ID   HOLIN_BPPZA             Reviewed;         131 AA.
AC   P07539;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1988, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Antiholin {ECO:0000250|UniProtKB:P11188};
DE   AltName: Full=Gene product 14;
DE            Short=gp14;
DE   AltName: Full=Lysis inhibitor 14-131 {ECO:0000250|UniProtKB:P11188};
DE   AltName: Full=Protein p14;
DE   Includes:
DE     RecName: Full=Holin {ECO:0000250|UniProtKB:P11188};
DE     AltName: Full=Lysis protein 14-129 {ECO:0000250|UniProtKB:P11188};
GN   Name=14;
OS   Bacillus phage PZA (Bacteriophage PZA).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Salasmaviridae; Picovirinae; Salasvirus; Bacillus virus PZA.
OX   NCBI_TaxID=10757;
OH   NCBI_TaxID=1423; Bacillus subtilis.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3095188; DOI=10.1016/0378-1119(86)90048-x;
RA   Paces V., Vlcek C., Urbanek P.;
RT   "Nucleotide sequence of the late region of Bacillus subtilis phage PZA, a
RT   close relative of phi 29.";
RL   Gene 44:107-114(1986).
CC   -!- FUNCTION: [Isoform Holin]: Accumulates harmlessly in the cytoplasmic
CC       membrane until it reaches a critical concentration that triggers the
CC       formation of micron-scale pores (holes) causing host cell membrane
CC       disruption and endolysin escape into the periplasmic space (By
CC       similarity). Determines the precise timing of host cell lysis (By
CC       similarity). Participates with the endolysin and spanin proteins in the
CC       sequential events which lead to the programmed host cell lysis
CC       releasing the mature viral particles from the host cell (By
CC       similarity). {ECO:0000250|UniProtKB:P03705}.
CC   -!- FUNCTION: [Isoform Antiholin]: Counteracts the aggregation of the holin
CC       molecules and thus of pore formation. {ECO:0000250|UniProtKB:P03705}.
CC   -!- SUBUNIT: [Isoform Holin]: Homomultimer. Interacts with isoform
CC       Antiholin; this interaction blocks the holin homomultimerization and
CC       delays host cell lysis. {ECO:0000250|UniProtKB:P03705}.
CC   -!- SUBCELLULAR LOCATION: Host cell inner membrane
CC       {ECO:0000250|UniProtKB:P03705}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P03705}. Note=Classified as a class I holin.
CC       {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative initiation; Named isoforms=2;
CC       Name=Antiholin {ECO:0000250|UniProtKB:P11188};
CC         IsoId=P07539-1; Sequence=Displayed;
CC       Name=Holin {ECO:0000250|UniProtKB:P11188};
CC         IsoId=P07539-2; Sequence=VSP_058250;
CC   -!- DOMAIN: Isoform Holin has 3 transmembrane regions whereas isoform
CC       Antiholin lacks the first transmembrane region.
CC       {ECO:0000250|UniProtKB:P03705}.
CC   -!- DOMAIN: The C-terminus acts as a cytoplasmic regulatory region.
CC       {ECO:0000250|UniProtKB:P03705}.
CC   -!- SIMILARITY: Belongs to the bacteriophage holin family. phi29likevirus
CC       holin subfamily. {ECO:0000305}.
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DR   EMBL; M11813; AAA88491.1; -; Genomic_DNA.
DR   PIR; I24831; WMBP14.
DR   SMR; P07539; -.
DR   Proteomes; UP000000855; 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   InterPro; IPR006480; Phage_holin_4_1.
DR   Pfam; PF05105; Phage_holin_4_1; 1.
DR   TIGRFAMs; TIGR01593; holin_tox_secr; 1.
PE   3: Inferred from homology;
KW   Alternative initiation; Cytolysis; Host cell inner membrane;
KW   Host cell lysis by virus; Host cell membrane; Host membrane; Late protein;
KW   Membrane; Transmembrane; Transmembrane helix; Viral release from host cell.
FT   CHAIN           1..131
FT                   /note="Antiholin"
FT                   /id="PRO_0000106599"
FT   TOPO_DOM        1..52
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P03705"
FT   TRANSMEM        53..75
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        76..78
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P03705"
FT   TRANSMEM        79..101
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        102..131
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P03705"
FT   VAR_SEQ         1..2
FT                   /note="Missing (in isoform Holin)"
FT                   /evidence="ECO:0000250|UniProtKB:P11188"
FT                   /id="VSP_058250"
FT   TOPO_DOM        P07539-2:1..15
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P03705"
FT   TRANSMEM        P07539-2:16..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        P07539-2:39..50
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P03705"
SQ   SEQUENCE   131 AA;  14977 MW;  46A23AE25A79C3D4 CRC64;
     MTMIAWMQHF LETDETKLIY WLTFLMVCMV VDTVLGVLFA KLNPNIKFSS FKIKTGVLIK
     VSEMILALLA VPFAVPFPAG LPLLYTVYTA LCVSEIYSIF GHLRLVDDKS DFLEILENFF
     KRTSGKNKED K