HOLIN_BPT4
ID HOLIN_BPT4 Reviewed; 218 AA.
AC P06808;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 02-JUN-2021, entry version 91.
DE RecName: Full=Holin {ECO:0000255|HAMAP-Rule:MF_04104};
DE AltName: Full=Lysis protein;
DE AltName: Full=Protein rV;
GN Name=t; Synonyms=rV;
OS Enterobacteria phage T4 (Bacteriophage T4).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Myoviridae; Tevenvirinae; Tequatrovirus.
OX NCBI_TaxID=10665;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3628006; DOI=10.1093/nar/15.16.6736;
RA Montag D., Degen M., Henning U.;
RT "Nucleotide sequence of gene t (lysis gene) of the E. coli phage T4.";
RL Nucleic Acids Res. 15:6736-6736(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12626685; DOI=10.1128/mmbr.67.1.86-156.2003;
RA Miller E.S., Kutter E., Mosig G., Arisaka F., Kunisawa T., Ruger W.;
RT "Bacteriophage T4 genome.";
RL Microbiol. Mol. Biol. Rev. 67:86-156(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-34.
RX PubMed=2958637; DOI=10.1016/0022-2836(87)90519-5;
RA Montag D., Riede I., Eschbach M.-L., Degen M., Henning U.;
RT "Receptor-recognizing proteins of T-even type bacteriophages. Constant and
RT hypervariable regions and an unusual case of evolution.";
RL J. Mol. Biol. 196:165-174(1987).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 202-218.
RC STRAIN=D;
RX PubMed=8416914; DOI=10.1128/jb.175.1.85-93.1993;
RA Orsini G., Ouhammouch M., Le Caer J.-P., Brody E.N.;
RT "The asiA gene of bacteriophage T4 codes for the anti-sigma 70 protein.";
RL J. Bacteriol. 175:85-93(1993).
RN [5]
RP FUNCTION, AND TOPOLOGY.
RX PubMed=11255004; DOI=10.1016/s0378-1119(01)00365-1;
RA Ramanculov E., Young R.;
RT "Genetic analysis of the T4 holin: timing and topology.";
RL Gene 265:25-36(2001).
RN [6]
RP INTERACTION WITH HOLIN, AND SUBCELLULAR LOCATION.
RX PubMed=16166524; DOI=10.1128/jb.187.19.6631-6640.2005;
RA Tran T.A., Struck D.K., Young R.;
RT "Periplasmic domains define holin-antiholin interactions in t4 lysis
RT inhibition.";
RL J. Bacteriol. 187:6631-6640(2005).
RN [7]
RP FUNCTION, MUTAGENESIS OF CYS-175 AND CYS-207, AND DISULFIDE BOND.
RX PubMed=22389108; DOI=10.1002/pro.2042;
RA Moussa S.H., Kuznetsov V., Tran T.A., Sacchettini J.C., Young R.;
RT "Protein determinants of phage T4 lysis inhibition.";
RL Protein Sci. 21:571-582(2012).
RN [8]
RP INTERACTION WITH LYSIS INHIBITION ACCESSORY PROTEIN.
RX PubMed=27381920; DOI=10.1128/jb.00294-16;
RA Chen Y., Young R.;
RT "The last r locus unveiled: T4 RIII is a cytoplasmic antiholin.";
RL J. Bacteriol. 198:2448-2457(2016).
CC -!- FUNCTION: Accumulates harmlessly in the cytoplasmic membrane until it
CC reaches a critical concentration that triggers the formation of micron-
CC scale pores (holes) causing host cell membrane disruption and endolysin
CC escape into the periplasmic space. Determines the precise timing of
CC host cell lysis. Participates with the endolysin and spanin proteins in
CC the sequential events which lead to the programmed host cell lysis
CC releasing the mature viral particles from the host cell.
CC {ECO:0000255|HAMAP-Rule:MF_04104, ECO:0000269|PubMed:11255004,
CC ECO:0000269|PubMed:22389108}.
CC -!- SUBUNIT: Homomultimer. Interacts (via C-terminus) with antiholin (via
CC C-terminus); this interaction blocks the holin homomultimerization and
CC delays host cell lysis (PubMed:16166524). Interacts (via N-terminus)
CC with the lysis inhibition accessory protein rIII; this interaction
CC stabilizes the holin-antiholin complex thereby resulting in a robust
CC block of the hole formation (PubMed:27381920). {ECO:0000255|HAMAP-
CC Rule:MF_04104, ECO:0000269|PubMed:16166524,
CC ECO:0000269|PubMed:27381920}.
