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    loiP metalloprotease LoiP [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 945173, updated on 3-Dec-2024

    Summary

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    Official Symbol
    loiP
    Official Full Name
    metalloprotease LoiP
    Primary source
    ECOCYC:EG11291
    Locus tag
    b2936
    See related
    ASAP:ABE-0009629
    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
    ECK2931; yggG
    Summary
    The heat shock protein YggG binds Era and mitigates the deleterious effect of overproducing mutant Era-1 protein (Huang, 2007). htpX, yggG, yfgC and ycaL are paralogs. [More information is available at EcoGene: EG11291]. YggG protein interacts directly with Era, an essential GTPase . [More information is available at EcoCyc: EG11291].
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    Genomic context

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    Sequence:
    NC_000913.3 (3081913..3082671)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene mannitol-specific PTS enzyme IIA component CmtB Neighboring gene transketolase 1 Neighboring gene agmatinase Neighboring gene biosynthetic arginine decarboxylase

    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 expression of truncated YggG protein and preparation of its polyclonal antibody]. Huang Y, et al. Xi Bao Yu Fen Zi Mian Yi Xue Za Zhi, 2004 Mar. PMID 15191718
    2. Influence of cyclic AMP, agmatine, and a novel protein encoded by a flanking gene on speB (agmatine ureohydrolase) in Escherichia coli. Szumanski MB, et al. J Bacteriol, 1992 Feb. PMID 1310091, Free PMC Article
    3. Analysis and sequence of the speB gene encoding agmatine ureohydrolase, a putrescine biosynthetic enzyme in Escherichia coli. Szumanski MB, et al. J Bacteriol, 1990 Feb. PMID 2153656, Free PMC Article
    4. Introduction of a stress-responsive gene, yggG, enhances the yield of L-phenylalanine with decreased acetic acid production in a recombinant Escherichia coli. Ojima Y, et al. Biotechnol Lett, 2009 Apr. PMID 19125225
    5. Proteolytic activity of HtpX, a membrane-bound and stress-controlled protease from Escherichia coli. Sakoh M, et al. J Biol Chem, 2005 Sep 30. PMID 16076848

    See all (17) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. We report that YggG of E. coli is a metalloprotease that cleaves its targets preferentially between Phe-Phe residues.
      Title: E. coli LoiP (YggG), a metalloprotease hydrolyzing Phe-Phe bonds.
    2. The expression regulation of the yggG gene under stress conditions and the YggG protein located on cell membrane are consistent with the bioinformatics analysis that YggG is functional as a heat shock protein that is associated with Era functions.
      Title: Expression and regulation of the yggG gene of Escherichia coli.
    3. The results indicated that YggG expression is significantly increased in response to stress caused by the Era-1 mutant protein in E. coli, thus promoting the growth of E. coli.
      Title: Up-regulation of yggG promotes the survival of Escherichia coli cells containing Era-1 mutant protein.
    Submit: New GeneRIF Correction

    General gene information

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    Homology

    Gene Ontology Provided by EcoCyc

    Function Evidence Code Pubs
    enables metal ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables metalloendopeptidase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables metalloendopeptidase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables metallopeptidase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables metallopeptidase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    Process Evidence Code Pubs
    acts_upstream_of_or_within cellular hypotonic response IEP
    Inferred from Expression Pattern
    more info
    		 PubMed 
    acts_upstream_of_or_within cellular response to UV IEP
    Inferred from Expression Pattern
    more info
    		 PubMed 
    acts_upstream_of_or_within cellular response to heat IEP
    Inferred from Expression Pattern
    more info
    		 PubMed 
    involved_in proteolysis IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in proteolysis involved in protein catabolic process IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    Component Evidence Code Pubs
    located_in cell outer membrane IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in cell outer membrane IEA
    Inferred from Electronic Annotation
    more info
    		  
    is_active_in membrane IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  

    General protein information

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    Preferred Names
    metalloprotease LoiP

    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
      3081913..3082671
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_417411.2 metalloprotease LoiP [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_417411.2

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A8T5YLC5
      Conserved Domains (1) summary
      cd07334
      Location:30 → 245
      M48C_loiP_like; Peptidase M48C Ste24p loiP-like, integral membrane protein
    Nucleotide Protein
    Heading Accession and Version

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