| IED ID | IndEnz0002014555 |
| Enzyme Type ID | protease014555 |
| Protein Name |
Capsule biosynthesis protein CapD proenzyme EC 2.3.2.- Cleaved into: Capsule biosynthesis protein CapD large chain; Capsule biosynthesis protein CapD small chain |
| Gene Name | capD dep pXO2-55 BXB0063 GBAA_pXO2_0063 |
| Organism | Bacillus anthracis |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus Bacillus cereus group Bacillus anthracis |
| Enzyme Sequence | MNSFKWGKKIILFCLIVSLMGGIGVSCSFNKIKDSVKQKIDSMGDKGTYGVSASHPLAVEEGMKVLKNGGSAVDAAIVVSYVLGVVELHASGIGGGGGMLIISKDKETFIDYRETTPYFTGNQKPHIGVPGFVAGMEYIHDNYGSLPMGELLQPAINYAEKGFKVDDSLTMRLDLAKPRIYSDKLSIFYPNGEPIETGETLIQTDLARTLKKIQKEGAKGFYEGGVARAISKTAKISLEDIKGYKVEVRKPVKGNYMGYDVYTAPPPFSGVTLLQMLKLAEKKEVYKDVDHTATYMSKMEEISRIAYQDRKKNLGDPNYVNMDPNKMVSDKYISTMKNENGDALSEAEHESTTHFVIIDRDGTVVSSTNTLSNFFGTGKYTAGFFLNNQLQNFGSEGFNSYEPGKRSRTFMAPTVLKKDGETIGIGSPGGNRIPQILTPILDKYTHGKGSLQDIINEYRFTFEKNTAYTEIQLSSEVKNELSRKGLNVKKKVSPAFFGGVQALIKDERDNVITGAGDGRRNGTWKSNK |
| Enzyme Length | 528 |
| Uniprot Accession Number | Q51693 |
| Absorption | |
| Active Site | ACT_SITE 352; /note="Nucleophile"; /evidence="ECO:0000269|PubMed:19017271, ECO:0000269|PubMed:19535342" |
| Activity Regulation | |
| Binding Site | BINDING 352; /note="Poly-gamma-D-glutamate"; /evidence="ECO:0000305|PubMed:19535342, ECO:0007744|PDB:3G9K, ECO:0007744|PDB:3GA9"; BINDING 520; /note="Poly-gamma-D-glutamate"; /evidence="ECO:0000305|PubMed:19535342, ECO:0007744|PDB:3G9K, ECO:0007744|PDB:3GA9" |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 2.3.2.- |
| Enzyme Function | FUNCTION: Transpeptidase that cleaves the poly-gamma-D-glutamate capsule and catalyzes the formation of an amide bond with the side-chain amino group of meso-diaminopimelic acid (m-DAP) in the peptidoglycan scaffold (PubMed:19017271). Degradation of the high-molecular weight capsule (H-capsule) to the lower-molecular weight capsule (L-capsule), which is released from the bacterial cell surface. The production of L-capsule is essential to mediate escape from host defenses. {ECO:0000269|PubMed:12134259, ECO:0000269|PubMed:19017271, ECO:0000269|PubMed:19535342, ECO:0000269|PubMed:8105361}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Capsule biogenesis; capsule polysaccharide biosynthesis. |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (16); Binding site (2); Chain (2); Erroneous initiation (2); Helix (23); Mutagenesis (4); Natural variant (1); Region (1); Signal peptide (1); Turn (4) |
| Keywords | 3D-structure;Capsule biogenesis/degradation;Direct protein sequencing;Hydrolase;Plasmid;Protease;Reference proteome;Signal;Transferase;Virulence;Zymogen |
| Interact With | |
| Induction | INDUCTION: Capsule synthesis is transcriptionally regulated by AtxA, AcpA and AcpB. {ECO:0000269|PubMed:14702298}. |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | PTM: Cleaved by autocatalysis into a large and a small subunit. |
| Signal Peptide | SIGNAL 1..26; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 3G9K; 3GA9; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | Plasmid pXO2; Plasmid pTE702 |
| Mass | 58,084 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.19.13; |