HOLIN_BPP22
ID HOLIN_BPP22 Reviewed; 108 AA.
AC P09962; Q7PCD7;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 07-APR-2021, entry version 95.
DE RecName: Full=Antiholin {ECO:0000303|PubMed:7831803};
DE AltName: Full=Lysis inhibitor 13-108 {ECO:0000303|PubMed:7831803};
GN Name=13;
OS Salmonella phage P22 (Bacteriophage P22).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Podoviridae; Lederbergvirus.
OX NCBI_TaxID=10754;
OH NCBI_TaxID=90371; Salmonella typhimurium.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=2998005; DOI=10.1016/0042-6822(85)90115-1;
RA Rennell D., Poteete A.R.;
RT "Phage P22 lysis genes: nucleotide sequences and functional relationships
RT with T4 and lambda genes.";
RL Virology 143:280-289(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Schicklmaier P., Huber J., Schmieger H.;
RL Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11053393; DOI=10.1128/jb.182.22.6472-6481.2000;
RA Vander Byl C.S., Kropinski A.M.B.;
RT "Sequence of the genome of Salmonella bacteriophage P22.";
RL J. Bacteriol. 182:6472-6481(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12562822; DOI=10.1128/jb.185.4.1475-1477.2003;
RA Pedulla M.L., Ford M.E., Karthikeyan T., Houtz J.M., Hendrix R.W.,
RA Hatfull G.F., Poteete A.R., Gilcrease E.B., Winn-Stapley D.A.,
RA Casjens S.R.;
RT "Corrected sequence of the bacteriophage P22 genome.";
RL J. Bacteriol. 185:1475-1477(2003).
RN [5]
RP FUNCTION, AND 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).
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. Determines
CC the precise timing of host cell lysis. Participates with the endolysin
CC and spanin proteins in the sequential events which lead to the
CC programmed host cell lysis releasing the mature viral particles from
CC the host cell. {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:0000303|PubMed:7831803}; Synonyms=Lysis inhibitor
CC 13-108 {ECO:0000303|PubMed:7831803};
CC IsoId=P09962-1; Sequence=Displayed;
CC Name=Holin {ECO:0000303|PubMed:7831803}; Synonyms=Lysis protein 13-105
CC {ECO:0000303|PubMed:7831803};
CC IsoId=P09962-2; Sequence=VSP_058251;
CC -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC {ECO:0000305}.
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 lambdavirus holin family. {ECO:0000305}.
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DR EMBL; M10997; AAA32265.1; -; Genomic_DNA.
DR EMBL; X67137; CAA47616.1; -; Genomic_DNA.
DR EMBL; AF217253; AAF75039.1; -; Genomic_DNA.
DR EMBL; BK000583; DAA01038.1; -; Genomic_DNA.
DR PIR; S22903; YVBPS2.
DR RefSeq; NP_059621.1; NC_002371.2. [P09962-1]
DR TCDB; 1.E.2.1.2; the Lambda holin s (Lambda holin) family.
DR GeneID; 1262842; -.
DR KEGG; vg:1262842; -.
DR Proteomes; UP000001795; Genome.
DR Proteomes; UP000007960; 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; IPR006481; Phage_lambda_GpS_holin.
DR Pfam; PF05106; Phage_holin_3_1; 1.
DR TIGRFAMs; TIGR01594; holin_lambda; 1.
PE 1: Evidence at protein level;
KW Alternative initiation; Cytolysis; Direct protein sequencing; Formylation;
KW Host cell inner membrane; Host cell lysis by virus; Host cell membrane;
KW Host membrane; Late protein; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Viral release from host cell.
FT CHAIN 1..108
FT /note="Antiholin"
FT /id="PRO_0000077653"
FT TOPO_DOM 1..38
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P03705"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 60..71
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P03705"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 93..108
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P03705"
FT VAR_SEQ 1..3
FT /note="Missing (in isoform Holin)"
FT /evidence="ECO:0000269|PubMed:7831803"
FT /id="VSP_058251"
FT TOPO_DOM P09962-2:1..6
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P03705"
FT TRANSMEM P09962-2:7..26
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P03705"
FT TOPO_DOM P09962-2:27..35
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P03705"
FT MOD_RES P09962-2:1
FT /note="N-formylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P03705"
SQ SEQUENCE 108 AA; 11682 MW; 6233F931AE7C787E CRC64;
MKKMPEKHDL LTAMMAAKEQ GIGAILAFAM AYLRGRYNGG AFKKTLIDAT MCAIIAWFIR
DLLVFAGLSS NLAYIASVFI GYIGTDSIGS LIKRFAAKKA GVDDANQQ
