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mrcB PBP-1Bgamma;peptidoglycan glycosyltransferase/peptidoglycan DD-transpeptidase MrcB [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 944843, updated on 17-Jul-2025
Official Symbol
mrcB
Official Full Name
PBP-1Bgamma;peptidoglycan glycosyltransferase/peptidoglycan DD-transpeptidase MrcB
Primary source
ECOCYC:EG10605
Locus tag
b0149
See related
ASAP:ABE-0000516
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
Lineage
Bacteria; Pseudomonadati; 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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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 Fe(3(+)) hydroxamate ABC transporter ATP binding subunit Neighboring gene Fe(3(+)) hydroxamate ABC transporter periplasmic binding protein

Genomic Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Related articles in PubMed

  1. Variability of peptidoglycan surface density in Escherichia coli. Caparrós M, et al. FEMS Microbiol Lett, 1994 Aug 1. PMID 8082828
  2. Moenomycin-mediated affinity purification of penicillin-binding protein 1b. Stembera K, et al. Chembiochem, 2002 Apr 2. PMID 11933234
  3. Lipid II: total synthesis of the bacterial cell wall precursor and utilization as a substrate for glycosyltransfer and transpeptidation by penicillin binding protein (PBP) 1b of Escherichia coli. Schwartz B, et al. J Am Chem Soc, 2001 Nov 28. PMID 11716719
  4. Evaluation of bactericidal activity of cefotaxime and other beta-lactams by a novel method. Satta G, et al. Drugs, 1988. PMID 3293978
  5. Differential responses of Escherichia coli cells expressing cytoplasmic domain mutants of penicillin-binding protein 1b after impairment of penicillin-binding proteins 1a and 3. Chalut C, et al. J Bacteriol, 2001 Jan. PMID 11114917, Free PMC Article

See all (111) 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
Products Interactant Other Gene Complex Source Pubs Description

Homology

Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
enables peptidoglycan glycosyltransferase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
Process Evidence Code Pubs
involved_in peptidoglycan biosynthetic process IBA
Inferred from Biological aspect of Ancestor
more info
  
Component Evidence Code Pubs
is_active_in outer membrane-bounded periplasmic space IBA
Inferred from Biological aspect of Ancestor
more info
  
Preferred Names
PBP-1Bgamma;peptidoglycan glycosyltransferase/peptidoglycan DD-transpeptidase MrcB

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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

    See identical proteins and their annotated locations for NP_414691.1

    Status: REVIEWED

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

  2. YP_010051172.1 PBP-1Bgamma

    Status: REVIEWED

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