Detail Information for IndEnz0002001297
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