CC -!- SUBCELLULAR LOCATION: Host cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_04104, ECO:0000305|PubMed:16166524}; Single-pass type II
CC membrane protein {ECO:0000255|HAMAP-Rule:MF_04104,
CC ECO:0000305|PubMed:16166524}; Periplasmic side {ECO:0000255|HAMAP-
CC Rule:MF_04104, ECO:0000305|PubMed:16166524}. Note=Classified as a class
CC III holin. {ECO:0000255|HAMAP-Rule:MF_04104}.
CC -!- PTM: Disulfide bond is required for functionality. {ECO:0000255|HAMAP-
CC Rule:MF_04104, ECO:0000269|PubMed:22389108}.
CC -!- SIMILARITY: Belongs to the T4likevirus holin family.
CC {ECO:0000255|HAMAP-Rule:MF_04104}.
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; Y00408; CAA68470.1; -; Genomic_DNA.
DR EMBL; AF158101; AAD42661.1; -; Genomic_DNA.
DR EMBL; X05677; CAA29164.1; -; Genomic_DNA.
DR EMBL; M99441; AAA32481.1; -; Genomic_DNA.
DR PIR; JF0028; YVBPT4.
DR RefSeq; NP_049865.1; NC_000866.4.
DR PDB; 6PSK; X-ray; 2.20 A; T=77-218.
DR PDB; 6PX4; X-ray; 1.65 A; B/T=77-218.
DR PDB; 6PXE; X-ray; 2.30 A; B/D/F/T=55-218.
DR PDBsum; 6PSK; -.
DR PDBsum; 6PX4; -.
DR PDBsum; 6PXE; -.
DR SMR; P06808; -.
DR TCDB; 1.E.8.1.1; the t4 holin (t4 holin) family.
DR GeneID; 1258610; -.
DR KEGG; vg:1258610; -.
DR Proteomes; UP000009087; Genome.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0034291; F:canonical holin activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR HAMAP; MF_04104; HOLIN_T4; 1.
DR InterPro; IPR020982; Phage_T4_GpT_holin.
DR Pfam; PF11031; Phage_holin_T; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytolysis; Disulfide bond; Host cell inner membrane;
KW Host cell lysis by virus; Host cell membrane; Host membrane; Membrane;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix;
KW Viral release from host cell.
FT CHAIN 1..218
FT /note="Holin"
FT /id="PRO_0000165066"
FT TOPO_DOM 1..34
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04104,
FT ECO:0000305|PubMed:11255004"
FT TRANSMEM 35..49
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04104,
FT ECO:0000305|PubMed:11255004"
FT TOPO_DOM 50..218
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04104,
FT ECO:0000305|PubMed:11255004"
FT DISULFID 175..207
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04104,
FT ECO:0000269|PubMed:22389108"
FT MUTAGEN 175
FT /note="C->S: Complete loss of lysis."
FT /evidence="ECO:0000269|PubMed:22389108"
FT MUTAGEN 207
FT /note="C->S: Complete loss of lysis."
FT /evidence="ECO:0000269|PubMed:22389108"
FT HELIX 67..71
FT /evidence="ECO:0007829|PDB:6PXE"
FT HELIX 78..93
FT /evidence="ECO:0007829|PDB:6PX4"
FT STRAND 96..105
FT /evidence="ECO:0007829|PDB:6PX4"
FT TURN 106..108
FT /evidence="ECO:0007829|PDB:6PX4"
FT STRAND 111..119
FT /evidence="ECO:0007829|PDB:6PX4"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:6PXE"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:6PX4"
FT STRAND 131..134
FT /evidence="ECO:0007829|PDB:6PXE"
FT HELIX 140..146
FT /evidence="ECO:0007829|PDB:6PX4"
FT STRAND 151..155
FT /evidence="ECO:0007829|PDB:6PX4"
FT STRAND 158..161
FT /evidence="ECO:0007829|PDB:6PX4"
FT STRAND 171..178
FT /evidence="ECO:0007829|PDB:6PX4"
FT STRAND 182..195
FT /evidence="ECO:0007829|PDB:6PX4"
FT HELIX 200..214
FT /evidence="ECO:0007829|PDB:6PX4"
SQ SEQUENCE 218 AA; 25176 MW; 9110BE111D772DF5 CRC64;
MAAPRISFSP SDILFGVLDR LFKDNATGKV LASRVAVVIL LFIMAIVWYR GDSFFEYYKQ
SKYETYSEII EKERTARFES VALEQLQIVH ISSEADFSAV YSFRPKNLNY FVDIIAYEGK
LPSTISEKSL GGYPVDKTMD EYTVHLNGRH YYSNSKFAFL PTKKPTPEIN YMYSCPYFNL
DNIYAGTITM YWYRNDHISN DRLESICAQA ARILGRAK
