IED ID | IndEnz0002008550 |
Enzyme Type ID | protease008550 |
Protein Name |
Penicillin-binding protein 2a PBP2a Cell wall synthase PBP2a Includes: Penicillin-insensitive transglycosylase EC 2.4.1.129 Peptidoglycan TGase Peptidoglycan glycosyltransferase ; Penicillin-sensitive transpeptidase EC 3.4.16.4 DD-transpeptidase |
Gene Name | pbp2a SPD_1821 |
Organism | Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) |
Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Lactobacillales Streptococcaceae Streptococcus Streptococcus pneumoniae Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) |
Enzyme Sequence | MKLDKLFEKFLSLFKKETSELEDSDSTILRRSRSDRKKLAQVGPIRKFWRRYHLTKIILILGLSAGLLVGIYLFAVAKSTNVNDLQNALKTRTLIFDREEKEAGALSGQKGTYVELTDISKNLQNAVIATEDRSFYKNDGINYGRFFLAIVTAGRSGGGSTITQQLAKNAYLSQDQTVERKAKEFFLALELSKKYSKEQILTMYLNNAYFGNGVWGVEDASKKYFGVSASEVSLDQAATLAGMLKGPELYNPLNSVEDSTNRRDTVLQNMVAAGYIDKNQETEAAEVDMTSQLHDKYEGKISDYRYPSYFDAVVNEAVSKYNLTEEEIVNNGYRIYTELDQNYQANMQIVYENTSLFPRAEDGTFAQSGSVALEPKTGGVRGVVGQVADNDKTGFRNFNYATQSKRSPGSTIKPLVVYTPAVEAGWALNKQLDNHTMQYDSYKVDNYAGIKTSREVPMYQSLAESLNLPAVATVNDLGVDKAFEAGEKFGLNMEKVDRVLGVALGSGVETNPLQMAQAYAAFANEGLMPEAHFISRIENASGQVIASHKNSQKRVIDKSVADKMTSMMLGTFTNGTGISSSPADYVMAGKTGTTEAVFNPEYTSDQWVIGYTPDVVISHWLGFPTTDENHYLAGSTSNGAAHVFRNIANTILPYTPGSTFTVENAYKQNGIAPANTKRQVQTNDNSQTDDNLSDIRGRAQSLVDEASRAISDAKIKEKAQTIWDSIVNLFR |
Enzyme Length | 731 |
Uniprot Accession Number | A0A0H2ZMF9 |
Absorption | |
Active Site | ACT_SITE 131; /note=Proton donor; for transglycosylase activity; /evidence=ECO:0000250|UniProtKB:Q8DNB6; ACT_SITE 410; /note=Acyl-ester intermediate; for transpeptidase activity; /evidence=ECO:0000250|UniProtKB:P02919 |
Activity Regulation | |
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:0000250|UniProtKB:Q8DNB6}; 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:Q8DNB6}; |
DNA Binding | |
EC Number | 2.4.1.129; 3.4.16.4 |
Enzyme Function | FUNCTION: Cell wall formation. Synthesis of cross-linked peptidoglycan (PG) from the lipid intermediates (By similarity). Binds dansylated lipid II and catalyzes the polymerization of glycan chains. Hydrolyzes S2d (N-benzoyl-D-alanylmercaptoacetic acid) molecule, a synthetic thiolester analog of cell wall stem peptide. Active against bocillin, a fluorescent penicillin. No transpeptidase activity with non-fluorescent lysine-containing lipid II as substrate (By similarity). {ECO:0000250|UniProtKB:P02918, ECO:0000250|UniProtKB:Q8DNB6}. |
Temperature Dependency | |
PH Dependency | |
Pathway | PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. {ECO:0000305}. |
nucleotide Binding | |
Features | Active site (2); Chain (1); Region (4); Topological domain (2); Transmembrane (1) |
Keywords | Acyltransferase;Antibiotic resistance;Carboxypeptidase;Cell membrane;Cell shape;Cell wall;Cell wall biogenesis/degradation;Glycosyltransferase;Hydrolase;Membrane;Multifunctional enzyme;Peptidoglycan synthesis;Protease;Secreted;Signal-anchor;Transferase;Transmembrane;Transmembrane helix |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:29487215}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q8DNB6}. Secreted, cell wall {ECO:0000305}. Note=Localizes to sites of new peptidoglycan (PG) synthesis at midcell independently of MacP. {ECO:0000269|PubMed:29487215}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 80,799 |
Kinetics | |
Metal Binding | |
Rhea ID | RHEA:23708 |
Cross Reference Brenda |