NP_BPPH2
ID NP_BPPH2 Reviewed; 104 AA.
AC P03685; B3VMP1;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=Histone-like protein p6 {ECO:0000303|PubMed:12480935};
DE AltName: Full=Double-stranded DNA-binding protein p6 {ECO:0000305};
DE AltName: Full=Gene product 6 {ECO:0000305};
DE Short=gp6 {ECO:0000305};
DE AltName: Full=Nucleoid-associated protein p6 {ECO:0000303|PubMed:12383516};
DE AltName: Full=Protein p6 {ECO:0000305};
GN Name=6;
OS Bacillus phage phi29 (Bacteriophage phi-29).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Salasmaviridae; Picovirinae; Salasvirus.
OX NCBI_TaxID=10756;
OH NCBI_TaxID=1423; Bacillus subtilis.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, AND IDENTIFICATION.
RX PubMed=6274853; DOI=10.1016/s0021-9258(19)68307-9;
RA Murray C.L., Rabinowitz J.C.;
RT "Nucleotide sequences of transcription and translation initiation regions
RT in Bacillus phage phi 29 early genes.";
RL J. Biol. Chem. 257:1053-1062(1982).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6809534; DOI=10.1016/0378-1119(82)90149-4;
RA Yoshikawa H., Ito J.;
RT "Nucleotide sequence of the major early region of bacteriophage phi 29.";
RL Gene 17:323-335(1982).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Villegas A.P., Lingohr E.J., Ceyssens P.-J., Kropinski A.M.;
RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-15.
RX PubMed=3763399; DOI=10.1093/nar/14.17.7129;
RA Innis C.A., Garvey K.J., Ito J.;
RT "Nucleotide sequence of phage phi 29 gene 7: structure of intergenic spacer
RT between the major early and late genes.";
RL Nucleic Acids Res. 14:7129-7129(1986).
RN [5]
RP FUNCTION, AND DNA-BINDING.
RX PubMed=2111580; DOI=10.1126/science.2111580;
RA Serrano M., Salas M., Hermoso J.M.;
RT "A novel nucleoprotein complex at a replication origin.";
RL Science 248:1012-1016(1990).
RN [6]
RP MUTAGENESIS.
RX PubMed=7808404; DOI=10.1007/bf00282215;
RA Bravo A., Hermoso J.M., Salas M.;
RT "A genetic approach to the identification of functional amino acids in
RT protein p6 of Bacillus subtilis phage phi 29.";
RL Mol. Gen. Genet. 245:529-536(1994).
RN [7]
RP DOMAIN, MUTAGENESIS OF LYS-3; GLN-6; ARG-7; THR-10; LYS-11; ASN-15 AND
RP LYS-18, AND DNA-BINDING.
RX PubMed=7925279; DOI=10.1002/j.1460-2075.1994.tb06755.x;
RA Freire R., Salas M., Hermoso J.M.;
RT "A new protein domain for binding to DNA through the minor groove.";
RL EMBO J. 13:4353-4360(1994).
RN [8]
RP FUNCTION.
RX PubMed=11384991; DOI=10.1074/jbc.m103738200;
RA Camacho A., Salas M.;
RT "Repression of bacteriophage phi 29 early promoter C2 by viral protein p6
RT is due to impairment of closed complex.";
RL J. Biol. Chem. 276:28927-28932(2001).
RN [9]
RP SUBUNIT, MUTAGENESIS OF ILE-9 AND ALA-45, AND DNA-BINDING.
RX PubMed=12383516; DOI=10.1016/s0378-1119(02)00857-0;
RA Abril A., Salas M., Hermoso J.M.;
RT "The in vivo function of phage phi29 nucleoid-associated protein p6
RT requires formation of dimers.";
RL Gene 296:187-194(2002).
RN [10]
RP INTERACTION WITH DNA REPLICATION PROTEIN 17.
RX PubMed=12480935; DOI=10.1074/jbc.m210289200;
RA Crucitti P., Abril A.M., Salas M.;
RT "Bacteriophage phi 29 early protein p17. Self-association and hetero-
RT association with the viral histone-like protein p6.";
RL J. Biol. Chem. 278:4906-4911(2003).
RN [11]
RP FUNCTION, AND DNA-BINDING.
RX PubMed=15247336; DOI=10.1093/nar/gkh668;
RA Gonzalez-Huici V., Alcorlo M., Salas M., Hermoso J.M.;
RT "Binding of phage Phi29 architectural protein p6 to the viral genome:
RT evidence for topological restriction of the phage linear DNA.";
RL Nucleic Acids Res. 32:3493-3502(2004).
RN [12]
RP FUNCTION, AND SUBUNIT.
RX PubMed=15118076; DOI=10.1093/nar/gkh565;
RA Gonzalez-Huici V., Salas M., Hermoso J.M.;
RT "Genome wide, supercoiling-dependent in vivo binding of a viral protein
RT involved in DNA replication and transcriptional control.";
RL Nucleic Acids Res. 32:2306-2314(2004).
RN [13]
RP REVIEW.
RX PubMed=15362097; DOI=10.1002/jmr.701;
RA Gonzalez-Huici V., Alcorlo M., Salas M., Hermoso J.M.;
RT "Bacteriophage phi29 protein p6: an architectural protein involved in
RT genome organization, replication and control of transcription.";
RL J. Mol. Recognit. 17:390-396(2004).
