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    ompX outer membrane protein X [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 944967, updated on 3-Dec-2024

    Summary

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    Official Symbol
    ompX
    Official Full Name
    outer membrane protein X
    Primary source
    ECOCYC:EG12117
    Locus tag
    b0814
    See related
    ASAP:ABE-0002784
    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
    ECK0803; ompP; ybiG
    Summary
    ompX is nduced by acid or base. [More information is available at EcoGene: EG12135]. OmpX is a small (18 kDa) outer-membrane protein (OMP). [More information is available at EcoCyc: EG12117].
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    Genomic context

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    Sequence:
    NC_000913.3 (850450..850965)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene L-threonine/L-homoserine exporter Neighboring gene protein YliM Neighboring gene phosphoethanolamine transferase OpgE Neighboring gene ncRNA Neighboring gene small protein MntS

    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. Effective rotational correlation times of proteins from NMR relaxation interference. Lee D, et al. J Magn Reson, 2006 Jan. PMID 16188473
    2. Effect of hydrostatic pressure on the synthesis of outer membrane proteins in Escherichia coli. Nakashima K, et al. Biosci Biotechnol Biochem, 1995 Jan. PMID 7765962
    3. Identification and characterization of an outer membrane protein, OmpX, in Escherichia coli that is homologous to a family of outer membrane proteins including Ail of Yersinia enterocolitica. Mecsas J, et al. J Bacteriol, 1995 Feb. PMID 7836315, Free PMC Article
    4. Strategy for membrane protein crystallization exemplified with OmpA and OmpX. Pautsch A, et al. Proteins, 1999 Feb 1. PMID 10022352
    5. Structure and function of bacterial outer membrane proteins: barrels in a nutshell. Koebnik R, et al. Mol Microbiol, 2000 Jul. PMID 10931321

    See all (51) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Chaperone Spy Protects Outer Membrane Proteins from Folding Stress via Dynamic Complex Formation.
      Title: Chaperone Spy Protects Outer Membrane Proteins from Folding Stress via Dynamic Complex Formation.
    2. a systematic study of all charged side chains of the E. coli outer membrane protein X (OmpX) identifies three distinct salt-bridge clusters in the core of OmpX that contribute significantly to protein stability in dodecylphosphocholine detergent micelles.
      Title: The electrostatic core of the outer membrane protein X from E. coli.
    3. Real-time qRT-PCR confirmed that OmpX overexpression affected curli production by regulating the transcription of the curli biosynthesis-related genes in the DeltatolC strain.
      Title: Overexpression of Outer Membrane Protein X (OmpX) Compensates for the Effect of TolC Inactivation on Biofilm Formation and Curli Production in Extraintestinal Pathogenic Escherichia coli (ExPEC).
    4. Tyrosine at position 76 of outer membrane protein X (OmpX)increases unassisted barrel folding in dodecylphoshphocholine (DPC) micelles, and only one tryptophan affects the thermodynamic stability of OmpX barrel in micelles.
      Title: Position-Specific contribution of interface tryptophans on membrane protein energetics.
    5. The global lifetime of the OmpX-Skp and tOmpA-Skp chaperone-substrate complex is seven orders of magnitude longer, emerging from the short local lifetimes by avidity.
      Title: Conformation and dynamics of the periplasmic membrane-protein-chaperone complexes OmpX-Skp and tOmpA-Skp.
    6. The analysis of the simulations provides a detailed picture of the structural and dynamic features of the considered peptide at atomic resolution that is of high relevance in the understanding of the OmpX folding process.
      Title: Residual structure in a peptide fragment of the outer membrane protein X under denaturing conditions: a molecular dynamics study.
    7. Data show that in lipid bilayers, OmpX adopts a transmembrane orientation with a 7 degrees tilt of its beta-barrel axis relative to the membrane normal, matching the hydrophobic thickness of the barrel with that of the membrane.
      Title: Orientation of the Escherichia coli outer membrane protein OmpX in phospholipid bilayer membranes determined by solid-State NMR.
    8. The transcription of the cyaR gene is stringently controlled by cAMP-cAMP receptor protein and, unexpectedly, cyaR expression is also up-regulated, directly or indirectly, by sigma(E).
      Title: Down-regulation of outer membrane proteins by noncoding RNAs: unraveling the cAMP-CRP- and sigmaE-dependent CyaR-ompX regulatory case.
    9. Data show that OmpX is folded in both glass-supported oriented lipid bilayers and in lipid bicelles that can be magnetically oriented with the membrane plane parallel or perpendicular to the direction of the magnetic field.
      Title: NMR structural studies of the bacterial outer membrane protein OmpX in oriented lipid bilayer membranes.
    10. N-terminus verified by Edman degradation on mature peptide
      Title: Extraction of membrane proteins by differential solubilization for separation using two-dimensional gel electrophoresis.
    Submit: New GeneRIF Correction

    General gene information

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    Homology

    Gene Ontology Provided by EcoCyc

    Function Evidence Code Pubs
    enables protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    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
    		  
    located_in host outer membrane IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

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    Preferred Names
    outer membrane protein X

    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
      850450..850965
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_415335.1 outer membrane protein X [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_415335.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A2W6PXJ0
      Conserved Domains (1) summary
      PRK09408
      Location:1 → 171
      ompX; outer membrane protein OmpX
    Nucleotide Protein
    Heading Accession and Version

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