HOL26_BPSPP
ID HOL26_BPSPP Reviewed; 82 AA.
AC O48472;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 23-FEB-2022, entry version 63.
DE RecName: Full=Putative antiholin {ECO:0000250|UniProtKB:P27360};
GN Name=26;
OS Bacillus phage SPP1 (Bacteriophage SPP1).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Siphoviridae.
OX NCBI_TaxID=10724;
OH NCBI_TaxID=1423; Bacillus subtilis.
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=9434185; DOI=10.1016/s0378-1119(97)00547-7;
RA Alonso J.C., Luder G., Stiege A.C., Chai S., Weise F., Trautner T.A.;
RT "The complete nucleotide sequence and functional organization of Bacillus
RT subtilis bacteriophage SPP1.";
RL Gene 204:201-212(1997).
RN [2]
RP FUNCTION.
RX PubMed=27328857; DOI=10.1111/mmi.13448;
RA Fernandes S., Sao-Jose C.;
RT "More than a hole: the holin lethal function may be required to fully
RT sensitize bacteria to the lytic action of canonical endolysins.";
RL Mol. Microbiol. 102:92-106(2016).
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=27825035; DOI=10.1016/j.virol.2016.10.030;
RA Fernandes S., Sao-Jose C.;
RT "Probing the function of the two holin-like proteins of bacteriophage
RT SPP1.";
RL Virology 500:184-189(2017).
CC -!- FUNCTION: [Isoform Holin-like protein 26]: Probably functions as a
CC holin together with holin-like protein 26. Accumulates harmlessly in
CC the cytoplasmic membrane until it reaches a critical concentration that
CC triggers the formation of micron-scale pores (holes) causing host cell
CC membrane disruption and endolysin escape into the periplasmic space.
CC Determines the precise timing of host cell lysis.
CC {ECO:0000305|PubMed:27328857}.
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-like protein 26]: Homomultimer. Interacts with
CC isoform Antiholin; this interaction blocks the holin
CC homomultimerization and delays host cell lysis.
CC {ECO:0000250|UniProtKB:P03705}.
CC -!- SUBCELLULAR LOCATION: Host cell inner membrane
CC {ECO:0000269|PubMed:27825035}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Classified as a class II holin.
CC {ECO:0000250|UniProtKB:P27360}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=Antiholin {ECO:0000250|UniProtKB:P27360};
CC IsoId=O48472-1; Sequence=Displayed;
CC Name=Holin-like protein 26 {ECO:0000250|UniProtKB:P27360};
CC IsoId=O48472-2; Sequence=VSP_058890;
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DR EMBL; X97918; CAA66519.1; -; Genomic_DNA.
DR PIR; T42312; T42312.
DR RefSeq; NP_690704.1; NC_004166.2. [O48472-1]
DR SMR; O48472; -.
DR TCDB; 1.E.31.1.13; the spp1 holin (spp1 holin) family.
DR GeneID; 955250; -.
DR KEGG; vg:955250; -.
DR Proteomes; UP000002559; Genome.
DR GO; GO:0020002; C:host cell plasma membrane; IDA:CACAO.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR InterPro; IPR006479; Holin.
DR Pfam; PF04688; Holin_SPP1; 1.
DR TIGRFAMs; TIGR01592; holin_SPP1; 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; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix;
KW Viral release from host cell.
FT CHAIN 1..82
FT /note="Putative antiholin"
FT /evidence="ECO:0000250|UniProtKB:P27360"
FT /id="PRO_0000439631"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 9..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 26..40
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 41..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 58..82
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT VAR_SEQ 1..2
FT /note="Missing (in isoform Holin-like protein 26)"
FT /evidence="ECO:0000250|UniProtKB:P27360"
FT /id="VSP_058890"
SQ SEQUENCE 82 AA; 9391 MW; 558F709AD9E0D3A0 CRC64;
MKMDTGTKVR TILFLIAWVN QLLSFDNLEP IPVDETTAQQ VYDAVSVLFT IVVTVWTSFK
NNYLTLKGRK QREALKKNGL TK