ID   VLYS_BPAPS              Reviewed;          94 AA.
AC   Q9T1T7;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 62.
DE   RecName: Full=Putative lysis protein S;
DE   AltName: Full=p11;
GN   Name=11;
OS   Acyrthosiphon pisum secondary endosymbiont phage 1 (Bacteriophage APSE-1).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Podoviridae; Sendosyvirus.
OX   NCBI_TaxID=2682836;
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10489345; DOI=10.1006/viro.1999.9902;
RA   van der Wilk F., Dullemans A.M., Verbeek M., van den Heuvel J.F.J.M.;
RT   "Isolation and characterization of APSE-1, a bacteriophage infecting the
RT   secondary endosymbiont of acyrthosiphon pisum.";
RL   Virology 262:104-113(1999).
CC   -!- FUNCTION: Essential for lysis of the bacterial cell wall by disrupting
CC       the cell membrane, thereby giving hydrolytic enzymes access to the cell
CC       wall. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the lambda phage S protein family.
CC       {ECO:0000305}.
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DR   EMBL; AF157835; AAF03954.1; -; Genomic_DNA.
DR   RefSeq; NP_050972.1; NC_000935.1.
DR   SMR; Q9T1T7; -.
DR   GeneID; 1262305; -.
DR   KEGG; vg:1262305; -.
DR   Proteomes; UP000000853; Genome.
DR   GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR006481; Phage_lambda_GpS_holin.
DR   Pfam; PF05106; Phage_holin_3_1; 1.
DR   TIGRFAMs; TIGR01594; holin_lambda; 1.
PE   3: Inferred from homology;
KW   Cytolysis; Host cell lysis by virus; Reference proteome;
KW   Viral release from host cell.
FT   CHAIN           1..94
FT                   /note="Putative lysis protein S"
FT                   /id="PRO_0000077652"
SQ   SEQUENCE   94 AA;  10589 MW;  C3EE1A3181150120 CRC64;
     MSEFCKPLLD ILRHQGTCAA LAFIMALLRA RYHRKDFYRS LLDALMCAML GGVAHELLQF
     LGLKADYSWL ASVAIGYLGV DRIGNWLKKK TGKL