Detail Information for IndEnz0002008550
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