Detail Information for IndEnz0002008555
IED ID IndEnz0002008555
Enzyme Type ID protease008555
Protein Name Penicillin-binding protein 1A
PBP-1a
PBP1a

Includes: Penicillin-insensitive transglycosylase
EC 2.4.1.129
Peptidoglycan TGase
; Penicillin-sensitive transpeptidase
EC 3.4.16.4
DD-transpeptidase
Gene Name mrcA ponA VC_2635
Organism Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Gammaproteobacteria Vibrionales Vibrionaceae Vibrio Vibrio cholerae Vibrio cholerae O1 Vibrio cholerae O1 biovar El Tor Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Enzyme Sequence MKFIKRLLVFSLICIILGVTTIFGFYFYVKSDLPDVATLRDVQLQTPMQVFSQDGKLIAQFGEKRRIPLKLEEMPKELIEAVIATEDSRYYEHYGFDPIGITRAAFAVLASGSASQGASTITQQLARNFFLSNEKKVMRKVKEIFIAIHIEQLLSKQEILELYLNKIYLGYRSYGVGAAAQAYFGKEVKDLTLGEIALIAGLPKAPSTMNPIYSVERATNRRNVVLQRMLDEKYITKAEYDAARAEPVLPKYHGAEIELNAPYVAEIARAWMVERYGEEAAYTSGMNVYTTVDSKLQRAANQAAINNLLAYDERHGYRGAEKELWQVNQPAWSSTQLSEYLSNEPTYGDMFPAAVLSVEEKSAQVWVKSYGVQTIAWEDMNWARRFINDDRQGPLPKSANEFLAAGQQIWVRPRTQDGAITAWKLTQVPNANTAFVAMNPENGAVTALVGGFNFVHNKFNRATQSVRQVGSSIKPFIYSAALNKGLTLATLINDAPINQWDESQGTAWRPKNSPPTYTGPTRLRIGLAQSKNVMAVRVLREVGLDETREYLTRFGFKLDQLPRSETIALGAGSLTPVQMAQGFSVFANNGYFVEPFYISRVENPFGNIEFSAEPKVVCHRECSSELDEFAEQDAASPYAPKVISEQNAFLTREMLYSNIWGGGEWSSDTGWNGTGWRAQALKRRDIGGKTGTTNDSKDAWYNGYAPGIVGVAWVGFDDHSRNLGKTAPNRNIEDDVSGAESGGKTALPAWVEFMSLALQDVPVQQKAVPNNIARVRIDRDTGLLTNKLDSSSMFEYFEAGTEPTEYVSEHVNESIYSTSSGEELF
Enzyme Length 825
Uniprot Accession Number Q9KNU5
Absorption
Active Site ACT_SITE 86; /note=Proton donor; for transglycosylase activity; /evidence=ECO:0000250|UniProtKB:P02919; ACT_SITE 471; /note=Acyl-ester intermediate; for transpeptidase activity; /evidence=ECO:0000250|UniProtKB:P02919
Activity Regulation
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:0000250|UniProtKB:P02918}; 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:P02918};
DNA Binding
EC Number 2.4.1.129; 3.4.16.4
Enzyme Function FUNCTION: Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross-linking of the peptide subunits). {ECO:0000250}.
Temperature Dependency
PH Dependency
Pathway PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
nucleotide Binding
Features Active site (2); Chain (1); Erroneous initiation (1); Region (2); Topological domain (2); Transmembrane (1)
Keywords Antibiotic resistance;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:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 91,987
Kinetics
Metal Binding
Rhea ID RHEA:23708
Cross Reference Brenda