ID   ENDO_BPT7               Reviewed;         149 AA.
AC   P00641;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Endonuclease I;
DE            EC=3.1.21.2;
DE   AltName: Full=Gene product 3;
DE            Short=Gp3;
DE   AltName: Full=Junction-resolving enzyme gp3;
GN   OrderedLocusNames=3;
OS   Escherichia phage T7 (Bacteriophage T7).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Autographiviridae; Studiervirinae; Teseptimavirus.
OX   NCBI_TaxID=10760;
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=6864790; DOI=10.1016/s0022-2836(83)80282-4;
RA   Dunn J.J., Studier F.W.;
RT   "Complete nucleotide sequence of bacteriophage T7 DNA and the locations of
RT   T7 genetic elements.";
RL   J. Mol. Biol. 166:477-535(1983).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7310871; DOI=10.1016/0022-2836(81)90178-9;
RA   Dunn J.J., Studier F.W.;
RT   "Nucleotide sequence from the genetic left end of bacteriophage T7 DNA to
RT   the beginning of gene 4.";
RL   J. Mol. Biol. 148:303-330(1981).
RN   [3]
RP   FUNCTION.
RX   PubMed=3972821; DOI=10.1016/s0021-9258(18)89488-1;
RA   Panayotatos N., Fontaine A.;
RT   "An endonuclease specific for single-stranded DNA selectively damages the
RT   genomic DNA and induces the SOS response.";
RL   J. Biol. Chem. 260:3173-3177(1985).
RN   [4]
RP   SUBUNIT, AND FUNCTION.
RX   PubMed=9236119; DOI=10.1006/jmbi.1997.1128;
RA   Parkinson M.J., Lilley D.M.;
RT   "The junction-resolving enzyme T7 endonuclease I: quaternary structure and
RT   interaction with DNA.";
RL   J. Mol. Biol. 270:169-178(1997).
RN   [5]
RP   FUNCTION.
RX   PubMed=12628932; DOI=10.1093/emboj/cdg132;
RA   Declais A.C., Fogg J.M., Freeman A.D., Coste F., Hadden J.M.,
RA   Phillips S.E., Lilley D.M.;
RT   "The complex between a four-way DNA junction and T7 endonuclease I.";
RL   EMBO J. 22:1398-1409(2003).
RN   [6]
RP   FUNCTION.
RX   PubMed=23207296; DOI=10.1016/j.jmb.2012.11.029;
RA   Freeman A.D., Declais A.C., Lilley D.M.;
RT   "The importance of the N-terminus of T7 endonuclease I in the interaction
RT   with DNA junctions.";
RL   J. Mol. Biol. 425:395-410(2013).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 12-149.
RX   PubMed=11135673; DOI=10.1038/83067;
RA   Hadden J.M., Convery M.A., Declais A.C., Lilley D.M., Phillips S.E.;
RT   "Crystal structure of the Holliday junction resolving enzyme T7
RT   endonuclease I.";
RL   Nat. Struct. Biol. 8:62-67(2001).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 12-149.
RX   PubMed=12093751; DOI=10.1093/emboj/cdf337;
RA   Hadden J.M., Declais A.C., Phillips S.E., Lilley D.M.;
RT   "Metal ions bound at the active site of the junction-resolving enzyme T7
RT   endonuclease I.";
RL   EMBO J. 21:3505-3515(2002).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS).
RX   PubMed=17873858; DOI=10.1038/nature06158;
RA   Hadden J.M., Declais A.C., Carr S.B., Lilley D.M., Phillips S.E.;
RT   "The structural basis of Holliday junction resolution by T7 endonuclease
RT   I.";
RL   Nature 449:621-624(2007).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 18-145.
RX   PubMed=18552127; DOI=10.1110/ps.036368.108;
RA   Guo Z., Eisenberg D.;
RT   "The structure of a fibril-forming sequence, NNQQNY, in the context of a
RT   globular fold.";
RL   Protein Sci. 17:1617-1623(2008).
CC   -!- FUNCTION: Junction-resolving enzyme that selectively binds and cleaves
CC       four-way (Holliday) DNA junctions present after viral genomic
CC       replication. These intermediates are created during DNA repair,
CC       processing of stalled replication forks and homologous genetic
CC       recombination. Introduces two nicks on the two non-crossing strands, at
CC       5' sides of the junction. Participates also together with gp6 in the
CC       degradation of host chromosome to provide nucleotides for phage DNA
CC       synthesis. {ECO:0000269|PubMed:12628932, ECO:0000269|PubMed:23207296,
CC       ECO:0000269|PubMed:3972821, ECO:0000269|PubMed:9236119}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage to 5'-phosphooligonucleotide end-
CC         products.; EC=3.1.21.2;
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:9236119}.
