pbpD
168
class A penicillin-binding protein 4
Locus
BSU_31490
Molecular weight
70.45 kDa
Isoelectric point
9.31
Function
bifunctional glucosyltransferase/ transpeptidase
Product
penicillin-binding protein 4
Essential
no
Synonyms
pbpD
Outlinks
Genomic Context
Categories containing this gene/protein
List of homologs in different organisms, belongs to COG0744 (Galperin et al., 2021)
This gene is a member of the following regulons
Gene
Coordinates
3,233,911 → 3,235,785
Phenotypes of a mutant
The protein
Catalyzed reaction/ biological activity
highly active transpeptidase, responsible for about 50% of D-amino acid incorporation PubMed
[GlcNAc-(1→4)-Mur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)](n)-diphospho-di-trans,octa-cis-undecaprenol + β-D-GlcNAc-(1→4)-Mur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)-diphospho-di-trans,octa-cis-undecaprenol --> [GlcNAc-(1→4)-Mur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-diphospho-di-trans-octa-cis-undecaprenol + di-trans,octa-cis-undecaprenyl diphosphate + H+ (according to UniProt)
Preferential cleavage: (Ac)(2)-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine (according to UniProt)
Protein family
N-terminal part: glycosyltransferase 51 family (according to UniProt)
C-terminal part: transpeptidase family (according to UniProt)
Structure
3VMA (PDB) (PBP1B from E. coli, 28% identity) PubMed
Paralogous protein(s)
cell membrane (according to UniProt)
during vegetative growth: septal, distinct spots at periphery PubMed
Additional information
loss of activity at alkaline pH PubMed
Expression and Regulation
Operons
Description
Sigma factors
Additional information
the terminator is NusA-dependent [ http://www.nature.com/articles/nmicrobiol20157 Reference]
Biological materials
Mutant
GFP fusion
References
Reviews
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Original Publications
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Time of last update: 2025-04-05 23:49:40
Author of last update: Jstuelk