ID   NP_BPNF                 Reviewed;         100 AA.
AC   B7SSM6;
DT   11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   29-SEP-2021, entry version 23.
DE   RecName: Full=Double-stranded DNA-binding protein;
DE   AltName: Full=Gene product 6;
DE            Short=gp6;
DE   AltName: Full=Nucleoid-associated protein p6;
DE   AltName: Full=Protein p6;
GN   Name=6 {ECO:0000312|EMBL:ACH57073.1};
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=19207565; DOI=10.1111/j.1462-2920.2008.01845.x;
RA   Castilla-Llorente V., Salas M., Meijer W.J.;
RT   "Different responses to Spo0A-mediated suppression of the related Bacillus
RT   subtilis phages Nf and phi29.";
RL   Environ. Microbiol. 11:1137-1149(2009).
CC   -!- FUNCTION: Histone-like nucleoprotein that binds to the viral dsDNA and
CC       responsible for wrapping and condensing the viral DNA about 4-fold.
CC       Forms a nucleoprotein complex in which the DNA adopts a right-handed
CC       toroidal conformation winding around a protein core. Binding
CC       specificity for the viral genome is based on supercoiling. The
CC       formation of the nucleoprotein complex at the genome ends, for which
CC       the binding affinity is highest, activates the initiation of viral DNA
CC       replication. The binding of p6 would recruit the complex formed by the
CC       TP and the DNA polymerase to the origin. Protein p6 is also involved in
CC       the early to late transcription switch. {ECO:0000250|UniProtKB:P03685}.
CC   -!- SUBUNIT: Homodimer. Homomultimer. Binds to double-stranded DNA giving
CC       rise to multimeric nucleoprotein complexes.
CC       {ECO:0000250|UniProtKB:P03685}.
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DR   EMBL; EU622808; ACH57073.1; -; Genomic_DNA.
DR   Proteomes; UP000000744; Genome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0030261; P:chromosome condensation; 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.
DR   InterPro; IPR035188; Histone-like_p6.
DR   Pfam; PF17548; p6; 1.
PE   3: Inferred from homology;
KW   DNA condensation; DNA replication; DNA-binding; Early protein;
KW   Reference proteome; Repressor; Transcription; Transcription regulation;
KW   Viral DNA replication.
FT   CHAIN           1..100
FT                   /note="Double-stranded DNA-binding protein"
FT                   /id="PRO_0000436077"
FT   DNA_BIND        1..19
FT                   /evidence="ECO:0000250|UniProtKB:P03685"
SQ   SEQUENCE   100 AA;  11332 MW;  E48A421C11018636 CRC64;
     MRKMMQREVT YTTAQLARMK MVDGEVTAEV LEPVTLIGNL SVEQAQREIN KRSEFKENPA
     QVVGVEANTQ LYELPLDVFL EHATVKERPA TKEEVAEVQA