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glpG rhomboid protease GlpG [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 947936, updated on 30-Jul-2025
Official Symbol
glpG
Official Full Name
rhomboid protease GlpG
Primary source
ECOCYC:EG10397
Locus tag
b3424
See related
ASAP:ABE-0011179
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
ECK3410
Summary
Six transmembrane regions verified. [More information is available at EcoGene: EG10397]. GlpG is a protease that may be involved in intramembrane proteolysis. [More information is available at EcoCyc: EG10397].
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Sequence:
NC_000913.3 (3560622..3561452, complement)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene RNA-splicing ligase Neighboring gene DNA-binding transcriptional activator RtcR Neighboring gene pseudo Neighboring gene thiosulfate sulfurtransferase GlpE Neighboring gene aerobic glycerol 3-phosphate dehydrogenase

Genomic Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Related articles in PubMed

  1. The Rhomboid Protease GlpG Promotes the Persistence of Extraintestinal Pathogenic Escherichia coli within the Gut. Russell CW, et al. Infect Immun, 2017 Jun. PMID 28373355, Free PMC Article
  2. Proteolytic action of GlpG, a rhomboid protease in the Escherichia coli cytoplasmic membrane. Maegawa S, et al. Biochemistry, 2005 Oct 18. PMID 16216077
  3. Functional characterization of Escherichia coli GlpG and additional rhomboid proteins using an aarA mutant of Providencia stuartii. Clemmer KM, et al. J Bacteriol, 2006 May. PMID 16621838, Free PMC Article
  4. Structural biology: enzyme theory holds water. Freeman M. Nature, 2006 Nov 9. PMID 17051148
  5. Crystal structure of a rhomboid family intramembrane protease. Wang Y, et al. Nature, 2006 Nov 9. PMID 17051161

See all (46) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. characterized the folding pathways of the Escherichia coli rhomboid protease GlpG and the human beta2-adrenergic receptor. Despite their evolutionary distance, both proteins fold in a strict N-to-C-terminal fashion, accruing structures in units of helical hairpins
    Title: Watching helical membrane proteins fold reveals a common N-to-C-terminal folding pathway.
  2. we present a detailed protocol for optimization of expression and purification of three rhomboid proteases from Escherichia coli (ecGlpG), Haemophilus influenzae (hiGlpG), and Providencia stuartii (AarA).
    Title: Production of Recombinant Rhomboid Proteases.
  3. The rhomboid protease GlpG, was found to promote extraintestinal pathogenic Escherichia coli survival within the mouse intestinal tract in the presence of the intact natural microbiota.
    Title: The Rhomboid Protease GlpG Promotes the Persistence of Extraintestinal Pathogenic Escherichia coli within the Gut.
  4. Unbinding of TM5 from the rest of the structure exposes GlpG's active site, consistent with studies of the catalytic mechanism of GlpG that suggest that TM5 serves as a substrate gate to the active site.
    Title: Topological constraints and modular structure in the folding and functional motions of GlpG, an intramembrane protease.
  5. Studied high-resolution structures of the catalytic transmembrane domain of the Escherichia coli GlpG rhomboid; this provided numerous insights that help explain how hydrolytic cleavage can be achieved below the membrane surface.
    Title: Influence of hydrophobic mismatch on the catalytic activity of Escherichia coli GlpG rhomboid protease.
  6. performed kinetic folding and unfolding experiments on 69 mutants (engineered every 2-3 residues throughout the 178-residue transmembrane domain) of GlpG, a membrane-embedded rhomboid protease from Escherichia coli
    Title: Cooperative folding of a polytopic α-helical membrane protein involves a compact N-terminal nucleus and nonnative loops.
  7. Peptidyl-chloromethylketones (CMKs) derived from the natural rhomboid substrate TatA from bacterium Providencia stuartii bind GlpG in a substrate-like manner, and their co-crystal structures with GlpG reveal the S1 to S4 subsites of the protease.
    Title: Substrate binding and specificity of rhomboid intramembrane protease revealed by substrate-peptide complex structures.
  8. Structure and mechanism of rhomboid protease.
    Title: Structure and mechanism of rhomboid protease.
  9. Data indicate that the rhomboid GlpG (ecGlpG) cytoplasmic domain exists as a dimer with extensive domain swapping between the two monomers.
    Title: Domain swapping in the cytoplasmic domain of the Escherichia coli rhomboid protease.
  10. GlpG is able to recognize and cleave truncated forms of MdfA but not the intact protein.
    Title: Cleavage of a multispanning membrane protein by an intramembrane serine protease.
Submit: New GeneRIF Correction See all GeneRIFs (18)
Products Interactant Other Gene Complex Source Pubs Description

Homology

Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
enables endopeptidase activity IMP
Inferred from Mutant Phenotype
more info
 PubMed 
enables hydrolase activity IEA
Inferred from Electronic Annotation
more info
  
enables identical protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables peptidase activity IEA
Inferred from Electronic Annotation
more info
  
enables serine-type endopeptidase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables serine-type endopeptidase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables serine-type endopeptidase activity IEA
Inferred from Electronic Annotation
more info
  
enables serine-type peptidase activity IEA
Inferred from Electronic Annotation
more info
  
Process Evidence Code Pubs
acts_upstream_of_or_within proteolysis IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in proteolysis IEA
Inferred from Electronic Annotation
more info
  
acts_upstream_of_or_within proteolysis IMP
Inferred from Mutant Phenotype
more info
 PubMed 
Component Evidence Code Pubs
located_in membrane 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
  
located_in plasma membrane ISM
Inferred from Sequence Model
more info
 PubMed 
located_in plasma membrane RCA
inferred from Reviewed Computational Analysis
more info
 PubMed 
Preferred Names
rhomboid protease GlpG
YP_026220.1

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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
    3560622..3561452 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. YP_026220.1 rhomboid protease GlpG

    See identical proteins and their annotated locations for YP_026220.1

    Status: REVIEWED

    UniProtKB/TrEMBL
    A0A895NRM7
    Conserved Domains (1) summary
    PRK10907
    Location:1 → 276
    PRK10907; intramembrane serine protease GlpG; Provisional
Nucleotide Protein
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