ANTIH_BPT4
ID ANTIH_BPT4 Reviewed; 97 AA.
AC P13304;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 23-FEB-2022, entry version 83.
DE RecName: Full=Antiholin {ECO:0000255|HAMAP-Rule:MF_04105};
DE AltName: Full=Protein rI;
GN Name=rI; Synonyms=58.6, rIA, tk.-2;
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=3024113; DOI=10.1093/nar/14.21.8637;
RA Valerie K., Stevens J., Lynch M., Henderson E.E., de Riel J.K.;
RT "Nucleotide sequence and analysis of the 58.3 to 65.5-kb early region of
RT bacteriophage T4.";
RL Nucleic Acids Res. 14:8637-8654(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Mzhavia N., Marusich E., Djavakhishvili T., Neitzel J., Peterson S.,
RA Awaya M., Eidermiller J., Canada D., Tracy J., Gailbreath K., Paddison P.,
RA Anderson B., Stidham T., Blattner F., Kutter E.M.;
RT "The 10.7 kb 'nonessential' region of bacteriophage T4 between the genes tk
RT and nrdC: twenty new t4 genes, generally conserved among T-even phages.";
RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP FUNCTION.
RX PubMed=9560373; DOI=10.1093/genetics/148.4.1539;
RA Paddison P., Abedon S.T., Dressman H.K., Gailbreath K., Tracy J.,
RA Mosser E., Neitzel J., Guttman B., Kutter E.;
RT "The roles of the bacteriophage T4 r genes in lysis inhibition and fine-
RT structure genetics: a new perspective.";
RL Genetics 148:1539-1550(1998).
RN [5]
RP INTERACTION WITH HOLIN, TOPOLOGY, 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 [6]
RP FUNCTION.
RX PubMed=17693511; DOI=10.1128/jb.00854-07;
RA Tran T.A., Struck D.K., Young R.;
RT "The T4 RI antiholin has an N-terminal signal anchor release domain that
RT targets it for degradation by DegP.";
RL J. Bacteriol. 189:7618-7625(2007).
RN [7]
RP FUNCTION, MUTAGENESIS OF CYS-69 AND CYS-75, DISULFIDE BOND, TOPOLOGY, AND
RP DOMAIN.
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).
CC -!- FUNCTION: Involved in lysis inhibition. Interacts with and inhibits the
CC holin thereby delaying the host cell lysis timing. Lysis inhibition is
CC imposed when a cell infected by a T4-like virus is superinfected by new
CC incoming viruses. This is probably due to the capsid content of the new
CC phage being released in the periplasm because of blockage of entry due
CC to superinfection exclusion. These periplasmically released viral
CC proteins must somehow activate the periplasmic antiholin, which in turn
CC will block the holin multimerization. {ECO:0000255|HAMAP-Rule:MF_04105,
CC ECO:0000269|PubMed:17693511, ECO:0000269|PubMed:22389108,
CC ECO:0000269|PubMed:9560373}.
CC -!- SUBUNIT: Interacts (via C-terminus) with holin (via C-terminus); this
CC interaction blocks the holin homomultimerization and delays the host
CC cell lysis. {ECO:0000255|HAMAP-Rule:MF_04105,
CC ECO:0000269|PubMed:16166524}.
CC -!- SUBCELLULAR LOCATION: Host cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_04105, ECO:0000305|PubMed:16166524}; Single-pass type II
CC membrane protein {ECO:0000255|HAMAP-Rule:MF_04105,
CC ECO:0000305|PubMed:16166524}.
CC -!- DOMAIN: The transmembrane signal-anchor domain can escape spontaneously
CC from the cell inner membrane. It is called SAR for signal-anchor-
CC release for that reason and explains why the antiholin is an extremely
CC instable protein. Superinfection might stabilize it so that it can
CC inhibit holin multimerization and delay lysis. {ECO:0000255|HAMAP-
CC Rule:MF_04105, ECO:0000269|PubMed:22389108}.
CC -!- PTM: Disulfide bond is required for functionality. {ECO:0000255|HAMAP-
CC Rule:MF_04105, ECO:0000269|PubMed:22389108}.
CC -!- SIMILARITY: Belongs to the T4likevirus antiholin family.
CC {ECO:0000255|HAMAP-Rule:MF_04105}.
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; X04567; CAA28236.1; -; Genomic_DNA.
DR EMBL; U76612; AAB26962.1; -; Genomic_DNA.
DR EMBL; AF158101; AAD42646.1; -; Genomic_DNA.
DR RefSeq; NP_049717.1; NC_000866.4.
DR PDB; 6PSH; X-ray; 2.21 A; A=25-97.
DR PDB; 6PSK; X-ray; 2.20 A; R=25-97.
DR PDB; 6PX4; X-ray; 1.65 A; A/R=25-97.
DR PDB; 6PXE; X-ray; 2.30 A; A/C/E/R=25-97.
DR PDBsum; 6PSH; -.
DR PDBsum; 6PSK; -.
DR PDBsum; 6PX4; -.
DR PDBsum; 6PXE; -.
DR SMR; P13304; -.
DR GeneID; 1258591; -.
DR KEGG; vg:1258591; -.
DR Proteomes; UP000009087; Genome.
DR GO; GO:0020002; C:host cell plasma membrane; IDA:CACAO.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:1901218; P:negative regulation of holin activity; IMP:CACAO.
DR HAMAP; MF_04105; ANTIH_T4; 1.
DR InterPro; IPR034696; RI_T4.
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..97
FT /note="Antiholin"
FT /id="PRO_0000003346"
FT TRANSMEM 1..24
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04105,
FT ECO:0000305|PubMed:16166524"
FT TOPO_DOM 25..97
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04105,
FT ECO:0000305|PubMed:16166524, ECO:0000305|PubMed:22389108"
FT DISULFID 69..75
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04105,
FT ECO:0000305|PubMed:22389108"
FT MUTAGEN 69
FT /note="C->S: Complete loss of lysis."
FT /evidence="ECO:0000269|PubMed:22389108"
FT MUTAGEN 75
FT /note="C->S: Complete loss of lysis."
FT /evidence="ECO:0000269|PubMed:22389108"
FT HELIX 28..40
FT /evidence="ECO:0007829|PDB:6PX4"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:6PX4"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:6PX4"
FT HELIX 50..66
FT /evidence="ECO:0007829|PDB:6PX4"
FT HELIX 72..89
FT /evidence="ECO:0007829|PDB:6PX4"
SQ SEQUENCE 97 AA; 11125 MW; EA0EBE97B91265D8 CRC64;
MALKATALFA MLGLSFVLSP SIEANVDPHF DKFMESGIRH VYMLFENKSV ESSEQFYSFM
RTTYKNDPCS SDFECIERGA EMAQSYARIM NIKLETE
