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HOLIN_BPPH2
ID   HOLIN_BPPH2             Reviewed;         131 AA.
AC   P11188; B3VMQ0;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   29-SEP-2021, entry version 82.
DE   RecName: Full=Antiholin {ECO:0000303|PubMed:7831803};
DE   AltName: Full=Gene product 14;
DE            Short=gp14;
DE   AltName: Full=Lysis inhibitor 14-131 {ECO:0000303|PubMed:7831803};
DE   AltName: Full=Protein p14;
DE   Includes:
DE     RecName: Full=Holin {ECO:0000303|PubMed:7831803};
DE     AltName: Full=Lysis protein 14-129 {ECO:0000303|PubMed:7831803};
GN   Name=14;
OS   Bacillus phage phi29 (Bacteriophage phi-29).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Salasmaviridae; Picovirinae; Salasvirus.
OX   NCBI_TaxID=10756;
OH   NCBI_TaxID=1423; Bacillus subtilis.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3803926; DOI=10.1016/0378-1119(86)90406-3;
RA   Vlcek C., Paces V.;
RT   "Nucleotide sequence of the late region of Bacillus phage phi 29 completes
RT   the 19,285-bp sequence of phi 29 genome. Comparison with the homologous
RT   sequence of phage PZA.";
RL   Gene 46:215-225(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3027653; DOI=10.1093/nar/14.24.10001;
RA   Garvey K.J., Saedi M.S., Ito J.;
RT   "Nucleotide sequence of Bacillus phage phi 29 genes 14 and 15: homology of
RT   gene 15 with other phage lysozymes.";
RL   Nucleic Acids Res. 14:10001-10008(1986).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Villegas A.P., Lingohr E.J., Ceyssens P.-J., Kropinski A.M.;
RL   Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   FUNCTION (ISOFORM HOLIN).
RX   PubMed=8432697; DOI=10.1128/jb.175.4.1038-1042.1993;
RA   Steiner M., Lubitz W., Blaesi U.;
RT   "The missing link in phage lysis of gram-positive bacteria: gene 14 of
RT   Bacillus subtilis phage phi 29 encodes the functional homolog of lambda S
RT   protein.";
RL   J. Bacteriol. 175:1038-1042(1993).
RN   [5]
RP   ALTERNATIVE INITIATION.
RX   PubMed=7831803; DOI=10.1016/s0042-6822(95)80063-8;
RA   Tedin K., Resch A., Steiner M., Blaesi U.;
RT   "Dual translational start motif evolutionarily conserved in the holin gene
RT   of Bacillus subtilis phage phi 29.";
RL   Virology 206:479-484(1995).
RN   [6]
RP   REVIEW.
RX   PubMed=8878031; DOI=10.1046/j.1365-2958.1996.331395.x;
RA   Blasi U., Young R.;
RT   "Two beginnings for a single purpose: the dual-start holins in the
RT   regulation of phage lysis.";
RL   Mol. Microbiol. 21:675-682(1996).
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 (Probable).
CC       Determines the precise timing of host cell lysis (By similarity).
CC       Participates with the endolysin and spanin proteins in the sequential
CC       events which lead to the programmed host cell lysis releasing the
CC       mature viral particles from the host cell (By similarity).
CC       {ECO:0000250|UniProtKB:P03705, ECO:0000305|PubMed:8432697}.
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:0000269|PubMed:7831803};
CC         IsoId=P11188-1; Sequence=Displayed;
CC       Name=Holin {ECO:0000269|PubMed:7831803};
CC         IsoId=P11188-2; Sequence=VSP_058249;
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; M14782; AAA32287.1; -; Genomic_DNA.
DR   EMBL; X04962; CAA28631.1; -; Genomic_DNA.
DR   EMBL; EU771092; ACE96037.1; -; Genomic_DNA.
DR   PIR; A24721; WMBP29.
DR   RefSeq; YP_002004543.1; NC_011048.1. [P11188-1]
DR   SMR; P11188; -.
DR   TCDB; 1.E.10.1.1; the bacillus subtilis Phi29 holin (Phi29 holin) family.
DR   GeneID; 6446519; -.
DR   KEGG; vg:6446519; -.
DR   Proteomes; UP000001207; 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   GO; GO:0044659; P:viral release from host cell by cytolysis; IDA:UniProtKB.
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; Reference proteome; Transmembrane; Transmembrane helix;
KW   Viral release from host cell.
FT   CHAIN           1..131
FT                   /note="Antiholin"
FT                   /id="PRO_0000106598"
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:0000269|PubMed:7831803"
FT                   /id="VSP_058249"
FT   CONFLICT        78..81
FT                   /note="PAGL -> LRVY (in Ref. 1; AAA32287)"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        P11188-2:1..14
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P03705"
FT   TRANSMEM        P11188-2:15..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P03705"
FT   TOPO_DOM        P11188-2:38..49
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P03705"
SQ   SEQUENCE   131 AA;  15032 MW;  9739B9F0D566C3D9 CRC64;
     MKMIAWMQHF LETDETKLIY WLTFLMVCMV VDTVLGVLFA KLNPNIKFSS FKIKTGVLIK
     VSEMILALLA IPFAVPFPAG LPLLYTVYTA LCVSEIYSIF GHLRLVDDKS DFLEILENFF
     KRTSGKNKEE K
 
 
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