TERM_BPNF
ID TERM_BPNF Reviewed; 266 AA.
AC P06812;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 29-SEP-2021, entry version 68.
DE RecName: Full=DNA terminal protein;
DE AltName: Full=Gene product 3;
DE Short=gp3;
DE AltName: Full=Protein p3;
GN Name=3; Synonyms=E;
OS Bacillus phage Nf (Bacteriophage Nf).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Salasmaviridae; Picovirinae; Beecentumtrevirus.
OX NCBI_TaxID=10753;
OH NCBI_TaxID=1423; Bacillus subtilis.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3601672; DOI=10.1093/nar/15.13.5251;
RA Leavitt M.C., Ito J.;
RT "Nucleotide sequence of Bacillus phage Nf terminal protein gene.";
RL Nucleic Acids Res. 15:5251-5259(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-104.
RX PubMed=3015737; DOI=10.1016/0378-1119(86)90302-1;
RA Mizukami Y., Sekiya T., Hirokawa H.;
RT "Nucleotide sequence of gene F of Bacillus phage Nf.";
RL Gene 42:231-235(1986).
RN [3]
RP FUNCTION.
RX PubMed=19011105; DOI=10.1073/pnas.0809882105;
RA Longas E., Villar L., Lazaro J.M., de Vega M., Salas M.;
RT "Phage phi29 and Nf terminal protein-priming domain specifies the internal
RT template nucleotide to initiate DNA replication.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:18290-18295(2008).
RN [4]
RP SUBCELLULAR LOCATION, AND NUCLEAR LOCALIZATION SIGNAL.
RX PubMed=23091024; DOI=10.1073/pnas.1216635109;
RA Redrejo-Rodriguez M., Munoz-Espin D., Holguera I., Mencia M., Salas M.;
RT "Functional eukaryotic nuclear localization signals are widespread in
RT terminal proteins of bacteriophages.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:18482-18487(2012).
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}. Host
CC nucleus {ECO:0000269|PubMed:23091024}. Note=Associates with the host
CC bacterial nucleoid through its N-terminal region.
CC {ECO:0000250|UniProtKB:P03681}.
CC -!- SIMILARITY: Belongs to the phi29likevirus DNA terminal protein family.
CC {ECO:0000305}.
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DR EMBL; Y00363; CAA68440.1; -; Genomic_DNA.
DR EMBL; M13664; AAA32196.1; -; Genomic_DNA.
DR PIR; A27856; ERBPNP.
DR SMR; P06812; -.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
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; Host nucleus; Hydrolase; Phosphoprotein;
KW Viral DNA replication; Virion; Virus entry into host cell.
FT CHAIN 1..266
FT /note="DNA terminal protein"
FT /id="PRO_0000106555"
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 MOTIF 25..34
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:23091024"
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; 31211 MW; 35528C2BC19954C4 CRC64;
MARNSRIRIT NNDKALYAKL VKNTKAKISR TKKKYGIDLS NEIELPPLES FQTREEFNKW
KQKQESFTNR ANQNYQFVKN KYGIVASKAK INEIAKNTKE AQRIVDEQRE EIEDKPFISG
GKQQGTVGQR MQILSPSQVT GISRPSDFNF DDVRSYARLR TLEEGMAEKA SPDYYDRRMT
QMHQNFIEIV EKSFNSDWLS DELVERLKKI PPDDFFELYL MFDEISFEYF DSEGEDVEAS
EAMLNKIHSY LDRYERGDVN LDLKGF
