Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Combined Automated Annotation using Multiple IEA Methods
The T4 RI antiholin has an N-terminal signal anchor release domain that targets it for degradation by DegP.
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The C-terminal hydrophilic domain of RI localised to the periplasm is sufficient to impose lysis inhibition through specific interaction with the periplasmic domain of holin T.
"At the molecular level, this is due to the inhibition of the holin, T, by the antiholin, RI. RI is only 97 residues and contains an N-terminal hydrophobic domain and a C-terminal hydrophilic domain; expression of the latter domain fused to a secretory signal sequence is sufficient to impose LIN, due to its specific interaction with the periplasmic domain of the T holin."
The Phage T4 Antiholin RI Has a Cleavable Signal Peptide, Not a SAR Domain.
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RI possesses a cleavable N-terminal signal peptide and is processed and released into the host periplasm as a mature soluble protein.
"Here we show that, in contrast to previous reports, this domain of RI is a cleavable signal peptide. RI is processed and released into the periplasm as a mature protein, and inactivation of its signal peptidase cleavage site blocks processing and membrane release."
UniProtKB record for P13304 (RI_BPT4)
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RI mediates lysis inhibition in response to superinfection by inhibiting holin T multimerization.
"Involved in lysis inhibition. Senses superinfections and inhibits the holin, thereby delaying the host cell lysis timing. The genomic DNA from the superinfecting phage bound to the complex holin-antiholin probably serves as a signal for the lysis inhibition and blocks the holin multimerization."
Deep research summary for Enterobacteria phage T4 antiholin rI
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RI acts as an antiholin that binds holin T and prevents holin oligomerization and membrane permeabilization.
"**Primary function:** RI is a **T-holin inhibitor (antiholin)** that binds the holin and prevents holin **oligomerization/triggering**, delaying membrane permeabilization and therefore delaying endolysin access to peptidoglycan"