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    pagP Lipid A palmitoyltransferase [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 946360, updated on 17-Dec-2024

    Summary

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    Official Symbol
    pagP
    Official Full Name
    Lipid A palmitoyltransferase
    Primary source
    ECOCYC:EG12180
    Locus tag
    b0622
    See related
    ASAP:ABE-0002139
    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
    crcA; ECK0615; ybeG
    Summary
    Mg(2+) stimulon-PhoPQ regulon, EvgAS-PhoPQ cascade enhanced-expression subset. [More information is available at EcoGene: EG12180]. A PagP homodimer catalyzes palmitate transfer from a phospholipid (sn-1 position) to lipid A or to a lipid A precursor (N-linked hydroxymyristate on the proximal unit) . [More information is available at EcoCyc: EG12180].
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    Genomic context

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    Sequence:
    NC_000913.3 (656557..657117)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene sensor histidine kinase DpiB Neighboring gene DNA-binding transcriptional dual regulator DpiA Neighboring gene anaerobic C4-dicarboxylate transporter DcuC Neighboring gene transcription antiterminator and regulator of RNA stability CspE Neighboring gene F(-) channel protein

    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. Salvaging the Thermodynamic Destabilization of Interface Histidine in Transmembrane β-Barrels. Iyer BR, et al. Biochemistry, 2018 Dec 4. PMID 30284812, Free PMC Article
    2. Biosynthesis of lipid A precursors in Escherichia coli. A membrane-bound enzyme that transfers a palmitoyl residue from a glycerophospholipid to lipid X. Brozek KA, et al. J Biol Chem, 1987 Apr 15. PMID 3549717
    3. Further characterization of the PhoP regulon: identification of new PhoP-activated virulence loci. Belden WJ, et al. Infect Immun, 1994 Nov. PMID 7927792, Free PMC Article
    4. Identification of PhoP-PhoQ activated genes within a duplicated region of the Salmonella typhimurium chromosome. Gunn JS, et al. Microb Pathog, 1998 Aug. PMID 9712687
    5. Lipid A acylation and bacterial resistance against vertebrate antimicrobial peptides. Guo L, et al. Cell, 1998 Oct 16. PMID 9790526

    See all (39) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Here, we assign a thermodynamic measure for the extent to which a single proline can be tolerated at the C-terminal interface of the model transmembrane beta-barrel PagP
      Title: Molecular Switch between Structural Compaction and Thermodynamic Stability by the Xxx-Pro Interface in Transmembrane β-Barrels.
    2. Placing histidine at the C-terminus universally destabilizes PagP by 4.0-8.0 kcal mol(-1) irrespective of the neighboring residue. Spectroscopic and electrophoretic measurements indicate that the altered stability may arise from a loss of barrel compaction.
      Title: Salvaging the Thermodynamic Destabilization of Interface Histidine in Transmembrane β-Barrels.
    3. Biofilm-associated lipid A palmitoylation is triggered upon induction of pagP transcription by the hyperosmolar biofilm environment. pagP induction is regulated by RcsB, the response regulator of the Rcs stress response pathway, and is not observed under planktonic conditions.
      Title: Increased Osmolarity in Biofilm Triggers RcsB-Dependent Lipid A Palmitoylation in Escherichia coli.
    4. Data suggest that, as PagP folds and interacts with lipid bilayer/micelle, thermodynamic contribution of interface amino acid residues correlates with change in non-polar accessible surface area; C-terminal beta-sheet motif is a recognition signal and it exerts considerable influence on folding cooperativity and stability of the folded beta-barrel.
      Title: Energetics of side-chain partitioning of β-signal residues in unassisted folding of a transmembrane β-barrel protein.
    5. the effects of changing the membrane composition and the relative concentrations of protein and lipid on the folding mechanism of the bacterial outer membrane protein PagP were investigated.
      Title: Malleability of the folding mechanism of the outer membrane protein PagP: parallel pathways and the effect of membrane elasticity.
    6. Molecular dynamics, mutagenesis, and a 1.4 A crystal structure of PagP in an SDS / 2-methyl-2,4-pentanediol cosolvent system reveal that phospholipid access occurs at the crenel present between strands F and G of PagP.
      Title: PagP crystallized from SDS/cosolvent reveals the route for phospholipid access to the hydrocarbon ruler.
    7. Within the hydrophobic and van der Waals-contacted environment of the PagP hydrocarbon ruler, side chain flexibility, combined with localized thioether-aromatic dispersion attraction, likely influences the specificity of acyl chain selection.
      Title: Inscribing the perimeter of the PagP hydrocarbon ruler by site-specific chemical alkylation.
    8. crystal structure; a striking structural similarity between PagP and the lipocalins suggests an evolutionary link between these proteins
      Title: A hydrocarbon ruler measures palmitate in the enzymatic acylation of endotoxin.
    Submit: New GeneRIF Correction

    Interactions

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    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

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    Homology

    Gene Ontology Provided by EcoCyc

    Function Evidence Code Pubs
    enables O-palmitoyltransferase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables O-palmitoyltransferase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables acyltransferase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    acts_upstream_of_or_within lipid A biosynthetic process IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in lipid A biosynthetic process IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in lipid A biosynthetic process IEA
    Inferred from Electronic Annotation
    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
    		  

    General protein information

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    Preferred Names
    Lipid A palmitoyltransferase

    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
      656557..657117
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_415155.1 Lipid A palmitoyltransferase [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_415155.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A376ZRZ5
      Conserved Domains (1) summary
      PRK11045
      Location:3 → 186
      pagP; lipid IV(A) palmitoyltransferase PagP
    Nucleotide Protein
    Heading Accession and Version

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