| IED ID | IndEnz0002008875 |
| Enzyme Type ID | protease008875 |
| Protein Name |
Penicillin-binding protein 2B PBP-2B EC 3.4.16.4 Penicillin-binding protein B Penicillin-sensitive peptidoglycan D,D-transpeptidase |
| Gene Name | pbpB BSU15160 |
| 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 | MPKKNKFMNRGAAILSICFALFFFVILGRMAYIQITGKANGEVLATKATEQHEKKRTIEASRGSILDRKGKVIAEDTATYKLIAILDKKMTTDVKHPQHVVNKEKTAEALSKVINLDKADILDILNKDAKQVEFGSAGRDITYSQKQKIEKMKLPGISFLRDTKRYYPNGVFASNLIGYAEVDEETNEISGAMGLEKVLDKYLKERDGYVTYESDKSGWELPNSKNKITAPKNGDNVYLTIDQKIQTFLEDSMTKVAQKYNPKKIMAAVVDPKTGKVLAMGQRPSFDPNKRDVTNYYNDLISYAYEPGSTMKIFTLAAAMQENVFNANEKYKSGTFEVGGAPVKDHNNGVGWGPTTYHDGVLRSSNVAFAKLAKEKLGYDRLNQYLHKFNFYQKTGIDLPGEVSSKINFKYEFDKASTAYGQASAVTPIQQIQAATAIANDGKMMKPYVIDHIVDPDKDKTIYQNKPESAGTPISASTAKKVRDILGEVVTSKIGTGQAYKIEGFDVAGKTGTAQIAGKGGYLDGTDNYIFSFMGMAPKDDPELLIYVAVQQPQLKAGQSSSDPVSEIFNPTMKNSLHYLNIEPTEKSDSDKEETKAQTMPDLTDQTVAAAQKKAKEENLTPIVIGSDVAVKEQYPKADEEVLTNQKVFLKTGGKIKMPDMTGWSRREVLQYGELAGIHIEVSGQGYAVSQSVKKDKEIKDKTVIKVKFKNPD |
| Enzyme Length | 713 |
| Uniprot Accession Number | Q07868 |
| Absorption | |
| Active Site | ACT_SITE 309; /note="Acyl-ester intermediate"; /evidence="ECO:0000250|UniProtKB:P0AD65, ECO:0000303|PubMed:8244929" |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Preferential cleavage: (Ac)(2)-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.; EC=3.4.16.4; Evidence={ECO:0000305|PubMed:28792086}; |
| DNA Binding | |
| EC Number | 3.4.16.4 |
| Enzyme Function | FUNCTION: Penicillin-binding proteins (PBPs) function in the late steps of murein biosynthesis. PBP-2B is required for vegetative cell division and sporulation septation. Beta-lactamase inactivates the PBPs by acylating an essential serine residue in the active site of these proteins, thereby interrupting normal cell wall synthesis (Probable). This protein itself, but not its transpeptidase activity, is required for cell division (PubMed:28792086). {ECO:0000269|PubMed:28792086, ECO:0000305}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Domain (2); Erroneous initiation (4); Mutagenesis (2); Sequence conflict (2); Topological domain (2); Transmembrane (1) |
| Keywords | Antibiotic resistance;Carboxypeptidase;Cell cycle;Cell division;Cell membrane;Cell shape;Cell wall biogenesis/degradation;Hydrolase;Membrane;Peptidoglycan synthesis;Protease;Reference proteome;Repeat;Sporulation;Transmembrane;Transmembrane helix |
| Interact With | P16655 |
| Induction | INDUCTION: Transcribed at a low constant level in all growth phases. Part of the mraZ-rsmH-ftsL-pbpB operon. {ECO:0000269|PubMed:8636036}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:3080407, ECO:0000269|PubMed:8244929, ECO:0000305|PubMed:28792086}; Single-pass membrane protein {ECO:0000255}. Note=Localizes at mid cell, to cell division sites; localization requires FtsZ. {ECO:0000269|PubMed:28792086}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 18363795; 18621900; 19192185; 20870765; 21630458; |
| Motif | |
| Gene Encoded By | |
| Mass | 78,948 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |