| IED ID | IndEnz0002003351 |
| Enzyme Type ID | protease003351 |
| Protein Name |
Peptidoglycan D,D-transpeptidase FtsI EC 3.4.16.4 Essential cell division protein FtsI Murein transpeptidase Penicillin-binding protein 3 PBP-3 Peptidoglycan synthase FtsI |
| Gene Name | ftsI pbpB b0084 JW0082 |
| Organism | Escherichia coli (strain K12) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
| Enzyme Sequence | MKAAAKTQKPKRQEEHANFISWRFALLCGCILLALAFLLGRVAWLQVISPDMLVKEGDMRSLRVQQVSTSRGMITDRSGRPLAVSVPVKAIWADPKEVHDAGGISVGDRWKALANALNIPLDQLSARINANPKGRFIYLARQVNPDMADYIKKLKLPGIHLREESRRYYPSGEVTAHLIGFTNVDSQGIEGVEKSFDKWLTGQPGERIVRKDRYGRVIEDISSTDSQAAHNLALSIDERLQALVYRELNNAVAFNKAESGSAVLVDVNTGEVLAMANSPSYNPNNLSGTPKEAMRNRTITDVFEPGSTVKPMVVMTALQRGVVRENSVLNTIPYRINGHEIKDVARYSELTLTGVLQKSSNVGVSKLALAMPSSALVDTYSRFGLGKATNLGLVGERSGLYPQKQRWSDIERATFSFGYGLMVTPLQLARVYATIGSYGIYRPLSITKVDPPVPGERVFPESIVRTVVHMMESVALPGGGGVKAAIKGYRIAIKTGTAKKVGPDGRYINKYIAYTAGVAPASQPRFALVVVINDPQAGKYYGGAVSAPVFGAIMGGVLRTMNIEPDALTTGDKNEFVINQGEGTGGRS |
| Enzyme Length | 588 |
| Uniprot Accession Number | P0AD68 |
| Absorption | |
| Active Site | ACT_SITE 307; /note="Acyl-ester intermediate"; /evidence="ECO:0000255|HAMAP-Rule:MF_02080, ECO:0000269|PubMed:3900044" |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by beta-lactam antibiotics such as penicillin, moenomycin, macarbomycin, furazlocillin and piperacillin. Antibiotics inhibit the activity by binding to the catalytic serine. {ECO:0000269|PubMed:3900044, ECO:0000269|PubMed:6450748, ECO:0000269|PubMed:7030331}. |
| 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_02080, ECO:0000269|PubMed:3531167, ECO:0000269|PubMed:6450748, ECO:0000269|PubMed:7030331}; |
| DNA Binding | |
| EC Number | 3.4.16.4 |
| Enzyme Function | FUNCTION: Essential cell division protein that catalyzes cross-linking of the peptidoglycan cell wall at the division septum (PubMed:1103132, PubMed:6450748, PubMed:9614966, PubMed:3531167, PubMed:7030331). Required for localization of FtsN (PubMed:9282742). {ECO:0000269|PubMed:1103132, ECO:0000269|PubMed:3531167, ECO:0000269|PubMed:6450748, ECO:0000269|PubMed:7030331, ECO:0000269|PubMed:9282742, ECO:0000269|PubMed:9614966}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. {ECO:0000255|HAMAP-Rule:MF_02080, ECO:0000269|PubMed:6450748}. |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (11); Chain (1); Helix (12); Mutagenesis (10); Propeptide (1); Topological domain (2); Transmembrane (1); Turn (3) |
| Keywords | 3D-structure;Carboxypeptidase;Cell cycle;Cell division;Cell inner membrane;Cell membrane;Cell shape;Cell wall biogenesis/degradation;Hydrolase;Membrane;Peptidoglycan synthesis;Protease;Reference proteome;Septation;Transmembrane;Transmembrane helix |
| Interact With | P0AEN4; P29131; P06136; P0ABG4; P02919; P46022; P58034; Q8DQM0 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_02080, ECO:0000269|PubMed:2677607, ECO:0000269|PubMed:9614966}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_02080, ECO:0000269|PubMed:2677607, ECO:0000269|PubMed:9614966}; Periplasmic side {ECO:0000269|PubMed:2677607, ECO:0000269|PubMed:9614966}. Note=The bulk of the molecule, except for the N-terminal membrane anchor region, protrudes into the periplasmic space (PubMed:2677607, PubMed:9614966). Localizes to the division septum during the later stages of cell growth and throughout septation (PubMed:9379897, PubMed:9603865, PubMed:9882665, PubMed:15601716). Localization is dependent on FtsZ, FtsA, FtsK, FtsQ, FtsL and FtsW, but not on FtsN (PubMed:9603865, PubMed:9882665, PubMed:11703663, PubMed:11807049). {ECO:0000269|PubMed:11703663, ECO:0000269|PubMed:11807049, ECO:0000269|PubMed:15601716, ECO:0000269|PubMed:2677607, ECO:0000269|PubMed:9379897, ECO:0000269|PubMed:9603865, ECO:0000269|PubMed:9614966, ECO:0000269|PubMed:9882665}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 6HZQ; 7ONW; |
| Mapped Pubmed ID | 15690043; 15774864; 16606699; 17938168; 18165305; 18978050; 19880599; 20079830; 22885295; 23756461; 24561554; 31301409; 34356681; |
| Motif | |
| Gene Encoded By | |
| Mass | 63,877 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |