IED ID | IndEnz0002009973 |
Enzyme Type ID | protease009973 |
Protein Name |
Penicillin-binding protein 1C PBP-1c PBP1c Includes: Penicillin-insensitive transglycosylase EC 2.4.1.129 Peptidoglycan TGase ; Transpeptidase-like module |
Gene Name | pbpC yfgN b2519 JW2503 |
Organism | Escherichia coli (strain K12) |
Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
Enzyme Sequence | MPRLLTKRGCWITLAAAPFLLFLAAWGADKLWPLPLHEVNPARVVVAQDGTPLWRFADADGIWRYPVTIEDVSPRYLEALINYEDRWFWKHPGVNPFSVARAAWQDLTSGRVISGGSTLTMQVARLLDPHPKTFGGKIRQLWRALQLEWHLSKREILTLYLNRAPFGGTLQGIGAASWAYLGKSPANLSYSEAAMLAVLPQAPSRLRPDRWPERAEAARNKVLERMAVQGVWSREQVKESREEPIWLAPRQMPQLAPLFSRMMLGKSKSDKITTTLDAGLQRRLEELAQNWKGRLPPRSSLAMIVVDHTDMRVRGWVGSVDLNDDSRFGHVDMVNSIRSPGSVLKPFVYGLALDEGLIHPASLLQDVPRRTGDYRPGNFDSGFHGPISMSEALVRSLNLPAVQVLEAYGPKRFAAKLRNVGLPLYLPNGAAPNLSLILGGAGAKLEDMAAAYTAFARHGKAGKLRLQPDDPLLERPLMSSGAAWIIRRIMADEAQPLPDSALPRVAPLAWKTGTSYGYRDAWAIGVNARYVIGIWTGRPDGTPVVGQFGFASAVPLLNQVNNILLSRSANLPEDPRPNSVTRGVICWPGGQSLPEGDGNCRRRLATWLLDGSQPPTLLLPEQEGINGIRFPIWLDENGKRVAADCPQARQEMINVWPLPLEPWLPASERRAVRLPPASTSCPPYGHDAQLPLQLTGVRDGAIIKRLPGAAEATLPLQSSGGAGERWWFLNGEPLTERGRNVTLHLTDKGDYQLLVMDDVGQIATVKFVMQ |
Enzyme Length | 770 |
Uniprot Accession Number | P76577 |
Absorption | |
Active Site | ACT_SITE 84; /note=Proton donor; for transglycosylase activity; /evidence=ECO:0000250|UniProtKB:P02919; ACT_SITE 342; /note=Acyl-ester intermediate; for transpeptidase activity; /evidence=ECO:0000250|UniProtKB:P02919 |
Activity Regulation | ACTIVITY REGULATION: Transglycosylase activity can be inhibited by moenomycin. |
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:10542235}; |
DNA Binding | |
EC Number | 2.4.1.129 |
Enzyme Function | FUNCTION: Cell wall formation. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a transpeptidase C-terminal domain which may not be functional. {ECO:0000269|PubMed:10542235}. |
Temperature Dependency | |
PH Dependency | |
Pathway | PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. |
nucleotide Binding | |
Features | Active site (2); Chain (1); Region (2); Topological domain (2); Transmembrane (1) |
Keywords | Carboxypeptidase;Cell inner membrane;Cell membrane;Cell shape;Cell wall biogenesis/degradation;Glycosyltransferase;Hydrolase;Membrane;Multifunctional enzyme;Peptidoglycan synthesis;Protease;Reference proteome;Signal-anchor;Transferase;Transmembrane;Transmembrane helix |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:10542235}; Single-pass type II membrane protein {ECO:0000250}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 10383966; 15690043; 15757509; 16606699; 18165305; 9449253; |
Motif | |
Gene Encoded By | |
Mass | 85,067 |
Kinetics | |
Metal Binding | |
Rhea ID | RHEA:23708 |
Cross Reference Brenda |