END2_BPT4
ID END2_BPT4 Reviewed; 136 AA.
AC P07059;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 03-SEP-2014, sequence version 3.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Endonuclease II;
DE EC=3.1.21.8 {ECO:0000269|PubMed:18539732, ECO:0000269|PubMed:19666720, ECO:0000269|PubMed:6887350, ECO:0000269|PubMed:8386173};
GN Name=denA;
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=3530746; DOI=10.1002/j.1460-2075.1986.tb04460.x;
RA Sjoeberg B.-M., Hahne S., Mathews C.Z., Mathews C.K., Rand K.N., Gait M.J.;
RT "The bacteriophage T4 gene for the small subunit of ribonucleotide
RT reductase contains an intron.";
RL EMBO J. 5:2031-2036(1986).
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 FUNCTION IN HOST DNA DEGRADATION, AND CATALYTIC ACTIVITY.
RX PubMed=6887350; DOI=10.1128/jvi.48.1.18-30.1983;
RA Carlson K., Wiberg J.S.;
RT "In vivo cleavage of cytosine-containing bacteriophage T4 DNA to
RT genetically distinct, discretely sized fragments.";
RL J. Virol. 48:18-30(1983).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=8386173; DOI=10.1016/s0021-9258(18)52959-8;
RA Carlson K., Krabbe M., Nystroem A.C., Kosturko L.D.;
RT "DNA determinants of restriction. Bacteriophage T4 endonuclease II-
RT dependent cleavage of plasmid DNA in vivo.";
RL J. Biol. Chem. 268:8908-8918(1993).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND MUTAGENESIS OF GLY-49; ARG-57;
RP LEU-84 AND GLU-118.
RX PubMed=18539732; DOI=10.1128/jb.00094-08;
RA Lagerbaeck P., Carlson K.;
RT "Amino acid residues in the GIY-YIG endonuclease II of phage T4 affecting
RT sequence recognition and binding as well as catalysis.";
RL J. Bacteriol. 190:5533-5544(2008).
RN [6]
RP SUBUNIT, CATALYTIC ACTIVITY, FUNCTION, AND DNA-BINDING.
RX PubMed=19666720; DOI=10.1093/nar/gkp652;
RA Lagerback P., Andersson E., Malmberg C., Carlson K.;
RT "Bacteriophage T4 endonuclease II, a promiscuous GIY-YIG nuclease, binds as
RT a tetramer to two DNA substrates.";
RL Nucleic Acids Res. 37:6174-6183(2009).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), AND SUBUNIT.
RX PubMed=20156453; DOI=10.1016/j.jmb.2010.01.076;
RA Andersson C.E., Lagerback P., Carlson K.;
RT "Structure of bacteriophage T4 endonuclease II mutant E118A, a tetrameric
RT GIY-YIG enzyme.";
RL J. Mol. Biol. 397:1003-1016(2010).
CC -!- FUNCTION: Contributes to the degradation of host DNA, permitting the
CC scavenging of host-derived nucleotides for phage DNA synthesis
CC (PubMed:19666720, PubMed:18539732). Sequence-specific endonuclease.
CC Catalyzes nicking of the bottom strand of double-stranded DNA between
CC the first and second base pair to the right of a top-strand CCGC motif.
CC Does not cleave native phage DNA, which contains 5-
CC hydroxymethylcytosine instead of cytosine.
CC {ECO:0000269|PubMed:18539732, ECO:0000269|PubMed:6887350,
CC ECO:0000269|PubMed:8386173, ECO:0000303|PubMed:18539732,
CC ECO:0000303|PubMed:19666720}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic nicking and cleavage of cytosine-containing
CC double-stranded DNA.; EC=3.1.21.8;
CC Evidence={ECO:0000269|PubMed:18539732, ECO:0000269|PubMed:19666720,
CC ECO:0000269|PubMed:6887350, ECO:0000269|PubMed:8386173};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:18539732};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:19666720,
CC ECO:0000269|PubMed:20156453}.
