ID   APNUC_BPT5              Reviewed;         114 AA.
AC   Q6QGS2;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=DNA-(apurinic or apyrimidinic site) endonuclease {ECO:0000255|HAMAP-Rule:MF_04167};
DE            EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_04167, ECO:0000269|PubMed:34074772};
DE   AltName: Full=AP endonuclease {ECO:0000255|HAMAP-Rule:MF_04167};
DE   AltName: Full=Apurinic-apyrimidinic endonuclease {ECO:0000255|HAMAP-Rule:MF_04167};
DE   AltName: Full=Protein 015 {ECO:0000303|PubMed:34074772};
GN   ORFNames=T5.015 {ECO:0000312|EMBL:AAS77062.1};
OS   Escherichia phage T5 (Enterobacteria phage T5).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Demerecviridae; Markadamsvirinae; Tequintavirus.
OX   NCBI_TaxID=2695836;
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Ksenzenko V.N., Kaliman A.V., Krutilina A.I., Shlyapnikov M.G.;
RT   "Bacteriophage T5 complete genome.";
RL   Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH HOST UNG.
RX   PubMed=34074772; DOI=10.1073/pnas.2026354118;
RA   Mahata T., Molshanski-Mor S., Goren M.G., Jana B., Kohen-Manor M.,
RA   Yosef I., Avram O., Pupko T., Salomon D., Qimron U.;
RT   "A phage mechanism for selective nicking of dUMP-containing DNA.";
RL   Proc. Natl. Acad. Sci. U.S.A. 118:0-0(2021).
CC   -!- FUNCTION: Performs endonucleolytic cleavage at abasic sites, which are
CC       generated by the base-excision activity of host Ung (PubMed:34074772).
CC       The cleavage generates a 5'-deoxyribose phosphate and 3'-hydroxyl end
CC       (PubMed:34074772). The sites are specifically recognized through the
CC       formation of a complex with host Ung (PubMed:34074772). The viral
CC       endonucleolytic activity damages the host DNA, blocks host DNA
CC       replication and induces cell division arrest (PubMed:34074772). This
CC       may provide an advantage for the phage and save nucleotides for the
CC       viral replication since it specifically targets the host DNA, which
CC       possesses more misincorporated uracils than the viral genome
CC       (Probable). {ECO:0000255|HAMAP-Rule:MF_04167,
CC       ECO:0000269|PubMed:34074772, ECO:0000305|PubMed:34074772}.
CC   -!- SUBUNIT: Interacts with host Ung; this interaction allows the viral AP
CC       endonuclease to localize to newly formed AP sites and cleave them,
CC       leading to inhibition of bacterial growth. {ECO:0000255|HAMAP-
CC       Rule:MF_04167, ECO:0000269|PubMed:34074772}.
CC   -!- SIMILARITY: Belongs to the apurinic/apyrimidinic endonuclease family.
CC       {ECO:0000255|HAMAP-Rule:MF_04167}.
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DR   EMBL; AY543070; AAS77062.1; -; Genomic_DNA.
DR   RefSeq; YP_006843.1; NC_005859.1.
DR   GeneID; 2777549; -.
DR   KEGG; vg:2777549; -.
DR   Proteomes; UP000002107; Genome.
DR   GO; GO:0004519; F:endonuclease activity; 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   HAMAP; MF_04167; APNUC_T5; 1.
PE   1: Evidence at protein level;
KW   Bacterial host gene expression shutoff by virus;
KW   Degradation of host chromosome by virus; Endonuclease;
KW   Host gene expression shutoff by virus; Host-virus interaction; Hydrolase;
KW   Nuclease; Reference proteome.
FT   CHAIN           1..114
FT                   /note="DNA-(apurinic or apyrimidinic site) endonuclease"
FT                   /id="PRO_0000454039"
SQ   SEQUENCE   114 AA;  12965 MW;  DE81BDDA5909ECD7 CRC64;
     MVIYEGNRFV AICRPGLLAN YLNQVSPEYK GVINIYEGKA HYKINAVVAR ELAFQFLTFA
     SCDIQVMGEA LIAENEDDFI NIFRKVYTER LIMKGAYIQS TAESIETAFR KVAQ