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mrcB PBP1Bgamma;peptidoglycan glycosyltransferase/peptidoglycan DD-transpeptidase MrcB [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 944843, updated on 23-Nov-2023

Summary

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Gene symbol
mrcB
Gene description
PBP1Bgamma;peptidoglycan glycosyltransferase/peptidoglycan DD-transpeptidase MrcB
Primary source
ASAP:ABE-0000516
Locus tag
b0149
See related
ECOCYC:EG10605
Gene type
protein coding
RefSeq status
PROVISIONAL
Organism
Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
Lineage
Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
Also known as
ECK0148; pbpF; ponB
Summary
MrcB is part of a complex with MltA and MipA. [More information is available at EcoGene: EG10605]. The murein sacculus (peptidoglycan) is a polymer made up of long chains of alternating N-acetylglucosamine and N-acetylmuramic acid residues crosslinked by peptide side chains. [More information is available at EcoCyc: EG10605].
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Genomic context

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Sequence:
NC_000913.3 (164730..167264)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene RNA 2',3'-cyclic phosphodiesterase Neighboring gene RNA-dependent NTPase HrpB Neighboring gene ferrichrome outer membrane transporter/phage receptor Neighboring gene iron(III) hydroxamate ABC transporter ATP binding subunit Neighboring gene iron(III) hydroxamate ABC transporter periplasmic binding protein

Genomic regions, transcripts, and products

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Genomic Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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Related articles in PubMed

  1. Class-A penicillin binding proteins do not contribute to cell shape but repair cell-wall defects. Vigouroux A, et al. Elife, 2020 Jan 6. PMID 31904338, Free PMC Article
  2. Peptidoglycan Remodeling Enables Escherichia coli To Survive Severe Outer Membrane Assembly Defect. Morè N, et al. mBio, 2019 Feb 5. PMID 30723128, Free PMC Article
  3. Structural Insights into Inhibition of Escherichia coli Penicillin-binding Protein 1B. King DT, et al. J Biol Chem, 2017 Jan 20. PMID 27899450, Free PMC Article
  4. Importance of the conserved residues in the peptidoglycan glycosyltransferase module of the class A penicillin-binding protein 1b of Escherichia coli. Terrak M, et al. J Biol Chem, 2008 Oct 17. PMID 18701463, Free PMC Article
  5. A method to assay penicillin-binding proteins. Pucci MJ, et al. Methods Mol Med, 2008. PMID 18437311

See all (119) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. Loss of cell wall integrity genes cpxA and mrcB causes flocculation in Escherichia coli.
    Title: Loss of cell wall integrity genes cpxA and mrcB causes flocculation in Escherichia coli.
  2. Upregulation of PBP1B and LpoB in cysB mutants confers mecillinam resistance in Escherichia coli.
    Title: Upregulation of PBP1B and LpoB in cysB Mutants Confers Mecillinam (Amdinocillin) Resistance in Escherichia coli.
  3. The lipoprotein LpoB is required to activate PBP1B, which is a major, bi-functional peptidoglycan synthase with glycan chain polymerising (glycosyltransferase) and peptide cross-linking (transpeptidase) activities. The authors show how the binding of LpoB to the regulatory UB2H domain of PBP1B activates both activities.
    Title: Induced conformational changes activate the peptidoglycan synthase PBP1B.
  4. The authors discovered that FtsBLQ inhibits the glycosyltransferase activity of PBP1b and that this inhibition was antagonized by the PBP1b activators FtsN and LpoB.
    Title: Regulation of the Peptidoglycan Polymerase Activity of PBP1b by Antagonist Actions of the Core Divisome Proteins FtsBLQ and FtsN.
  5. crystal structures of E. coli PBP1b bound to multiple different beta-lactams in the transpeptidase active site and complement these data with gel-based competition assays to provide a detailed structural understanding of its inhibition. Taken together, these biochemical and structural data allow us to propose new insights into inhibition of both enzymatic domains in PBP1b.
    Title: Structural Insights into Inhibition of Escherichia coli Penicillin-binding Protein 1B.
  6. the X-ray crystal structure of the bifunctional transglycosylase penicillin-binding protein 1b (PBP1b) from Escherichia coli in complex with its inhibitor moenomycin to 2.16-A resolution was determined.
    Title: Crystal structure of the membrane-bound bifunctional transglycosylase PBP1b from Escherichia coli.
  7. findings show that PBP1b is vital for competitive survival of E. coli during extended stationary phase; loss of PBP1b leads to the stationary phase-specific competition defective phenotype and causes cells to become more sensitive to osmotic stress
    Title: Role of penicillin-binding protein 1b in competitive stationary-phase survival of Escherichia coli.
  8. direct interaction between a class B PBP (PBP3) and a class A PBP (PBP1B) in vitro and in vivo, indicating that different murein synthases might act in concert to enlarge the murein sacculus during cell division
    Title: Interaction between two murein (peptidoglycan) synthases, PBP3 and PBP1B, in Escherichia coli.
Submit: New GeneRIF Correction

