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

Summary

Go to the top of the page Help

Official Symbol: mrcB
Official Full Name: PBP1Bgamma;peptidoglycan glycosyltransferase/peptidoglycan DD-transpeptidase MrcB
Primary source: ECOCYC:EG10605
Locus tag: b0149
See related: ASAP:ABE-0000516
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].
NEW: Try the new Gene table
Try the new Transcript table

Genomic context

Go to the top of the page Help

Sequence:: NC_000913.3 (164730..167264)

NC_000913.3 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

Go to the top of the page Help

Go to reference sequence details

Genomic Sequence:: NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

Go to the top of the page Help

GeneRIFs: Gene References Into Functions

What's a GeneRIF?

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.
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.
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.
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.
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.
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.
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.
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

Go to the top of the page

Interactions

Go to the top of the page Help

Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

Go to the top of the page Help

Homology

Orthologs from OrthoDB

Gene Ontology Provided by EcoCyc

Function	Evidence Code	Pubs
enables carboxypeptidase activity	IEA Inferred from Electronic Annotation more info
enables glycosyltransferase activity	IEA Inferred from Electronic Annotation 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

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 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	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 more info	PubMed
is_active_in outer membrane-bounded periplasmic space	IBA Inferred from Biological aspect of Ancestor 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

Go to the top of the page Help

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

NCBI Reference Sequences (RefSeq)

Go to the top of the page Help

NEW Try the new Transcript table

Genome Annotation

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

Reference assembly

Genomic

NC_000913.3 Reference assembly

Range

164730..167264

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

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
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