U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

Links from GEO Profiles

    • Showing Current items.

    rseP intramembrane zinc metalloprotease RseP [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 944871, updated on 3-Dec-2024

    Summary

    Go to the top of the page Help
    Official Symbol
    rseP
    Official Full Name
    intramembrane zinc metalloprotease RseP
    Primary source
    ECOCYC:EG12436
    Locus tag
    b0176
    See related
    ASAP:ABE-0000603
    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
    ecfE; ECK0175; yaeL
    Summary
    RpoE regulon. [More information is available at EcoGene: EG12436]. YaeL is a protease that resides in the inner membrane . [More information is available at EcoCyc: EG12436].
    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 (196546..197898)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene ditrans,polycis-undecaprenyl-diphosphate synthase [(2E,6E)-farnesyl-diphosphate specific] Neighboring gene CDP-diglyceride synthetase Neighboring gene outer membrane protein assembly factor BamA Neighboring gene periplasmic chaperone Skp

    Genomic regions, transcripts, and products

    Go to the top of the page Help
    Genomic Sequence:
    NC_000913.3

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

    Go to the top of the pageHelp

    Related articles in PubMed

    1. Biochemical Characterization of Function and Structure of RseP, an Escherichia coli S2P Protease. Hizukuri Y, et al. Methods Enzymol, 2017. PMID 28065260
    2. Roles of the membrane-reentrant β-hairpin-like loop of RseP protease in selective substrate cleavage. Akiyama K, et al. Elife, 2015 Oct 8. PMID 26447507, Free PMC Article
    3. A family of membrane-embedded metalloproteases involved in regulated proteolysis of membrane-associated transcription factors. Rudner DZ, et al. Proc Natl Acad Sci U S A, 1999 Dec 21. PMID 10611287, Free PMC Article
    4. Post-liberation cleavage of signal peptides is catalyzed by the site-2 protease (S2P) in bacteria. Saito A, et al. Proc Natl Acad Sci U S A, 2011 Aug 16. PMID 21810987, Free PMC Article
    5. Regulated intramembrane proteolysis: a control mechanism conserved from bacteria to humans. Brown MS, et al. Cell, 2000 Feb 18. PMID 10693756

    See all (39) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Instability of CII is needed for efficient switching between lytic and lysogenic development in bacteriophage 186.
      Title: Instability of CII is needed for efficient switching between lytic and lysogenic development in bacteriophage 186.
    2. we describe several methods for characterization of the proteolytic functions and structure of RseP mainly in vivo, including a proteolytic activity assay using model substrates, an in vitro analysis of cleavage of signal peptides in a detergent solution and in the membrane vesicles, structural analysis of membrane-embedded RseP based on the thiol modifiability of introduced cysteine residues, and the protein interaction
      Title: Biochemical Characterization of Function and Structure of RseP, an Escherichia coli S2P Protease.
    3. Mutations disturbing the possible beta-strand conformation of the loop impaired RseP proteolytic activity and that some of these mutations resulted in the differential cleavage of different substrates.
      Title: Roles of the membrane-reentrant β-hairpin-like loop of RseP protease in selective substrate cleavage.
    4. study concludes that recognition of the cleaved amino acid by the RseP PDZ domain is not essential for sequential cleavage of RseA and sigma(E) stress response in vivo
      Title: PDZ domains of RseP are not essential for sequential cleavage of RseA or stress-induced σ(E) activation in vivo.
    5. Escherichia coli RseP, an site-2 protease (S2P) family I-CLiP, introduces a cleavage into signal peptides after their signal peptidase-mediated liberation from preproteins
      Title: Post-liberation cleavage of signal peptides is catalyzed by the site-2 protease (S2P) in bacteria.
    6. after DegS cleavage, the newly exposed carboxyl terminus of RseA may facilitate Site-2 cleavage through direct interaction with the PDZ domain.
      Title: Cleavage of RseA by RseP requires a carboxyl-terminal hydrophobic amino acid following DegS cleavage.
    7. circularly permutated PDZ domains control RseP, the S2P family intramembrane protease of Escherichia coli
      Title: A pair of circularly permutated PDZ domains control RseP, the S2P family intramembrane protease of Escherichia coli.
    8. RseP catalyzes proteolytic cleavage of the membrane-bound anti-sigma(E) protein RseA as an essential step in transmembrane signal transduction in the sigma(E) extracytoplasmic stress response pathway.
      Title: Substrate recognition and binding by RseP, an Escherichia coli intramembrane protease.
    9. RseP, which is required for normal sigmaE activation, prevents toxicity due to the presence of two specific outer membrane proteins that are down-regulated by RseX
      Title: Down-regulation of porins by a small RNA bypasses the essentiality of the regulated intramembrane proteolysis protease RseP in Escherichia coli.
    Submit: New GeneRIF Correction

    General gene information

    Go to the top of the page Help

    Homology

    Gene Ontology Provided by EcoCyc

    Function Evidence Code Pubs
    enables anti-sigma factor antagonist activity EXP
    Inferred from Experiment
    more info
    		 PubMed 
    enables anti-sigma factor antagonist activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables anti-sigma factor antagonist activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    enables endopeptidase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables metal ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables metalloendopeptidase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables metalloendopeptidase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables metallopeptidase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    acts_upstream_of_or_within cellular response to cell envelope stress IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    acts_upstream_of_or_within positive regulation of DNA-templated transcription IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in proteolysis IEA
    Inferred from Electronic Annotation
    more info
    		  
    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
    		  

    General protein information

    Go to the top of the page Help
    Preferred Names
    intramembrane zinc metalloprotease RseP

    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

    1. NC_000913.3 Reference assembly

      Range
      196546..197898
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_414718.1 intramembrane zinc metalloprotease RseP [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_414718.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A8S7EC66
      Conserved Domains (1) summary
      PRK10779
      Location:2 → 450
      PRK10779; sigma E protease regulator RseP
    Nucleotide Protein
    Heading Accession and Version

    Gene LinkOut

    The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.