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    degS serine endoprotease [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 947865, updated on 3-Dec-2024

    Summary

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    Official Symbol
    degS
    Official Full Name
    serine endoprotease
    Primary source
    ECOCYC:EG11652
    Locus tag
    b3235
    See related
    ASAP:ABE-0010611
    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
    ECK3224; hhoB; htrH
    Summary
    degS is an essential gene. [More information is available at EcoGene: EG11652]. Upon extracytoplasmic stress, misfolded/unfolded porins interact with the DegS PDZ domain, releasing an inhibitory interaction and activating DegS protease . [More information is available at EcoCyc: EG11652].
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    Genomic context

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    Sequence:
    NC_000913.3 (3382200..3383267)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene Z-ring associated protein G Neighboring gene periplasmic serine endoprotease Neighboring gene malate dehydrogenase Neighboring gene DNA-binding transcriptional dual regulator ArgR

    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. Expression, crystallization and crystallographic analysis of DegS, a stress sensor of the bacterial periplasm. Grininger M, et al. Acta Crystallogr D Biol Crystallogr, 2004 Aug. PMID 15272167
    2. Mechanisms for allosteric activation of protease DegS by ligand binding and oligomerization as revealed from molecular dynamics simulations. Lu C, et al. Proteins, 2016 Nov. PMID 27556733
    3. Structural analysis of DegS, a stress sensor of the bacterial periplasm. Zeth K. FEBS Lett, 2004 Jul 2. PMID 15225661
    4. Crystal structure of the DegS stress sensor: How a PDZ domain recognizes misfolded protein and activates a protease. Wilken C, et al. Cell, 2004 May 14. PMID 15137941
    5. Allosteric regulation of DegS protease subunits through a shared energy landscape. Mauldin RV, et al. Nat Chem Biol, 2013 Feb. PMID 23201899, Free PMC Article

    See all (45) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. The enhanced sigma E factor activity of DegS A323E substitution suppresses a number of assembly-defective conditions without exhibiting the toxicity associated with high levels of sigma E factor activity.
      Title: Fine-Tuning of σ(E) Activation Suppresses Multiple Assembly-Defective Mutations in Escherichia coli.
    2. Suppressor mutations in degS overcome the acute temperature-sensitive phenotype of DeltadegP and DeltadegP Deltatol-pal mutants of Escherichia coli.
      Title: Suppressor Mutations in degS Overcome the Acute Temperature-Sensitive Phenotype of ΔdegP and ΔdegP Δtol-pal Mutants of Escherichia coli.
    3. Mechanisms for allosteric activation of protease DegS by ligand binding and oligomerization has been described.
      Title: Mechanisms for allosteric activation of protease DegS by ligand binding and oligomerization as revealed from molecular dynamics simulations.
    4. DegS and RseB are proposed to be stress sensor proteins for sigmaE signal transduction [review]
      Title: Two stress sensor proteins for the expression of sigmaE regulon: DegS and RseB.
    5. analysis of allosteric regulation of DegS protease subunits through a shared energy landscape
      Title: Allosteric regulation of DegS protease subunits through a shared energy landscape.
    6. Allostery is an intrinsic property of the protease domain of DegS
      Title: Allostery is an intrinsic property of the protease domain of DegS: implications for enzyme function and evolution.
    7. The combined introduction of loop L2 and PDZ domain 1 of DegP into DegS converted DegS even further into a DegP-like protease.
      Title: Conversion of a regulatory into a degradative protease.
    8. 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.
    9. Self-cleavage occurs when HtrA reassembles back into the hexameric structure
      Title: Characterization of the autocleavage process of the Escherichia coli HtrA protein: implications for its physiological role.
    10. Residues involved in the DegS allosteric switch are conserved in the DegP/HtrA and HtrA2/Omi families, suggesting that many PDZ proteases use a common mechanism of allosteric activation.
      Title: Allosteric activation of DegS, a stress sensor PDZ protease.
    Submit: New GeneRIF Correction See all GeneRIFs (13)

    General gene information

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    Homology

    Gene Ontology Provided by EcoCyc

    Function Evidence Code Pubs
    enables endopeptidase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables identical protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables peptidase activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    enables protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables serine-type endopeptidase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables serine-type endopeptidase activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    enables serine-type peptidase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables serine-type peptidase activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Process Evidence Code Pubs
    acts_upstream_of_or_within cellular response to misfolded protein IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    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 outer membrane-bounded periplasmic space IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in plasma membrane IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

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    Preferred Names
    serine endoprotease

    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
      3382200..3383267
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_417702.1 serine endoprotease [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_417702.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A1V2GF05
      Conserved Domains (1) summary
      PRK10898
      Location:1 → 354
      PRK10898; serine endoprotease DegS
    Nucleotide Protein
    Heading Accession and Version

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