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DR EMBL; X04140; CAA27759.1; -; Genomic_DNA.
DR EMBL; AF158101; AAD42558.1; -; Genomic_DNA.
DR PIR; S08603; ZNBPT4.
DR RefSeq; NP_049840.1; NC_000866.4.
DR PDB; 2WSH; X-ray; 1.90 A; A/B/C/D=1-136.
DR PDBsum; 2WSH; -.
DR SMR; P07059; -.
DR GeneID; 1258710; -.
DR KEGG; vg:1258710; -.
DR BRENDA; 3.1.21.8; 732.
DR EvolutionaryTrace; P07059; -.
DR Proteomes; UP000009087; Genome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0099015; P:degradation of host chromosome by virus; IEA:UniProtKB-KW.
DR GO; GO:0039657; P:suppression by virus of host gene expression; IEA:UniProtKB-KW.
DR CDD; cd10436; GIY-YIG_EndoII_Hpy188I_like; 1.
DR InterPro; IPR044556; EndoII-like_GIY-YIG.
DR InterPro; IPR000305; GIY-YIG_endonuc.
DR InterPro; IPR035901; GIY-YIG_endonuc_sf.
DR InterPro; IPR016413; Phage_T4_DenA_endoDNaseII.
DR Pfam; PF01541; GIY-YIG; 1.
DR PIRSF; PIRSF004362; Endonuclease_II_phage_DenA; 1.
DR SMART; SM00465; GIYc; 1.
DR SUPFAM; SSF82771; SSF82771; 1.
DR PROSITE; PS50164; GIY_YIG; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Bacterial host gene expression shutoff by virus;
KW Degradation of host chromosome by virus; DNA-binding; Endonuclease;
KW Host gene expression shutoff by virus; Host-virus interaction; Hydrolase;
KW Magnesium; Metal-binding; Nuclease; Reference proteome.
FT CHAIN 1..136
FT /note="Endonuclease II"
FT /id="PRO_0000164932"
FT DOMAIN 32..131
FT /note="GIY-YIG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00977"
FT MUTAGEN 49
FT /note="G->A: Nearly abolishes endonuclease activity."
FT /evidence="ECO:0000269|PubMed:18539732"
FT MUTAGEN 57
FT /note="R->A: Nearly abolishes endonuclease activity."
FT /evidence="ECO:0000269|PubMed:18539732"
FT MUTAGEN 84
FT /note="L->P: Nearly abolishes endonuclease activity."
FT /evidence="ECO:0000269|PubMed:18539732"
FT MUTAGEN 118
FT /note="E->A: Abolishes endonuclease activity."
FT /evidence="ECO:0000269|PubMed:18539732"
FT HELIX 1..7
FT /evidence="ECO:0007829|PDB:2WSH"
FT STRAND 11..16
FT /evidence="ECO:0007829|PDB:2WSH"
FT STRAND 34..41
FT /evidence="ECO:0007829|PDB:2WSH"
FT STRAND 44..52
FT /evidence="ECO:0007829|PDB:2WSH"
FT HELIX 54..66
FT /evidence="ECO:0007829|PDB:2WSH"
FT HELIX 75..85
FT /evidence="ECO:0007829|PDB:2WSH"
FT STRAND 90..96
FT /evidence="ECO:0007829|PDB:2WSH"
FT STRAND 99..104
FT /evidence="ECO:0007829|PDB:2WSH"
FT STRAND 107..112
FT /evidence="ECO:0007829|PDB:2WSH"
FT HELIX 114..125
FT /evidence="ECO:0007829|PDB:2WSH"
SQ SEQUENCE 136 AA; 15802 MW; 223499122C6EF8BB CRC64;
MKEIATEYSF IKYTELELDD NGSIKQLSIP NKYNVIYAIA INDELVYIGK TKNLRKRINY
YRTAINRKDK TSDSTKSALI HSALKEGSKV EFYARQCFNL SMTNELGTMT IATIDLEEPL
FIKLFNPPWN IQHKKK
