| IED ID | IndEnz0002012917 |
| Enzyme Type ID | protease012917 |
| Protein Name |
Penicillin-binding protein 3 PBP 3 EC 3.4.16.4 PSPB20 Penicillin-binding protein C |
| Gene Name | pbpC ycsM yzsA BSU04140 |
| 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 | MLKKCILLVFLCVGLIGLIGCSKTDSPEDRMEAFVKQWNDQQFDDMYQSLTKDVKKEISKKDFVNRYKAIYEQAGVKNLKVTAGEVDKDDQDNKTMKHIPYKVSMNTNAGKVSFKNTAVLKLEKTDDEESWNIDWDPSFIFKQLADDKTVQIMSIEPKRGQIYDKNGKGLAVNTDVPEIGIVPGELGDKKEKVIKELAKKLDLTEDDIKKKLDQGWVKDDSFVPLKKVKPDQEKLVSEATSLQGVTRTNVSSRYYPYGEKTAHLTGYVRAITAEELKKKKEGTYSDTSNIGIAGLENVYEDKLRGTTGWKIYVPQTGEVIAEKKAKDGEDLHLTIDIKTQMKLYDELKDDSGAAVALQPKTGETLALVSAPSYDPNGFIFGWSDKEWKKLNKDKNNPFSAKFNKTYAPGSTIKPIAAAIGIKNGTLKADEKKTIKGKEWQKDSSWGGYSVTRVSERLQQVDLENALITSDNIYFAQNALDMGADTFTKGLKTFGFSEDVPYEFPIQKSSIANDKLDSDILLADTGYGQGQMQMSPLHLATAYTPFVDNGDLVKPTLIKKDSQTADVWHKQVVTKEGAADITKGLKGVVEDERGSAYQPVVKGITVAGKTGTAELKTSKDDKDGTENGWFVGYDYENKDLLVAMMIQNVQDRGGSHYVVEKAKKQFQSN |
| Enzyme Length | 668 |
| Uniprot Accession Number | P42971 |
| Absorption | |
| Active Site | ACT_SITE 410; /note=Acyl-ester intermediate; /evidence=ECO:0000250|UniProtKB:P0AD65 |
| 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}; |
| DNA Binding | |
| EC Number | 3.4.16.4 |
| Enzyme Function | FUNCTION: Penicillin-binding proteins (PBPs) function in the late steps of murein biosynthesis (Probable). Probably required for both cortical and vegetative peptidoglycan synthesis (Probable). Although not usually required for cell division, in the absence of PBP 2B (pbpB) it becomes essential. Confers resistance to oxacillin and cephalexin (PubMed:28792086). {ECO:0000269|PubMed:28792086, ECO:0000305, ECO:0000305|PubMed:3080407}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Mutagenesis (1); Sequence conflict (2); Transmembrane (1) |
| Keywords | Antibiotic resistance;Carboxypeptidase;Cell membrane;Cell shape;Cell wall biogenesis/degradation;Direct protein sequencing;Hydrolase;Membrane;Peptidoglycan synthesis;Protease;Reference proteome;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | INDUCTION: Transcribed during vegetative growth, drops off after entry into stationary phase and the onset of sporulation. Transcription rises again 70-80 minutes after germination. {ECO:0000269|PubMed:8830698}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20713508, ECO:0000269|PubMed:22882210, ECO:0000269|PubMed:3080407}; Single-pass membrane protein {ECO:0000305}. Forespore inner membrane {ECO:0000269|PubMed:3080407}; Single-pass membrane protein {ECO:0000255}. Forespore outer membrane {ECO:0000269|PubMed:3080407}; Single-pass membrane protein. Membrane raft {ECO:0000269|PubMed:20713508, ECO:0000269|PubMed:22882210}; Single-pass membrane protein {ECO:0000255}. Note=Localizes at mid cell; localization requires FtsZ and PBP 2B (pbpB) (PubMed:28792086). Present in detergent-resistant membrane (DRM) fractions that may be equivalent to eukaryotic membrane rafts; these rafts include proteins involved in signaling, molecule trafficking and protein secretion (PubMed:20713508, PubMed:22882210). {ECO:0000269|PubMed:20713508, ECO:0000269|PubMed:22882210, ECO:0000269|PubMed:28792086}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 19192185; |
| Motif | |
| Gene Encoded By | |
| Mass | 74,406 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |