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    bepA beta-barrel assembly-enhancing protease [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 947029, updated on 17-Dec-2024

    Summary

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    Official Symbol
    bepA
    Official Full Name
    beta-barrel assembly-enhancing protease
    Primary source
    ECOCYC:G7311
    Locus tag
    b2494
    See related
    ASAP:ABE-0008212
    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
    ECK2490; yfgC
    Summary
    Overexpression causes abnormal biofilm architecture. [More information is available at EcoGene: EG14199].
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    Genomic context

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    Sequence:
    NC_000913.3 (2616094..2617557)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene formate channel FocB Neighboring gene putative transporter YfgO Neighboring gene putative oxidoreductase YfgD Neighboring gene inibitor of reinitiation of DNA replication

    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. Structural Basis for the Function of the β-Barrel Assembly-Enhancing Protease BepA. Shahrizal M, et al. J Mol Biol, 2019 Feb 1. PMID 30521812
    2. Protease homolog BepA (YfgC) promotes assembly and degradation of β-barrel membrane proteins in Escherichia coli. Narita S, et al. Proc Natl Acad Sci U S A, 2013 Sep 17. PMID 24003122, Free PMC Article
    3. Edge-strand of BepA interacts with immature LptD on the β-barrel assembly machine to direct it to on- and off-pathways. Miyazaki R, et al. Elife, 2021 Aug 31. PMID 34463613, Free PMC Article
    4. Genetic architecture of intrinsic antibiotic susceptibility. Girgis HS, et al. PLoS One, 2009 May 20. PMID 19462005, Free PMC Article
    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 (14) citations in PubMed

    GeneRIFs: Gene References Into Functions

    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 metal ion binding ISM
    Inferred from Sequence Model
    more info
    		 PubMed 
    enables metalloendopeptidase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables metalloendopeptidase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables metalloendopeptidase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables metalloendopeptidase activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    enables metallopeptidase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables metallopeptidase activity RCA
    inferred from Reviewed Computational Analysis
    more info
    		 PubMed 
    enables peptidase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables protein disulfide isomerase activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    enables zinc ion binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables zinc ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    acts_upstream_of_or_within Gram-negative-bacterium-type cell outer membrane assembly EXP
    Inferred from Experiment
    more info
    		 PubMed 
    acts_upstream_of_or_within Gram-negative-bacterium-type cell outer membrane assembly IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in chaperone-mediated protein folding IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within chaperone-mediated protein folding IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in proteolysis IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within proteolysis involved in protein catabolic process EXP
    Inferred from Experiment
    more info
    		 PubMed 
    involved_in proteolysis involved in protein catabolic process IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    acts_upstream_of_or_within proteolysis involved in protein catabolic process IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    Component Evidence Code Pubs
    is_active_in membrane IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in membrane IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in membrane IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in outer membrane-bounded periplasmic space TAS
    Traceable Author Statement
    more info
    		 PubMed 
    located_in periplasmic space IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

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    Preferred Names
    beta-barrel assembly-enhancing protease
    NP_416989.1

    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
      2616094..2617557
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_416989.1 beta-barrel assembly-enhancing protease [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_416989.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A376WUW5, A0A8T3UHN6
      Conserved Domains (2) summary
      COG4783
      Location:1 → 486
      YfgC; Putative Zn-dependent protease, contains TPR repeats [General function prediction only]
      sd00006
      Location:311 → 337
      TPR; TPR repeat [structural motif]
    Nucleotide Protein
    Heading Accession and Version

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