Pathways from PubChem

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Interactions

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Products Interactant Other Gene Complex Source Pubs Description

General gene information

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Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
enables carboxypeptidase activity IEA
Inferred from Electronic Annotation
more info
  
enables catalytic activity IEA
Inferred from Electronic Annotation
more info
  
enables glycosyltransferase activity IEA
Inferred from Electronic Annotation
more info
  
enables hydrolase activity IEA
Inferred from Electronic Annotation
more info
  
enables penicillin binding IBA
Inferred from Biological aspect of Ancestor
more info
  
enables penicillin binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables penicillin binding IEA
Inferred from Electronic Annotation
more info
  
enables peptidase activity IEA
Inferred from Electronic Annotation
more info
  
enables peptidoglycan glycosyltransferase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables peptidoglycan glycosyltransferase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables peptidoglycan glycosyltransferase activity IEA
Inferred from Electronic Annotation
more info
  
enables protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables serine-type D-Ala-D-Ala carboxypeptidase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables serine-type D-Ala-D-Ala carboxypeptidase activity IEA
Inferred from Electronic Annotation
more info
  
enables transferase activity IEA
Inferred from Electronic Annotation
more info
  
Process Evidence Code Pubs
involved_in cell wall organization IEA
Inferred from Electronic Annotation
more info
  
involved_in cell wall repair IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in metabolic process IEA
Inferred from Electronic Annotation
more info
  
involved_in peptidoglycan biosynthetic process IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in peptidoglycan biosynthetic process IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in peptidoglycan biosynthetic process IEA
Inferred from Electronic Annotation
more info
  
acts_upstream_of_or_within peptidoglycan biosynthetic process IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in peptidoglycan biosynthetic process IMP
Inferred from Mutant Phenotype
more info
 PubMed 
acts_upstream_of_or_within positive regulation of bipolar cell growth IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in proteolysis IEA
Inferred from Electronic Annotation
more info
  
involved_in regulation of cell shape IEA
Inferred from Electronic Annotation
more info
  
involved_in response to antibiotic IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in response to antibiotic IEA
Inferred from Electronic Annotation
more info
  
involved_in response to antibiotic IMP
Inferred from Mutant Phenotype
more info
 PubMed 
Component Evidence Code Pubs
located_in membrane HDA PubMed 
located_in membrane IEA
Inferred from Electronic Annotation
more info
  
is_active_in outer membrane-bounded periplasmic space IDA
Inferred from Direct Assay
more info
 PubMed 
located_in peptidoglycan-based cell wall IEA
Inferred from Electronic Annotation
more info
  
located_in plasma membrane IDA
Inferred from Direct Assay
more info
 PubMed 
located_in plasma membrane IEA
Inferred from Electronic Annotation
more info
  

General protein information

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Preferred Names
PBP1Bgamma;peptidoglycan glycosyltransferase/peptidoglycan DD-transpeptidase MrcB

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_000913.3 Reference assembly

    Range
    164730..167264
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_414691.1 peptidoglycan glycosyltransferase/peptidoglycan DD-transpeptidase MrcB [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for NP_414691.1

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A3G1CIG7
    Conserved Domains (1) summary
    PRK09506
    Location:1 → 843
    mrcB; bifunctional glycosyl transferase/transpeptidase; Reviewed

  2. YP_010051172.1 PBP1Bgamma [Escherichia coli str. K-12 substr. MG1655]

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A418GQX5
    Conserved Domains (1) summary
    PRK09506
    Location:20 → 798
    mrcB; bifunctional glycosyl transferase/transpeptidase; Reviewed
Nucleotide Protein
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