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

    Gene ID: 947936, updated on 3-Dec-2024

    Summary

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    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
    PROVISIONAL
    Organism
    Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
    Lineage
    Bacteria; 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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    Genomic context

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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 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. 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)

    Interactions

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    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

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    Homology

    Gene Ontology Provided by EcoCyc

    Function Evidence Code Pubs
    enables endopeptidase activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    enables identical protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    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 

    General protein information

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    Preferred Names
    rhomboid protease GlpG
    YP_026220.1

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

    mRNA and Protein(s)

    1. YP_026220.1 rhomboid protease GlpG [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for YP_026220.1

      Status: PROVISIONAL

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

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