ID   TERM_BPPZA              Reviewed;         266 AA.
AC   P06951;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   23-FEB-2022, entry version 74.
DE   RecName: Full=DNA terminal protein;
DE   AltName: Full=Gene product 3;
DE            Short=gp3;
DE   AltName: Full=Protein p3;
GN   Name=3;
OS   Bacillus phage PZA (Bacteriophage PZA).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Salasmaviridae; Picovirinae; Salasvirus; Bacillus virus PZA.
OX   NCBI_TaxID=10757;
OH   NCBI_TaxID=1423; Bacillus subtilis.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3934048; DOI=10.1016/0378-1119(85)90202-1;
RA   Paces V., Vlcek C., Urbanek P., Hostomsky Z.;
RT   "Nucleotide sequence of the major early region of Bacillus subtilis phage
RT   PZA, a close relative of phi 29.";
RL   Gene 38:45-56(1985).
CC   -!- FUNCTION: Acts as a primer for DNA elongation during viral genomic
CC       replication. Acts as the small terminase protein during packaging.
CC       Recruits the phage DNA polymerase to the bacterial nucleoid. Primer
CC       terminal protein (TP) is covalently linked to the 5'-ends of both
CC       strands of the genome through a phosphodiester bond between the beta-
CC       hydroxyl group of a serine residue and the 5'-phosphate of the terminal
CC       deoxyadenylate (dAMP). To start replication, the DNA polymerase forms a
CC       heterodimer with a free TP that recognizes the replication origins at
CC       both 5' ends of the linear chromosome, and initiates replication using
CC       as primer the OH-group of Ser-232 of the TP. Since the polymerase
CC       initiates the replication on the second thymine, the TP-dAMP initiation
CC       product slides backwards to recover the template information of the
CC       first nucleotide. {ECO:0000250|UniProtKB:P03681}.
CC   -!- FUNCTION: Hydrolyzes host peptidoglycans during virus entry.
CC       {ECO:0000250|UniProtKB:P03681}.
CC   -!- SUBUNIT: Interacts with the viral polymerase; this interaction allows
CC       the initiation of TP-primed DNA replication at both viral DNA ends.
CC       Binds to ssDNA. Interacts with the replication protein p1. Part of a
CC       DNA-gp3-gp16 complex. {ECO:0000250|UniProtKB:P03681}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P03681}.
CC       Note=Associates with the host bacterial nucleoid through its N-terminal
CC       region. {ECO:0000250|UniProtKB:P03681}.
CC   -!- SIMILARITY: Belongs to the phi29likevirus DNA terminal protein family.
CC       {ECO:0000305}.
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DR   EMBL; M11813; AAA88477.1; -; Genomic_DNA.
DR   PIR; E24528; ERBP3Z.
DR   SMR; P06951; -.
DR   Proteomes; UP000000855; Genome.
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:0006269; P:DNA replication, synthesis of RNA primer; IEA:InterPro.
DR   GO; GO:0018142; P:protein-DNA covalent cross-linking; IEA:InterPro.
DR   GO; GO:0039693; P:viral DNA genome replication; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.1270.230; -; 1.
DR   InterPro; IPR008770; DNA_terminal_Gp3.
DR   InterPro; IPR043124; DNA_terminal_Gp3_C.
DR   InterPro; IPR037216; DNA_terminal_Gp3_sf.
DR   Pfam; PF05435; Phi-29_GP3; 1.
DR   PIRSF; PIRSF004179; Phi-29_GP3; 1.
DR   SUPFAM; SSF140919; SSF140919; 1.
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..266
FT                   /note="DNA terminal protein"
FT                   /id="PRO_0000106557"
FT   REGION          1..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000250|UniProtKB:P03681"
FT   REGION          74..172
FT                   /note="Intermediate; makes extensive contacts with the
FT                   phage DNA polymerase"
FT                   /evidence="ECO:0000250|UniProtKB:P03681"
FT   REGION          173..266
FT                   /note="Priming"
FT                   /evidence="ECO:0000250|UniProtKB:P03681"
FT   REGION          256..258
FT                   /note="Interaction with the viral DNA polymerase"
FT                   /evidence="ECO:0000250|UniProtKB:P03681"
FT   SITE            230
FT                   /note="Positions the 3' end of the template strand at the
FT                   active site of the DNA polymerase"
FT                   /evidence="ECO:0000250|UniProtKB:P03681"
FT   MOD_RES         232
FT                   /note="O-(5'-phospho-DNA)-serine"
FT                   /evidence="ECO:0000250|UniProtKB:P03681"
SQ   SEQUENCE   266 AA;  31067 MW;  C8130B2A717522BF CRC64;
     MARSPRIRIK DNDKAEYARL VKNTKAKIAR TKKKYGVDLS AEINIPDLES FETRAQFNKW
     KEQASSFTNR ANMRYQFEKN AYGVVASKAK IAEIERNTKE VQRLVDEKIN AMKDKEYYAG
     GKPQGTIEQR IAMTSPAHVT GINRPRDFDF SKVRTYSRLR TLEESMEMRT DPQYYEKKMI
     QLQLNFIKSV EGSFNSFDAA DELIEELKKI PPDDFYELFL RISEISFEEF DSEGNTVENV
     EGNVYKILSY LEQYRRGDFD LSLKGF