ID   P56_BPPH2               Reviewed;          56 AA.
AC   Q38503;
DT   11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   29-SEP-2021, entry version 64.
DE   RecName: Full=Protein p56 {ECO:0000303|PubMed:17698500};
GN   Name=0.8 {ECO:0000312|EMBL:ACE96021.1};
OS   Bacillus phage phi29 (Bacteriophage phi-29).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Salasmaviridae; Picovirinae; Salasvirus.
OX   NCBI_TaxID=10756 {ECO:0000312|EMBL:CAA24477.1};
OH   NCBI_TaxID=1423; Bacillus subtilis.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6809534; DOI=10.1016/0378-1119(82)90149-4;
RA   Yoshikawa H., Ito J.;
RT   "Nucleotide sequence of the major early region of bacteriophage phi 29.";
RL   Gene 17:323-335(1982).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Villegas A.P., Lingohr E.J., Ceyssens P.-J., Kropinski A.M.;
RL   Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION, SUBUNIT, AND INTERACTION WITH BACILLUS SUBTILIS URACIL-DNA
RP   GLYCOSYLASE.
RX   PubMed=17698500; DOI=10.1093/nar/gkm584;
RA   Serrano-Heras G., Ruiz-Maso J.A., del Solar G., Espinosa M., Bravo A.,
RA   Salas M.;
RT   "Protein p56 from the Bacillus subtilis phage phi29 inhibits DNA-binding
RT   ability of uracil-DNA glycosylase.";
RL   Nucleic Acids Res. 35:5393-5401(2007).
RN   [4]
RP   FUNCTION.
RX   PubMed=18845683; DOI=10.1073/pnas.0808797105;
RA   Serrano-Heras G., Bravo A., Salas M.;
RT   "Phage phi29 protein p56 prevents viral DNA replication impairment caused
RT   by uracil excision activity of uracil-DNA glycosylase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:19044-19049(2008).
RN   [5]
RP   FUNCTION.
RX   PubMed=21542855; DOI=10.1111/j.1365-2958.2011.07675.x;
RA   Perez-Lago L., Serrano-Heras G., Banos B., Lazaro J.M., Alcorlo M.,
RA   Villar L., Salas M.;
RT   "Characterization of Bacillus subtilis uracil-DNA glycosylase and its
RT   inhibition by phage phi29 protein p56.";
RL   Mol. Microbiol. 80:1657-1666(2011).
RN   [6] {ECO:0007744|PDB:2LE2}
RP   STRUCTURE BY NMR, AND SUBUNIT.
RX   PubMed=21890898; DOI=10.1093/nar/gkr667;
RA   Asensio J.L., Perez-Lago L., Lazaro J.M., Gonzalez C., Serrano-Heras G.,
RA   Salas M.;
RT   "Novel dimeric structure of phage phi29-encoded protein p56: insights into
RT   uracil-DNA glycosylase inhibition.";
RL   Nucleic Acids Res. 39:9779-9788(2011).
RN   [7] {ECO:0007744|PDB:3ZOQ}
RP   X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS).
RX   PubMed=23671337; DOI=10.1093/nar/gkt395;
RA   Banos-Sanz J.I., Mojardin L., Sanz-Aparicio J., Lazaro J.M., Villar L.,
RA   Serrano-Heras G., Gonzalez B., Salas M.;
RT   "Crystal structure and functional insights into uracil-DNA glycosylase
RT   inhibition by phage 29 DNA mimic protein p56.";
RL   Nucleic Acids Res. 41:6761-6773(2013).
CC   -!- FUNCTION: Inhibits the host uracil-DNA glycosylase (UDG), an enzyme
CC       which removes uracil residues from DNA by the base excision repair.
CC       Interacts with host uracil-DNA glycosylase and prevents the latter from
CC       binding to DNA. Since the viral DNA polymerase efficiently incorporates
CC       dUMP into DNA, the virus needs to prevent the deleterious effect caused
CC       by host UDG when it eliminates uracil residues present in the viral
CC       genome. {ECO:0000269|PubMed:17698500, ECO:0000269|PubMed:18845683,
CC       ECO:0000269|PubMed:21542855}.
CC   -!- SUBUNIT: Homodimer (PubMed:17698500, PubMed:21890898). Interacts with
CC       host UDG; this interaction inhibits the uracil-DNA glycosylase
CC       (PubMed:17698500). {ECO:0000269|PubMed:17698500,
CC       ECO:0000269|PubMed:21890898}.
CC   -!- SIMILARITY: Belongs to the phi29likevirus protein p56 family.
CC       {ECO:0000305}.
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DR   EMBL; EU771092; ACE96021.1; -; Genomic_DNA.
DR   EMBL; V01155; CAA24477.1; -; Genomic_DNA.
DR   RefSeq; YP_002004527.1; NC_011048.1.
DR   PDB; 2LE2; NMR; -; A/B=1-56.
DR   PDB; 3ZOQ; X-ray; 1.45 A; B/C=1-56.
DR   PDBsum; 2LE2; -.
DR   PDBsum; 3ZOQ; -.
DR   SMR; Q38503; -.
DR   GeneID; 6446503; -.
DR   KEGG; vg:6446503; -.
DR   EvolutionaryTrace; Q38503; -.
DR   Proteomes; UP000001207; Genome.
DR   GO; GO:0051701; P:biological process involved in interaction with host; IPI:UniProtKB.
PE   1: Evidence at protein level;
KW   3D-structure; Early protein; Host-virus interaction; Reference proteome.
FT   CHAIN           1..56
FT                   /note="Protein p56"
FT                   /id="PRO_0000436073"
FT   STRAND          4..6
FT                   /evidence="ECO:0007829|PDB:2LE2"
FT   STRAND          10..17
FT                   /evidence="ECO:0007829|PDB:3ZOQ"
FT   STRAND          23..31
FT                   /evidence="ECO:0007829|PDB:3ZOQ"
FT   HELIX           33..41
FT                   /evidence="ECO:0007829|PDB:3ZOQ"
FT   STRAND          45..54
FT                   /evidence="ECO:0007829|PDB:3ZOQ"
SQ   SEQUENCE   56 AA;  6565 MW;  39EA59B62BE8D950 CRC64;
     MVQNDFVDSY DVTMLLQDDD GKQYYEYHKG LSLSDFEVLY GNTADEIIKL RLDKVL