| IED ID | IndEnz0002001297 |
| Enzyme Type ID | protease001297 |
| Protein Name |
Peptidoglycan D,D-transpeptidase MrdA EC 3.4.16.4 Penicillin-binding protein 2 PBP-2 |
| Gene Name | mrdA pbpA b0635 JW0630 |
| Organism | Escherichia coli (strain K12) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
| Enzyme Sequence | MKLQNSFRDYTAESALFVRRALVAFLGILLLTGVLIANLYNLQIVRFTDYQTRSNENRIKLVPIAPSRGIIYDRNGIPLALNRTIYQIEMMPEKVDNVQQTLDALRSVVDLTDDDIAAFRKERARSHRFTSIPVKTNLTEVQVARFAVNQYRFPGVEVKGYKRRYYPYGSALTHVIGYVSKINDKDVERLNNDGKLANYAATHDIGKLGIERYYEDVLHGQTGYEEVEVNNRGRVIRQLKEVPPQAGHDIYLTLDLKLQQYIETLLAGSRAAVVVTDPRTGGVLALVSTPSYDPNLFVDGISSKDYSALLNDPNTPLVNRATQGVYPPASTVKPYVAVSALSAGVITRNTTLFDPGWWQLPGSEKRYRDWKKWGHGRLNVTRSLEESADTFFYQVAYDMGIDRLSEWMGKFGYGHYTGIDLAEERSGNMPTREWKQKRFKKPWYQGDTIPVGIGQGYWTATPIQMSKALMILINDGIVKVPHLLMSTAEDGKQVPWVQPHEPPVGDIHSGYWELAKDGMYGVANRPNGTAHKYFASAPYKIAAKSGTAQVFGLKANETYNAHKIAERLRDHKLMTAFAPYNNPQVAVAMILENGGAGPAVGTLMRQILDHIMLGDNNTDLPAENPAVAAAEDH |
| Enzyme Length | 633 |
| Uniprot Accession Number | P0AD65 |
| Absorption | |
| Active Site | ACT_SITE 330; /note="Acyl-ester intermediate"; /evidence="ECO:0000255|HAMAP-Rule:MF_02081, ECO:0000269|PubMed:3148617" |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by mecillinam and benzylpenicillin. {ECO:0000269|PubMed:1103132, ECO:0000269|PubMed:3009484}. |
| 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:0000255|HAMAP-Rule:MF_02081, ECO:0000269|PubMed:3009484}; |
| DNA Binding | |
| EC Number | 3.4.16.4 |
| Enzyme Function | FUNCTION: Catalyzes cross-linking of the peptidoglycan cell wall (PubMed:3009484). Responsible for the determination of the rod shape of the cell (PubMed:1103132). Is probably required for lateral peptidoglycan synthesis and maintenance of the correct diameter during lateral and centripetal growth (PubMed:12519203). {ECO:0000269|PubMed:1103132, ECO:0000269|PubMed:12519203, ECO:0000269|PubMed:3009484}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. {ECO:0000255|HAMAP-Rule:MF_02081, ECO:0000269|PubMed:3009484}. |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (22); Chain (1); Helix (27); Mutagenesis (1); Transmembrane (1); Turn (4) |
| Keywords | 3D-structure;Carboxypeptidase;Cell inner membrane;Cell membrane;Cell shape;Cell wall biogenesis/degradation;Direct protein sequencing;Hydrolase;Membrane;Peptidoglycan synthesis;Protease;Reference proteome;Transmembrane;Transmembrane helix |
| Interact With | P02918 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_02081, ECO:0000269|PubMed:1103132, ECO:0000269|PubMed:3009484}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_02081}. Note=Localizes preferentially in the lateral wall and at mid-cell in comparison with the old cell pole. Localization at mid-cell is dependent on active FtsI. {ECO:0000269|PubMed:12519203}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (3) |
| Cross Reference PDB | 6G9F; 6G9P; 6G9S; |
| Mapped Pubmed ID | 10969046; 11014799; 11051618; 11099493; 11254985; 11766406; 12107141; 15853883; 16606699; 16619114; 16751270; 17188233; 17581120; 1885519; 201607; 20706981; 2254246; 3073932; 30995398; 31061526; 6180685; 6300030; 6451612; |
| Motif | |
| Gene Encoded By | |
| Mass | 70,857 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |