| IED ID | IndEnz0002007427 |
| Enzyme Type ID | protease007427 |
| Protein Name |
Penicillin-binding protein 2D PBP-2D PBP2d Includes: Penicillin-insensitive transglycosylase EC 2.4.1.129 Peptidoglycan TGase ; Penicillin-sensitive transpeptidase EC 3.4.16.4 DD-transpeptidase |
| Gene Name | pbpG ywhE BSU37510 |
| 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 | MDAMTNKRLRLTLKTVRAFIFLGAFAALAAAAVFMTVILIAKYQGAPSVQVPQSTILYASDGSKLGETNYGEKRYWVPLKDMNPTIVKATVAIEDQNFYDHHGFDYKRMAGAALADLKAFAKVQGASTITQQYARNLYLEHDKTWKRKWNEAFYTIRLEQNYSKDEILEGYLNTIYYGHGAYGIEAASRLYFGKHAKNLTDAEAALLAGIPKGPSGYSPYVNETKAKERQKTIVRMMEKQQMISQKKADELIKEPLSYQPLNKQVSKRKAPYFYDNAMRELEKKLGMTREQIETSGLNVYTTVDKRMQRIAEETITETVNAGSDIQVGFSAIDPRTGNVLALVGGRDYQKSPFDRTTQAKRQPASTIKPLLYYKAIQSGFTPVTLMKSEETEFQIDAKGETYSPSNYNGYYANKPITLLQALALSDNIYAVKTHLFLGTNKLVKTAKEFGITAHLQALPSLALGTEPVRPIEMVNAYAMLANGGKKIEPTFISRVTDAAGHVLYENPNQHKQVLDEKAAFVTASMMTGMFDIDLNGYTSVTGRTIANRLTRTYAGKSGTTSADSWMIGFNPKLAAGVWTGYDKNSTIDSVEEKSYAKTIWADFMEDALKGEPETAFKPPKGVTGVYIDPETGYSSGPGCAAKHYTYFVKGTEPANVCYGAEPAKQTKDRLPSKEKPASEKKWWDKWLGRHH |
| Enzyme Length | 691 |
| Uniprot Accession Number | P70997 |
| Absorption | |
| Active Site | ACT_SITE 94; /note=Proton donor; for transglycosylase activity; /evidence=ECO:0000250|UniProtKB:P02919; ACT_SITE 365; /note=Acyl-ester intermediate; for transpeptidase activity; /evidence=ECO:0000250|UniProtKB:P02919 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+); Xref=Rhea:RHEA:23708, Rhea:RHEA-COMP:9602, Rhea:RHEA-COMP:9603, ChEBI:CHEBI:15378, ChEBI:CHEBI:58405, ChEBI:CHEBI:60033, ChEBI:CHEBI:78435; EC=2.4.1.129; Evidence={ECO:0000250|UniProtKB:P02918}; 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:0000250|UniProtKB:P02918}; |
| DNA Binding | |
| EC Number | 2.4.1.129; 3.4.16.4 |
| Enzyme Function | FUNCTION: Involved in the polymerization and cross-linking of spore peptidoglycan. May be required for synthesis of the spore germ cell wall, the first layer of peptidoglycan synthesized on the surface of the inner forespore membrane. {ECO:0000269|PubMed:10767540, ECO:0000269|PubMed:11567005}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Compositional bias (1); Frameshift (1); Region (3); Topological domain (2); Transmembrane (1) |
| Keywords | Carboxypeptidase;Cell membrane;Cell shape;Cell wall biogenesis/degradation;Glycosyltransferase;Hydrolase;Membrane;Multifunctional enzyme;Peptidoglycan synthesis;Protease;Reference proteome;Signal-anchor;Transferase;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 19192185; |
| Motif | |
| Gene Encoded By | |
| Mass | 77,037 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:23708 |
| Cross Reference Brenda |