Literature summary for 3.4.25.2 extracted from

Baytshtok, V.; Chen, J.; Glynn, S.E.; Nager, A.R.; Grant, R.A.; Baker, T.A.; Sauer, R.T.
Covalently linked HslU hexamers support a probabilistic mechanism that links ATP hydrolysis to protein unfolding and translocation (2017), J. Biol. Chem., 292, 5695-5704 .

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Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0A6H5 and P0A7B8	P0A6H5 i.e. subunit HslU, P0A7B8 i.e. subunit HslV	-

General Information

General Information	Comment	Organism
physiological function	constrction of subunit HslU pseudohexamers containing mixtures of ATPase active and inactive subunits at defined positions in the hexameric ring. Genetic tethering impairs subunit HslV binding and degradation, even for pseudohexamers with six active subunits, but disulfide-linked pseudohexamers do not have these defects. Pseudohexamers containing different patterns of hydrolytically active and inactive subunits retain the ability to unfold protein substrates and/or collaborate with HslV in their degradation	Escherichia coli

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Release 2023.1 (January 2023)