| IED ID | IndEnz0002004714 |
| Enzyme Type ID | protease004714 |
| Protein Name |
Peptidoglycan DL-endopeptidase CwlO EC 3.4.-.- D-gamma-glutamyl-meso-diaminopimelyl DL-endopeptidase PSPA2 |
| Gene Name | cwlO yvcE yzkA BSU34800 |
| 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 | MRKSLITLGLASVIGTSSFLIPFTSKTASAETLDEKKQKIESKQSEVASSIEAKEKELTELQENQSKIEKELKDINDKALDTSNKIEDKKEENDKTKEEIKKLKKEIKETEARIEKRNEILKKRVRSLQESGGSQGYIDVLLGSTSFGDFISRATAVSSIVDADKDLIKQQEQDKAKLEDSEADLNDKLKEVQAALAKLETMQKDLDKQLNEKDKLFDEAKASQKKTAKAISELKSEASELANQKANTEAEQARIKKEQEAAAALIKKQEEAQKASDETQTDDSQTATTESSKASSSDDSSDNSSDNSSNGSSNSSSNGSSSKKSSGSNSNSGGTVISNSGGIEGAISVGSSIVGQSPYKFGGGRTQSDINNRIFDCSSFVRWAYASAGVNLGPVGGTTTDTLVGRGQAVSASEMKRGDLVFFDTYKTNGHVGIYLGNGTFLNDNTSHGVSVDSMSNPYWKAAFKGVVRRVVQ |
| Enzyme Length | 473 |
| Uniprot Accession Number | P40767 |
| Absorption | |
| Active Site | ACT_SITE 377; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU01284; ACT_SITE 431; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU01284; ACT_SITE 443; /evidence=ECO:0000255|PROSITE-ProRule:PRU01284 |
| Activity Regulation | ACTIVITY REGULATION: Detected in exponentially growing cells, the 50 and 30 kDa processing products disappear upon entry into stationary phase with the concomitant appearance of a 20 kDa products. The 50 kDa form persists in the absence of extracellular proteases (PubMed:11987133). {ECO:0000269|PubMed:11987133}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.-.- |
| Enzyme Function | FUNCTION: The C-terminal part of CwlO shows a cell wall hydrolytic DL-endopeptidase activity. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Compositional bias (2); Domain (1); Region (3); Signal peptide (1) |
| Keywords | Cell wall;Cell wall biogenesis/degradation;Hydrolase;Protease;Reference proteome;Secreted;Signal;Thiol protease |
| Interact With | |
| Induction | INDUCTION: Positively regulated by the two-component system YycFG. {ECO:0000269|PubMed:17581128}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11987133}. Secreted, cell wall {ECO:0000269|PubMed:11987133}. |
| Modified Residue | |
| Post Translational Modification | PTM: Identified in the extracellular proteome as a number of processing products of about 50 and 30 kDa. |
| Signal Peptide | SIGNAL 1..30; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 51,033 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |