Literature summary for 3.1.13.1 extracted from

Lu, F.; Taghbalout, A.
Membrane association via an amino-terminal amphipathic helix is required for the cellular organization and function of RNase II (2013), J. Biol. Chem., 288, 7241-7251.

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Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
cell surface	RNase II is organized into cellular structures that appear to coil around the Escherichia coli cell periphery. The ability of RNase II to maintain cell viability in the absence of exoribonuclease polynucleotide phosphorylase is markedly diminished when the RNase II cellular structures are lost due to changes in the amphipathicity of the amino-terminal helix	Escherichia coli	9986	-
membrane	RNase II is associated with the cytoplasmic membrane by its amino-terminal amphipathic helix. The helix also acts as an autonomous transplantable membrane binding domain capable of directing normally cytoplasmic proteins to the membrane	Escherichia coli	16020	-

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P30850	-	-

Synonyms

Synonyms	Comment	Organism
RNase II	-	Escherichia coli

General Information

General Information	Comment	Organism
physiological function	RNase II self-interaction and the ability of the protein to assemble into organized cellular structures requires the membrane binding domain. The ability of RNase II to maintain cell viability in the absence of exoribonuclease polynucleotide phosphorylase is markedly diminished when the RNase II cellular structures are lost due to changes in the amphipathicity of the amino-terminal helix	Escherichia coli

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Release 2023.1 (January 2023)