Literature summary for 2.7.8.36 extracted from

Entova, S.; Guan, Z.; Imperiali, B.
Investigation of the conserved reentrant membrane helix in the monotopic phosphoglycosyl transferase superfamily supports key molecular interactions with polyprenol phosphate substrates (2019), Arch. Biochem. Biophys., 675, 108111 .

Search for more literature for 2.7.8.36

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Campylobacter jejuni subsp. jejuni

Protein Variants

Protein Variants	Comment	Organism
P24A	the enrichment of undecaprenyl phosphate in the native membrane environment of PglC is largely abrogated by the mutation. Residue Pro24 plays a key role in polyprenyl phosphate binding and specificity	Campylobacter jejuni subsp. jejuni

Organism

Organism	UniProt	Comment	Textmining
Campylobacter jejuni subsp. jejuni	Q0P9D0	serotype O:2	-
Campylobacter jejuni subsp. jejuni ATCC 700819	Q0P9D0	serotype O:2	-

Synonyms

Synonyms	Comment	Organism
PglC	-	Campylobacter jejuni subsp. jejuni

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
additional information	-	wild-type SUMO-PglC shows cooperative denaturation in the presence of 300 microM undecaprenyl phopshate, with a 22.3 degree increase in thermal stability. Mutant P24A SUMO-PglC shows apparent stabilization at higher temperatures in 300 microM undecaprenyl phospate, but no longer exhibits cooperative denaturation and remains partially soluble even at elevated temperatures	Campylobacter jejuni subsp. jejuni

General Information

General Information	Comment	Organism
physiological function	a conserved proline residue in the reentrant membrane-helix drives polyprenol phosphate recognition and specificity. Polyprenol phosphates at physiologically relevant levels increase the disorder of the local lipid bilayer, this effect is confined to polyprenol phosphates with specific isoprene geometries	Campylobacter jejuni subsp. jejuni

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Release 2023.1 (January 2023)