| IED ID | IndEnz0002008345 |
| Enzyme Type ID | protease008345 |
| Protein Name |
Penicillin-binding protein 1B PBP-1b PBP1b Murein polymerase Includes: Penicillin-insensitive transglycosylase EC 2.4.1.129 Peptidoglycan TGase Peptidoglycan glycosyltransferase ; Penicillin-sensitive transpeptidase EC 3.4.16.4 DD-transpeptidase |
| Gene Name | mrcB pbpF ponB b0149 JW0145 |
| Organism | Escherichia coli (strain K12) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
| Enzyme Sequence | MAGNDREPIGRKGKPTRPVKQKVSRRRYEDDDDYDDYDDYEDEEPMPRKGKGKGKGRKPRGKRGWLWLLLKLAIVFAVLIAIYGVYLDQKIRSRIDGKVWQLPAAVYGRMVNLEPDMTISKNEMVKLLEATQYRQVSKMTRPGEFTVQANSIEMIRRPFDFPDSKEGQVRARLTFDGDHLATIVNMENNRQFGFFRLDPRLITMISSPNGEQRLFVPRSGFPDLLVDTLLATEDRHFYEHDGISLYSIGRAVLANLTAGRTVQGASTLTQQLVKNLFLSSERSYWRKANEAYMALIMDARYSKDRILELYMNEVYLGQSGDNEIRGFPLASLYYFGRPVEELSLDQQALLVGMVKGASIYNPWRNPKLALERRNLVLRLLQQQQIIDQELYDMLSARPLGVQPRGGVISPQPAFMQLVRQELQAKLGDKVKDLSGVKIFTTFDSVAQDAAEKAAVEGIPALKKQRKLSDLETAIVVVDRFSGEVRAMVGGSEPQFAGYNRAMQARRSIGSLAKPATYLTALSQPKIYRLNTWIADAPIALRQPNGQVWSPQNDDRRYSESGRVMLVDALTRSMNVPTVNLGMALGLPAVTETWIKLGVPKDQLHPVPAMLLGALNLTPIEVAQAFQTIASGGNRAPLSALRSVIAEDGKVLYQSFPQAERAVPAQAAYLTLWTMQQVVQRGTGRQLGAKYPNLHLAGKTGTTNNNVDTWFAGIDGSTVTITWVGRDNNQPTKLYGASGAMSIYQRYLANQTPTPLNLVPPEDIADMGVDYDGNFVCSGGMRILPVWTSDPQSLCQQSEMQQQPSGNPFDQSSQPQQQPQQQPAQQEQKDSDGVAGWIKDMFGSN |
| Enzyme Length | 844 |
| Uniprot Accession Number | P02919 |
| Absorption | |
| Active Site | ACT_SITE 233; /note=Proton donor; for transglycosylase activity; /evidence=ECO:0000305|PubMed:10564478; ACT_SITE 510; /note=Acyl-ester intermediate; for transpeptidase activity; /evidence=ECO:0000269|PubMed:10564478 |
| 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:0000269|PubMed:19458048, ECO:0000269|PubMed:6389538}; 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:0000269|PubMed:6389538}; |
| DNA Binding | |
| EC Number | 2.4.1.129; 3.4.16.4 |
| Enzyme Function | FUNCTION: Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross-linking of the peptide subunits). |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. |
| nucleotide Binding | |
| Features | Active site (2); Alternative sequence (1); Beta strand (41); Chain (1); Compositional bias (1); Erroneous initiation (1); Helix (31); Mutagenesis (3); Region (6); Sequence conflict (3); Topological domain (2); Transmembrane (1); Turn (8) |
| Keywords | 3D-structure;Alternative initiation;Antibiotic resistance;Carboxypeptidase;Cell inner membrane;Cell membrane;Cell shape;Cell wall biogenesis/degradation;Direct protein sequencing;Glycosyltransferase;Hydrolase;Membrane;Multifunctional enzyme;Peptidoglycan synthesis;Protease;Reference proteome;Signal-anchor;Transferase;Transmembrane;Transmembrane helix |
| Interact With | P0AD68; P29131; P0AB38 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell inner membrane; Single-pass type II membrane protein. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | NMR spectroscopy (2); Electron microscopy (1); X-ray crystallography (8) |
| Cross Reference PDB | 3FWL; 3VMA; 5FGZ; 5HL9; 5HLA; 5HLB; 5HLD; 6FZK; 6G5R; 6YN0; 7LQ6; |
| Mapped Pubmed ID | 16606699; 16858726; 17938168; 18165305; 20847002; 21183073; 21183074; 26731698; 27899450; 30044025; 33109614; 33986273; |
| Motif | |
| Gene Encoded By | |
| Mass | 94,293 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:23708 |
| Cross Reference Brenda | 2.4.1.129; |