | IndEnz0002002582 |
Enzyme Type ID | protease002582 |
Protein Name |
L-Ala--D-Glu endopeptidase EC 3.4.-.- Peptidoglycan hydrolase Sporulation-specific endopeptidase |
Gene Name | lytH yunA yutA BSU32340 |
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 | MKVLLSALLLLLFAFEPSASGKKLSDPVLSKRMELYHKIEAVTQIPWYALAAVDQYEENVRSNRKDLPEKAGIISIYIPDDIWSGPENPNPKDDAPLSIKVFDGIGMDGDGDGKAEVSNDEDILYTFSQYLLSYGTDEDNIRIGLWNYYRRDQTVGIISEFMKLFKAYGHIDLGEHAFPLPIRTDYSYRSTWGDARGFGGRRIHEGTDIFAHYGLPVKSTCYGVVEMKGWNRFGGWRIGIRDINNTYHYFAHLNGFAKGIKTGQIVEPGQVIGSVGSSGYGPPGTAGKFPPHLHYGMYKDNGRTEWSFDPYPHLRAWERYEYQKKK |
Enzyme Length | 326 |
Uniprot Accession Number | O32130 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.4.-.- |
Enzyme Function | FUNCTION: L-Ala--D-Glu endopeptidase involved in production of single L-alanine side chains from tetrapeptides in the spore cortex peptidoglycan. Therefore, is required for the endospore cortex maturation. {ECO:0000269|PubMed:12813075}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Chain (1); Metal binding (4); Signal peptide (1) |
Keywords | Cell cycle;Cell wall biogenesis/degradation;Differentiation;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Signal;Sporulation;Zinc |
Interact With | |
Induction | INDUCTION: Expressed under the control of the late mother cell-specific sigma factor sigma-K. {ECO:0000269|PubMed:12813075}. |
Subcellular Location | |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..19; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 36,957 |
Kinetics | |
Metal Binding | METAL 204; /note=Zinc; /evidence=ECO:0000250; METAL 208; /note=Zinc; /evidence=ECO:0000250; METAL 292; /note=Zinc; /evidence=ECO:0000250; METAL 294; /note=Zinc; /evidence=ECO:0000250 |
Rhea ID | |
Cross Reference Brenda |