RN [14]
RP FUNCTION, AND INTERACTION WITH THE LATE GENES ACTIVATOR P4.
RX PubMed=12426390; DOI=10.1093/emboj/cdf623;
RA Calles B., Salas M., Rojo F.;
RT "The phi29 transcriptional regulator contacts the nucleoid protein p6 to
RT organize a repression complex.";
RL EMBO J. 21:6185-6194(2002).
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:0000269|PubMed:11384991,
CC ECO:0000269|PubMed:12426390, ECO:0000269|PubMed:15118076,
CC ECO:0000269|PubMed:15247336, ECO:0000269|PubMed:2111580}.
CC -!- SUBUNIT: Homodimer (PubMed:12383516). Homomultimer (PubMed:12383516).
CC Binds to double-stranded DNA giving rise to multimeric nucleoprotein
CC complexes (PubMed:12383516). Binding specificity for the viral DNA is
CC based on supercoiling, the viral genome having a negative superhelicity
CC lower than that of plasmid DNA (PubMed:15118076). Interacts with the
CC DNA replication protein p17; this interaction optimizes the binding of
CC protein p6 at the viral DNA ends, thus favoring the initiation of
CC replication (PubMed:12480935). Interacts with the late genes activator
CC p4 (via C-terminus) (PubMed:12426390). {ECO:0000269|PubMed:12383516,
CC ECO:0000269|PubMed:12426390, ECO:0000269|PubMed:12480935,
CC ECO:0000269|PubMed:15118076}.
CC -!- INDUCTION: Expressed in the early phase of the viral replicative cycle.
CC {ECO:0000269|PubMed:6274853}.
CC -!- DOMAIN: The N-terminus is involved in DNA-binding.
CC {ECO:0000269|PubMed:7925279}.
CC -!- SIMILARITY: Belongs to the phi29likevirus histone-like protein p6
CC family. {ECO:0000305}.
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DR EMBL; V01154; CAA24471.1; -; Genomic_DNA.
DR EMBL; V01155; CAA24486.1; -; Genomic_DNA.
DR EMBL; EU771092; ACE96028.1; -; Genomic_DNA.
DR EMBL; X04386; CAA27973.1; -; Genomic_DNA.
DR PIR; B92343; ERBP69.
DR RefSeq; YP_002004534.1; NC_011048.1.
DR GeneID; 6446509; -.
DR KEGG; vg:6446509; -.
DR Proteomes; UP000001207; Genome.
DR GO; GO:0017053; C:transcription repressor complex; IDA:CACAO.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0001217; F:DNA-binding transcription repressor activity; IMP:CACAO.
DR GO; GO:0030261; P:chromosome condensation; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0046782; P:regulation of viral transcription; IDA:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-templated; IMP:CACAO.
DR GO; GO:0039693; P:viral DNA genome replication; IDA:UniProtKB.
DR InterPro; IPR035188; Histone-like_p6.
DR Pfam; PF17548; p6; 1.
PE 1: Evidence at protein level;
KW DNA condensation; DNA replication; DNA-binding; Early protein;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Viral DNA replication.
FT CHAIN 1..104
FT /note="Histone-like protein p6"
FT /id="PRO_0000106568"
FT DNA_BIND 1..19
FT /evidence="ECO:0000269|PubMed:7925279"
FT REGION 85..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 3
FT /note="K->A: Decreased DNA-binding affinity. No effect on
FT dimerization."
FT /evidence="ECO:0000269|PubMed:7925279"
FT MUTAGEN 6
FT /note="Q->A,K: Decreased DNA-binding affinity. No effect on
FT dimerization."
FT /evidence="ECO:0000269|PubMed:7925279"
FT MUTAGEN 7
FT /note="R->A: Strong loss of DNA-binding affinity and no
FT formation of the initiation complex. No effect on
FT dimerization."
FT /evidence="ECO:0000269|PubMed:7925279"
FT MUTAGEN 9
FT /note="I->T: Deficient in dimer formation and viral DNA
FT replication."
FT /evidence="ECO:0000269|PubMed:12383516"
FT MUTAGEN 10
FT /note="T->A,K: Decreased DNA-binding affinity. No effect on
FT dimerization."
FT /evidence="ECO:0000269|PubMed:7925279"
FT MUTAGEN 11
FT /note="K->A: Decreased DNA-binding affinity. No effect on
FT dimerization."
FT /evidence="ECO:0000269|PubMed:7925279"
FT MUTAGEN 15
FT /note="N->A,K: No effect on DNA-binding affinity. No effect
FT on dimerization."
FT /evidence="ECO:0000269|PubMed:7925279"
FT MUTAGEN 18
FT /note="K->A: Decreased DNA-binding affinity. No effect on
FT dimerization."
FT /evidence="ECO:0000269|PubMed:7925279"
FT MUTAGEN 45
FT /note="A->V: Deficient in dimer formation and viral DNA
FT replication."
FT /evidence="ECO:0000269|PubMed:12383516"
SQ SEQUENCE 104 AA; 12005 MW; A6201B2DA0B1A4A0 CRC64;
MAKMMQREIT KTTVNVAKMV MVDGEVQVEQ LPSETFVGNL TMEQAQWRMK RKYKGEPVQV
VSVEPNTEVY ELPVEKFLEV ATVRVEKDED QEEQTEAPEE QVAE
