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

Summary

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Gene symbol: pagP
Gene description: Lipid A palmitoyltransferase
Primary source: ASAP:ABE-0002139
Locus tag: b0622
See related: ECOCYC:EG12180
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_000913.3 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

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.
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.
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.
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.
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.
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.
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.
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.

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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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
enables transferase 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
located_in 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

NC_000913.3 Reference assembly

Range

656557..657117

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

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