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; V01127; CAA24345.1; -; Genomic_DNA.
DR   EMBL; V01146; CAA24402.1; -; Genomic_DNA.
DR   PIR; B94615; NEBP37.
DR   RefSeq; NP_041972.1; NC_001604.1.
DR   PDB; 1FZR; X-ray; 2.10 A; A/B/C/D=12-149.
DR   PDB; 1M0D; X-ray; 1.90 A; A/B/C/D=12-149.
DR   PDB; 1M0I; X-ray; 2.55 A; A/B/C/D=12-149.
DR   PDB; 2PFJ; X-ray; 3.10 A; A/B=1-149.
DR   PDB; 3CAE; X-ray; 3.00 A; A/B/C/D/E/F/G/H/I/J=18-145.
DR   PDBsum; 1FZR; -.
DR   PDBsum; 1M0D; -.
DR   PDBsum; 1M0I; -.
DR   PDBsum; 2PFJ; -.
DR   PDBsum; 3CAE; -.
DR   SMR; P00641; -.
DR   DIP; DIP-41668N; -.
DR   IntAct; P00641; 1.
DR   MINT; P00641; -.
DR   GeneID; 1261079; -.
DR   KEGG; vg:1261079; -.
DR   BRENDA; 3.1.21.10; 736.
DR   EvolutionaryTrace; P00641; -.
DR   Proteomes; UP000000840; Genome.
DR   GO; GO:0008821; F:crossover junction endodeoxyribonuclease activity; IDA:CACAO.
DR   GO; GO:0008833; F:deoxyribonuclease IV (phage-T4-induced) activity; IEA:UniProtKB-EC.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:1990238; F:double-stranded DNA endodeoxyribonuclease activity; IDA:CACAO.
DR   GO; GO:0099015; P:degradation of host chromosome by virus; IEA:UniProtKB-KW.
DR   GO; GO:0015074; P:DNA integration; IEA:InterPro.
DR   GO; GO:0039657; P:suppression by virus of host gene expression; IEA:UniProtKB-KW.
DR   InterPro; IPR008029; Phage_T7_Gp3_endoDNaseI.
DR   InterPro; IPR011335; Restrct_endonuc-II-like.
DR   Pfam; PF05367; Phage_endo_I; 1.
DR   SUPFAM; SSF52980; SSF52980; 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   Nuclease; Reference proteome.
FT   CHAIN           1..149
FT                   /note="Endonuclease I"
FT                   /id="PRO_0000106486"
FT   HELIX           18..29
FT                   /evidence="ECO:0007829|PDB:1M0D"
FT   STRAND          35..37
FT                   /evidence="ECO:0007829|PDB:1M0D"
FT   STRAND          39..45
FT                   /evidence="ECO:0007829|PDB:1M0D"
FT   STRAND          48..52
FT                   /evidence="ECO:0007829|PDB:1M0D"
FT   STRAND          55..57
FT                   /evidence="ECO:0007829|PDB:1M0D"
FT   STRAND          63..69
FT                   /evidence="ECO:0007829|PDB:1M0D"
FT   HELIX           72..84
FT                   /evidence="ECO:0007829|PDB:1M0D"
FT   STRAND          90..95
FT                   /evidence="ECO:0007829|PDB:1M0D"
FT   STRAND          99..102
FT                   /evidence="ECO:0007829|PDB:1M0D"
FT   HELIX           109..116
FT                   /evidence="ECO:0007829|PDB:1M0D"
FT   STRAND          120..124
FT                   /evidence="ECO:0007829|PDB:1M0D"
FT   HELIX           127..131
FT                   /evidence="ECO:0007829|PDB:1M0D"
FT   HELIX           139..141
FT                   /evidence="ECO:0007829|PDB:1M0D"
FT   STRAND          142..144
FT                   /evidence="ECO:0007829|PDB:1M0D"
SQ   SEQUENCE   149 AA;  17172 MW;  D092AA28E3743BC1 CRC64;
     MAGYGAKGIR KVGAFRSGLE DKVSKQLESK GIKFEYEEWK VPYVIPASNH TYTPDFLLPN
     GIFVETKGLW ESDDRKKHLL IREQHPELDI RIVFSSSRTK LYKGSPTSYG EFCEKHGIKF
     ADKLIPAEWI KEPKKEVPFD RLKRKGGKK