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    appA light-/oxygen-sensing antirepressor AppA [ Cereibacter sphaeroides 2.4.1 ]

    Gene ID: 3718631, updated on 26-Dec-2024

    Summary

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    Gene symbol
    appA
    Gene description
    light-/oxygen-sensing antirepressor AppA
    Locus tag
    RSP_RS00740
    Gene type
    protein coding
    Organism
    Cereibacter sphaeroides 2.4.1 (strain: 2.4.1, culture-collection: ATCC:BAA-808, type-material: type strain of Rhodobacter sphaeroides)
    Lineage
    Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria; Rhodobacterales; Paracoccaceae; Cereibacter
    Old locus tag
    RSP_1565
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    Genomic context

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    Location:
    chromosome: 1
    Sequence:
    Chromosome: 1; NC_007493.2 (155127..156479, complement)

    Chromosome 1 - NC_007493.2Genomic Context describing neighboring genes Neighboring gene LLM class flavin-dependent oxidoreductase Neighboring gene AI-2E family transporter Neighboring gene sirohydrochlorin chelatase Neighboring gene ATP-binding protein

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_007493.2

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Role of active site conformational changes in photocycle activation of the AppA BLUF photoreceptor. Goyal P, et al. Proc Natl Acad Sci U S A, 2017 Feb 14. PMID 28137837, Free PMC Article
    2. Electron transfer quenching in light adapted and mutant forms of the AppA BLUF domain. Laptenok SP, et al. Faraday Discuss, 2015. PMID 25633480
    3. Redox and light control the heme-sensing activity of AppA. Yin L, et al. mBio, 2013 Aug 27. PMID 23982072, Free PMC Article
    4. Glutamine rotamers in BLUF photoreceptors: a mechanistic reappraisal. Udvarhelyi A, et al. J Phys Chem B, 2013 Mar 14. PMID 23421521
    5. On the midpoint potential of the FAD chromophore in a BLUF-domain containing photoreceptor protein. Arents JC, et al. FEBS Lett, 2011 Jan 3. PMID 21110976

    See all (15) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. The calculated energy gaps between the locally excited and charge-transfer states suggest that electron transfer from Tyr21 to the flavin is more facile for configurations conducive to proton transfer. When the active site conformation is not conducive to PCET from Tyr21, Trp104 can directly compete with Tyr21 for electron transfer to the flavin through a nonproductive pathway, impeding the signaling efficiency.
      Title: Role of active site conformational changes in photocycle activation of the AppA BLUF photoreceptor.
    2. If a charge separated state has a role in the AppA BLUF domain photocycle, it is only as a very short lived intermediate.
      Title: Electron transfer quenching in light adapted and mutant forms of the AppA BLUF domain.
    3. Light, redox, and heme are integrated inputs that control AppA's ability to disrupt the DNA binding activity of PpsR.
      Title: Redox and light control the heme-sensing activity of AppA.
    4. The study proposes physical criteria for the dark and light state structures as well as for the light-activation process to evaluate existing models of the flavin-binding BLUF domain of AppA using quantum-chemical calculations.
      Title: Glutamine rotamers in BLUF photoreceptors: a mechanistic reappraisal.
    5. Data show that the redox-midpoint potential of the FAD chromophore in the BLUF domain of anti-transcriptional regulator AppA equals approximately -260mV relative to the calomel electrode.
      Title: On the midpoint potential of the FAD chromophore in a BLUF-domain containing photoreceptor protein.
    6. While on the one hand, blue light is sensed by the flavin adenine dinucleotide-binding BLUF domain of AppA, on the other, light is absorbed by bacteriochlorophyll signals through PrrB/PrrA.
      Title: In vivo sensitivity of blue-light-dependent signaling mediated by AppA/PpsR or PrrB/PrrA in Rhodobacter sphaeroides.
    7. Expression of AppA is PrrA dependent. PrrA affects AppA transcription and posttranscriptional regulation.
      Title: Hierarchical regulation of photosynthesis gene expression by the oxygen-responsive PrrBA and AppA-PpsR systems of Rhodobacter sphaeroides.
    8. Study shows binding of the cofactor haem to a domain in the C-terminal part of AppA and redox activity of bound haem.
      Title: A haem cofactor is required for redox and light signalling by the AppA protein of Rhodobacter sphaeroides.
    9. Based on our data, we present a model for the interdependence of AppA/PpsR signaling and the PrrA transcriptional activator in light-dependent gene expression.
      Title: The AppA and PpsR proteins from Rhodobacter sphaeroides can establish a redox-dependent signal chain but fail to transmit blue-light signals in other bacteria.
    10. Results describe a time-resolved fluorescence spectroscopy and subpicosecond transient absorption spectroscopy study of the BLUF domain of wild-type AppA and a photoinactive Y21F mutant of AppA.
      Title: Time-resolved spectroscopic studies of the AppA blue-light receptor BLUF domain from Rhodobacter sphaeroides.
    Submit: New GeneRIF Correction See all GeneRIFs (12)

    General protein information

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    Preferred Names
    light-/oxygen-sensing antirepressor AppA

    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_007493.2 Reference assembly

      Range
      155127..156479 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. WP_011336839.1 light-/oxygen-sensing antirepressor AppA [Cereibacter sphaeroides]

      See identical proteins and their annotated locations for WP_011336839.1

      UniProtKB/TrEMBL
      Q3J677, Q53119
    Nucleotide Protein
    Heading Accession and Version