ID   HOLIN_BPML5             Reviewed;         131 AA.
AC   Q05296;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 52.
DE   RecName: Full=Holin {ECO:0000255|HAMAP-Rule:MF_04168};
DE   AltName: Full=Gene product 11 {ECO:0000305};
DE            Short=gp11 {ECO:0000305};
GN   Name=11;
OS   Mycobacterium phage L5 (Mycobacteriophage L5).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Siphoviridae; Fromanvirus.
OX   NCBI_TaxID=31757;
OH   NCBI_TaxID=1763; Mycobacterium.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=8459766; DOI=10.1111/j.1365-2958.1993.tb01131.x;
RA   Hatfull G.F., Sarkis G.J.;
RT   "DNA sequence, structure and gene expression of mycobacteriophage L5: a
RT   phage system for mycobacterial genetics.";
RL   Mol. Microbiol. 7:395-405(1993).
CC   -!- FUNCTION: Accumulates harmlessly in the cytoplasmic membrane until it
CC       reaches a critical concentration that triggers the formation of micron-
CC       scale pores (holes) causing host cell membrane disruption and endolysin
CC       escape into the periplasmic space. Determines the precise timing of
CC       host cell lysis. Participates with the endolysin protein in the
CC       sequential events which lead to the programmed host cell lysis
CC       releasing the mature viral particles from the host cell.
CC       {ECO:0000255|HAMAP-Rule:MF_04168}.
CC   -!- SUBUNIT: Homomultimer. Self-associates to form a pore.
CC       {ECO:0000255|HAMAP-Rule:MF_04168}.
CC   -!- SUBCELLULAR LOCATION: Host cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_04168}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_04168}.
CC   -!- DOMAIN: The first transmembrane region undergoes a helix to beta-
CC       hairpin conformational change, which is responsible for its self-
CC       association and pore formation in the host membrane. The coiled coil
CC       region is required for host cell lysis and for cytotoxic activity. The
CC       C-terminus determines the size of the hole. {ECO:0000255|HAMAP-
CC       Rule:MF_04168}.
CC   -!- SIMILARITY: Belongs to the Mycobacterium phage D29 holin family.
CC       {ECO:0000255|HAMAP-Rule:MF_04168}.
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DR   EMBL; Z18946; CAA79387.1; -; Genomic_DNA.
DR   PIR; S30956; S30956.
DR   RefSeq; NP_039675.1; NC_001335.1.
DR   SMR; Q05296; -.
DR   GeneID; 2942970; -.
DR   KEGG; vg:2942970; -.
DR   Proteomes; UP000002123; Genome.
DR   GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR   HAMAP; MF_04168; HOLIN_D29; 1.
DR   InterPro; IPR032121; Myco_phage_holin.
DR   Pfam; PF16081; Phage_holin_7_1; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Cytolysis; Host cell inner membrane; Host cell lysis by virus;
KW   Host cell membrane; Host membrane; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix; Viral release from host cell.
FT   CHAIN           1..131
FT                   /note="Holin"
FT                   /id="PRO_0000164711"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04168"
FT   TRANSMEM        40..60
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04168"
FT   COILED          74..104
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   131 AA;  13353 MW;  B241D1B74A423EEF CRC64;
     MSPKIRQTIY LLGTAAPALL GIVLIWGGLD AESAADLGDI IAGVVSILVS GAPAVAAGTV
     RSQRKDGTLS TSPVDQVTKG VEQVLAARQS AEAEVAKVKQ ALETAVSGSL PQLGPLATQI
     LNVADDTVWR P