HOLIN_BPPRD
ID HOLIN_BPPRD Reviewed; 117 AA.
AC Q3T4L9;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 02-JUN-2021, entry version 57.
DE RecName: Full=Holin;
DE AltName: Full=Protein P35;
GN Name=XXXV;
OS Enterobacteria phage PRD1 (Bacteriophage PRD1).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Kalamavirales; Tectiviridae; Alphatectivirus.
OX NCBI_TaxID=10658;
OH NCBI_TaxID=471; Acinetobacter calcoaceticus.
OH NCBI_TaxID=562; Escherichia coli.
OH NCBI_TaxID=584; Proteus mirabilis.
OH NCBI_TaxID=287; Pseudomonas aeruginosa.
OH NCBI_TaxID=294; Pseudomonas fluorescens.
OH NCBI_TaxID=303; Pseudomonas putida (Arthrobacter siderocapsulatus).
OH NCBI_TaxID=90371; Salmonella typhimurium.
OH NCBI_TaxID=666; Vibrio cholerae.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1853567; DOI=10.1016/0042-6822(91)90995-n;
RA Bamford J.K.H., Haenninen A.-L., Pakula T.M., Ojala P.M., Kalkkinen N.,
RA Frilander M., Bamford D.H.;
RT "Genome organization of membrane-containing bacteriophage PRD1.";
RL Virology 183:658-676(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15946683; DOI=10.1016/j.jmb.2005.04.059;
RA Saren A.M., Ravantti J.J., Benson S.D., Burnett R.M., Paulin L.,
RA Bamford D.H., Bamford J.K.H.;
RT "A snapshot of viral evolution from genome analysis of the tectiviridae
RT family.";
RL J. Mol. Biol. 350:427-440(2005).
RN [3]
RP FUNCTION, AND MUTAGENESIS.
RX PubMed=12813073; DOI=10.1128/jb.185.13.3795-3803.2003;
RA Rydman P.S., Bamford D.H.;
RT "Identification and mutational analysis of bacteriophage PRD1 holin protein
RT P35.";
RL J. Bacteriol. 185:3795-3803(2003).
RN [4]
RP FUNCTION.
RX PubMed=16030234; DOI=10.1128/jb.187.15.5397-5405.2005;
RA Ziedaite G., Daugelavicius R., Bamford J.K.H., Bamford D.H.;
RT "The holin protein of bacteriophage PRD1 forms a pore for small-molecule
RT and endolysin translocation.";
RL J. Bacteriol. 187:5397-5405(2005).
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
CC (PubMed:12813073, PubMed:16030234). Determines the precise timing of
CC host cell lysis (By similarity). Participates with the endolysin and
CC spanin proteins in the sequential events which lead to the programmed
CC host cell lysis releasing the mature viral particles from the host cell
CC (By similarity). {ECO:0000250|UniProtKB:P03705,
CC ECO:0000269|PubMed:12813073, ECO:0000269|PubMed:16030234}.
CC -!- FUNCTION: Isoform Antiholin: Counteracts the aggregation of the holin
CC molecules and thus of pore formation. {ECO:0000250|UniProtKB:P03705}.
CC -!- SUBUNIT: Homomultimer. Isoform Holin: Interacts with isoform Antiholin;
CC this interaction blocks the holin homomultimerization and delays host
CC 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY848689; AAX45922.1; -; Genomic_DNA.
DR RefSeq; YP_001542615.1; NC_001421.2.
DR TCDB; 1.E.5.1.1; the prd1 phage p35 holin (p35 holin) family.
DR Proteomes; UP000002143; 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:0003824; F:catalytic activity; IEA:UniProtKB-KW.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0044659; P:viral release from host cell by cytolysis; IDA:CACAO.
DR InterPro; IPR032126; LydA_holin.
DR Pfam; PF16083; Phage_holin_3_3; 1.
PE 3: Inferred from homology;
KW Antimicrobial; Bacteriolytic enzyme; 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..117
FT /note="Holin"
FT /id="PRO_0000234092"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 67..87
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 97..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 117 AA; 12778 MW; F73511CBE428EDC2 CRC64;
MMENDEWWKY LIFPLVATLG GIVNYSKRAL AMKRFSKLEF AVEAVSAAFV GLMVTLGGAA
MDLSPHWLGM AAGMSGWMGA DFVKAVFSQF VQSKIAPINQ PGPIDSDNDK PGRTFND
