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1.E.1.1.1
Lysis protein S; also called ''pinholin'' or pinholin S(21)68, of 71 aas and 2 TMSs. It forms small heptameric pores that depolarize the membrane (Park et al., 2007; Pang et al., 2009).  This holin is of topological Class II, forming 2 TMSs, with the N- and C-termini inside (Park et al. 2006). TMS1 partially externalizes from the lipid bilayer regulates channel-formation and interacts with the membrane surface, whereas TMS2 remains buried in the lipid bilayer in the active conformation and forms the pore (Ahammad et al. 2019). Pinholin S(21)68 triggers the lytic cycle of bacteriophage phi21 in infected Escherichia coli. Activated transmembrane dimers oligomerize into small holes and uncouple the proton gradient. Structural models have been proposed for (1) the oligomeric pinhole (right-handed heptameric TMD2 bundle), (2) the active dimer (right-handed Gly-zipped TMD2/TMD2 dimer), and (3) the full-length pinholin protein before being triggered (Gly-zipped TMD2/TMD1-TMD1/TMD2 dimer in a line) (Steger et al. 2020).

Accession Number:P27360
Protein Name:VLYS aka S
Length:71
Molecular Weight:7893.00
Species:Bacteriophage P21 (Bacteriophage 21) [10711]
Number of TMSs:2
Location1 / Topology2 / Orientation3: Cell membrane1 / Multi-pass membrane protein2
Substrate endolysin, small molecules

Cross database links:

Pfam: PF04971   

Gene Ontology

GO:0016998 P:cell wall macromolecule catabolic process
GO:0019835 P:cytolysis

References (1)

[1] “Dual start motif in two lambdoid S genes unrelated to lambda S.”  Bonovich M.T.et.al.   2019562

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MKSMDKISTG IAYGTSAGSA GYWFLQWLDQ VSPSQWAAIG VLGSLVLGFL TYLTNLYFKI 
61:	REDRRKAARG E