NP_BPPZA
ID NP_BPPZA Reviewed; 96 AA.
AC P06955;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 23-FEB-2022, entry version 62.
DE RecName: Full=Histone-like protein p6 {ECO:0000250|UniProtKB:P03685};
DE AltName: Full=Double-stranded DNA-binding protein {ECO:0000250|UniProtKB:P03685};
DE AltName: Full=Double-stranded DNA-binding protein p6 {ECO:0000250|UniProtKB:P03685};
DE AltName: Full=Gene product 6 {ECO:0000250|UniProtKB:P03685};
DE Short=gp6 {ECO:0000250|UniProtKB:P03685};
DE AltName: Full=Histone-like binding protein {ECO:0000250|UniProtKB:P03685};
DE AltName: Full=Nucleoid-associated protein p6 {ECO:0000250|UniProtKB:P03685};
DE AltName: Full=Protein p6 {ECO:0000250|UniProtKB:P03685};
GN Name=6;
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: Histone-like nucleoprotein that binds to the viral dsDNA and
CC responsible for wrapping and compacting 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. Binds ito most, if
CC not all, the viral genome, although with different affinity, the
CC highest one corresponding to the genome ends. The formation of the
CC nucleoprotein complex at the genome ends, activates the initiation of
CC viral DNA replication. The binding of p6 would recruit the complex
CC formed by the TP and the DNA polymerase to the origin. Protein p6 also
CC represses early transcription from promoter C2, and, together with
CC protein p4, represses transcription from promoters A2b and A2c and
CC activates late transcription from promoter A3. Protein p6 is therefore
CC involved in the early to late transcription switch. The formation of
CC the nucleoprotein complex at the right end of the phage genome where
CC the early promoter C2 is located affects local topology, which may
CC contribute to the promoter repression. {ECO:0000250|UniProtKB:P03685}.
CC -!- SUBUNIT: Homodimer. Homomultimer. Binds to double-stranded DNA giving
CC rise to multimeric nucleoprotein complexes. Binding specificity for the
CC viral DNA is based on supercoiling, the viral genome having a negative
CC superhelicity lower than that of plasmid DNA. Interacts with the DNA
CC replication protein p17; this interaction optimizes the binding of
CC protein p6 at the viral DNA ends, thus favoring the initiation of
CC replication. {ECO:0000250|UniProtKB:P03685}.
CC -!- DOMAIN: The N-terminus is involved in DNA-binding.
CC {ECO:0000250|UniProtKB:P03685}.
CC -!- SIMILARITY: Belongs to the phi29likevirus histone-like protein p6
CC family. {ECO:0000305}.
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DR EMBL; M11813; AAA88473.1; -; Genomic_DNA.
DR PIR; I24528; ERBP6Z.
DR PRIDE; P06955; -.
DR Proteomes; UP000000855; 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; Repressor;
KW Transcription; Transcription regulation; Viral DNA replication.
FT CHAIN 1..96
FT /note="Histone-like protein p6"
FT /id="PRO_0000106569"
FT DNA_BIND 1..19
FT /evidence="ECO:0000250|UniProtKB:P03685"
SQ SEQUENCE 96 AA; 11050 MW; 49DF291A99EF4F8E CRC64;
MAKMMQREIT KTTVNVAKMV MVDGEVQVEQ LPSETFVGNL SMEQAQWRMK RKYKGEPVQV
VSVEPNTEVY ELPVEKFLEV ATVRVEKEDS EEQVAE