| IED ID | IndEnz0002001142 |
| Enzyme Type ID | protease001142 |
| Protein Name |
Penicillin-binding protein 1A PBP1a Includes: Penicillin-insensitive transglycosylase EC 2.4.1.129 Peptidoglycan TGase ; Penicillin-sensitive transpeptidase EC 3.4.16.4 DD-transpeptidase |
| Gene Name | pbpA CLB_3112 |
| Organism | Clostridium botulinum (strain ATCC 19397 / Type A) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Clostridia Eubacteriales Clostridiaceae Clostridium Clostridium botulinum Clostridium botulinum A Clostridium botulinum (strain ATCC 19397 / Type A) |
| Enzyme Sequence | MGKKKKKRKSSAFKIILNVFLSIFLVAGVAFGGIVFAMIKTAPPLNVQQVLTFDEPSILYDDKGQYMDKVITNEQRIVVDYKNVPQNLKNAFVSIEDERFYKHHGVDIKRFTGVILINVTNKIKRSSKLQGASTLTQQLIKNTVLSSEVSIKRKVQEMYLSIQLEKELSKDEILGAYMNSIFLGGNALGVEAASKQYFNKSVKDLSLIECAFIAGVPQSPSVYYPYSSASKKNPSIYLNRTKTVLYKMLDNGYITQNDYNKALKDLDSKKLVFAKPSAPSNKLAYEWFSIPAIEQVKKDLKTQYKYDDKQIHNLLVNGGLKVYTTMNKNLQDKTQNTINNAYYLNSYKSNGMIYPQASAVIMDYHNGEVKTIIGGRGDQPARSYNRAASYNYLRPAGSSIKPLTVYSAAIDSKKATAATGFEDSPIPNNIGRKYSSGAPYNPKNSPDIYYGYVNVREALMRSINVVAVKLVDKIGLNTSIQYAEKFGIPIDQHDRSSIASLSLGELHKGTNPLIMAQAYGVFGNNGTYTEAKLYTKVVDRTGKVLLEPKTNTKKVLSPEAAFITYDMLQGPVSESGTGPQANFGNMEVRGKTGTSSDMKNLWFCGLTPYYSAAVWIGNDNSSTVDGVYSSTAARLWGDIMKEFHVNLPYKQVQKPASVVTANVDRISGKLPTQLSYRDPRGSTVYNEFFINGTIPTEYDDIHVEAQINKLTGKLASKFTPSFLVESRVFLRRDYSPGVELLDQQWLLPYSIDEGGSLPPTEEKNNSNTRDKNKDKNKNKNKDKNPSQDKPNNNNNDNNSNNNNNNNDNNNNTKPPENDSNQNHEDNKNKQ |
| Enzyme Length | 830 |
| Uniprot Accession Number | A7FY32 |
| Absorption | |
| Active Site | ACT_SITE 96; /note=Proton donor; for transglycosylase activity; /evidence=ECO:0000250|UniProtKB:P02919; ACT_SITE 398; /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: 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). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Compositional bias (2); Region (3); Topological domain (2); Transmembrane (1) |
| Keywords | Antibiotic resistance;Carboxypeptidase;Cell membrane;Cell shape;Cell wall biogenesis/degradation;Glycosyltransferase;Hydrolase;Membrane;Multifunctional enzyme;Peptidoglycan synthesis;Protease;Signal-anchor;Transferase;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 92,704 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:23708 |
| Cross Reference Brenda |