ID   TERM_BPM2               Reviewed;          15 AA.
AC   P19897;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   29-SEP-2021, entry version 54.
DE   RecName: Full=DNA terminal protein;
DE   AltName: Full=Protein GP3;
DE   Flags: Fragment;
GN   Name=3; Synonyms=E;
OS   Bacillus phage M2 (Bacteriophage M2).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Salasmaviridae; Picovirinae; Salasvirus;
OC   unclassified Salasvirus.
OX   NCBI_TaxID=331976;
OH   NCBI_TaxID=1386; Bacillus.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2515115; DOI=10.1016/0378-1119(89)90498-8;
RA   Matsumoto K., Takano H., Kim C.I., Hirokawa H.;
RT   "Primary structure of bacteriophage M2 DNA polymerase: conserved segments
RT   within protein-priming DNA polymerases and DNA polymerase I of Escherichia
RT   coli.";
RL   Gene 84:247-255(1989).
RN   [2]
RP   FUNCTION.
RX   PubMed=14763988; DOI=10.1046/j.1365-2958.2003.03894.x;
RA   Moak M., Molineux I.J.;
RT   "Peptidoglycan hydrolytic activities associated with bacteriophage
RT   virions.";
RL   Mol. Microbiol. 51:1169-1183(2004).
CC   -!- FUNCTION: Acts as a primer for viral genomic replication. DNA terminal
CC       protein is covalently linked to the 5'-ends of both strands of the
CC       genome through a phosphodiester bond between the beta-hydroxyl group of
CC       a serine residue and the 5'-phosphate of the terminal deoxyadenylate.
CC       This protein is essential for DNA replication and is involved in the
CC       priming of DNA elongation (By similarity). {ECO:0000250}.
CC   -!- FUNCTION: Hydrolyzes host peptidoglycans during virus entry.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer with viral polymerase. Binds to ssDNA (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the phi29likevirus DNA terminal protein family.
CC       {ECO:0000305}.
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DR   EMBL; M33144; AAA32367.1; -; Genomic_DNA.
DR   PIR; PQ0017; PQ0017.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0098932; P:disruption by virus of host cell wall peptidoglycan during virus entry; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0039693; P:viral DNA genome replication; IEA:UniProtKB-KW.
PE   3: Inferred from homology;
KW   Covalent protein-DNA linkage;
KW   Degradation of host cell envelope components during virus entry;
KW   Degradation of host peptidoglycans during virus entry; DNA replication;
KW   Early protein; Hydrolase; Phosphoprotein; Viral DNA replication; Virion;
KW   Virus entry into host cell.
FT   CHAIN           <1..15
FT                   /note="DNA terminal protein"
FT                   /id="PRO_0000106554"
FT   NON_TER         1
SQ   SEQUENCE   15 AA;  1797 MW;  D3CBAFF8759DEA06 CRC64;
     DRYERGDVNL DLKGF