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Database: UniProt
Entry: TF4_BPPH2
LinkDB: TF4_BPPH2
Original site: TF4_BPPH2 
ID   TF4_BPPH2               Reviewed;         125 AA.
AC   P03682; B3VMN8;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   12-AUG-2020, entry version 107.
DE   RecName: Full=Late genes activator p4 {ECO:0000305};
DE   AltName: Full=Gene product 4 {ECO:0000305};
DE            Short=gp4 {ECO:0000305};
DE   AltName: Full=Protein p4 {ECO:0000305};
GN   Name=4;
OS   Bacillus phage phi29 (Bacteriophage phi-29).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Podoviridae; Picovirinae; Salasvirus.
OX   NCBI_TaxID=10756;
OH   NCBI_TaxID=1423; Bacillus subtilis.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6292852; DOI=10.1093/nar/10.19.5785;
RA   Escarmis C., Salas M.;
RT   "Nucleotide sequence of the early genes 3 and 4 of bacteriophage phi 29.";
RL   Nucleic Acids Res. 10:5785-5798(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   FUNCTION, AND DNA-BINDING.
RX   PubMed=2107318; DOI=10.1016/0022-2836(90)90072-t;
RA   Rojo F., Zaballos A., Salas M.;
RT   "Bend induced by the phage phi 29 transcriptional activator in the viral
RT   late promoter is required for activation.";
RL   J. Mol. Biol. 211:713-725(1990).
RN   [5]
RP   INTERACTION WITH HOST RNA POLYMERASE, FUNCTION, MUTAGENESIS OF ARG-116;
RP   LEU-117; GLU-119 AND ARG-120, AND DNA-BINDING.
RX   PubMed=8617213; DOI=10.1002/j.1460-2075.1996.tb00368.x;
RA   Monsalve M., Mencia M., Rojo F., Salas M.;
RT   "Activation and repression of transcription at two different phage phi29
RT   promoters are mediated by interaction of the same residues of regulatory
RT   protein p4 with RNA polymerase.";
RL   EMBO J. 15:383-391(1996).
RN   [6]
RP   INTERACTION WITH HOST RNA POLYMERASE, AND DNA-BINDING.
RX   PubMed=8799127; DOI=10.1073/pnas.93.17.8913;
RA   Monsalve M., Mencia M., Salas M., Rojo F.;
RT   "Protein p4 represses phage phi 29 A2c promoter by interacting with the
RT   alpha subunit of Bacillus subtilis RNA polymerase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:8913-8918(1996).
RN   [7]
RP   REVIEW.
RX   PubMed=9594570; DOI=10.1016/s0079-6603(08)60888-0;
RA   Rojo F., Mencia M., Monsalve M., Salas M.;
RT   "Transcription activation and repression by interaction of a regulator with
RT   the alpha subunit of RNA polymerase: the model of phage phi 29 protein
RT   p4.";
RL   Prog. Nucleic Acid Res. Mol. Biol. 60:29-46(1998).
RN   [8]
RP   FUNCTION, AND INTERACTION WITH HOST RNA POLYMERASE.
RX   PubMed=9784366; DOI=10.1006/jmbi.1998.2084;
RA   Monsalve M., Calles B., Mencia M., Rojo F., Salas M.;
RT   "Binding of phage phi29 protein p4 to the early A2c promoter: recruitment
RT   of a repressor by the RNA polymerase.";
RL   J. Mol. Biol. 283:559-569(1998).
RN   [9]
RP   FUNCTION.
RX   PubMed=21614197; DOI=10.3390/ijms11125129;
RA   Camacho A., Salas M.;
RT   "Molecular interactions and protein-induced DNA hairpin in the
RT   transcriptional control of bacteriophage phi29 DNA.";
RL   Int. J. Mol. Sci. 11:5129-5142(2010).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 2-116 IN COMPLEX WITH DNA.
RX   PubMed=16600871; DOI=10.1016/j.molcel.2006.02.019;
RA   Badia D., Camacho A., Perez-Lago L., Escandon C., Salas M., Coll M.;
RT   "The structure of phage phi29 transcription regulator p4-DNA complex
RT   reveals an N-hook motif for DNA.";
RL   Mol. Cell 22:73-81(2006).
RN   [11]
RP   FUNCTION.
RX   PubMed=11689446; DOI=10.1093/emboj/20.21.6060;
RA   Camacho A., Salas M.;
RT   "Mechanism for the switch of phi29 DNA early to late transcription by
RT   regulatory protein p4 and histone-like protein p6.";
RL   EMBO J. 20:6060-6070(2001).
RN   [12]
RP   FUNCTION, AND INTERACTION WITH HISTONE-LIKE PROTEIN P6.
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).
RN   [13]
RP   FUNCTION.
RX   PubMed=14757050; DOI=10.1016/j.jmb.2003.12.039;
RA   Camacho A., Salas M.;
RT   "Molecular interplay between RNA polymerase and two transcriptional
RT   regulators in promoter switch.";
RL   J. Mol. Biol. 336:357-368(2004).
CC   -!- FUNCTION: Mediates, together with protein p6, the early to late
CC       transcriptional switch by stabilizing the binding of host RNA
CC       polymerase (RNAP) to the late A3 promoter. Activates transcription from
CC       the late A3 promoter and represses the main early promoters A2b and A2c
CC       by modifying the topology of the sequences encompassing early promoters
CC       A2c and A2b and late promoter A3 in a hairpin. Proteins p6 and p4 bind
CC       cooperatively to an approximately 200 bp DNA region located between the
CC       late A3 and the early A2c promoters. Binding of p4 molecules induces
CC       the reorganization of the binding of protein p6, giving rise to the
CC       nucleoprotein complex responsible for the switch from early to late
CC       transcription. {ECO:0000269|PubMed:11689446,
CC       ECO:0000269|PubMed:12426390, ECO:0000269|PubMed:14757050,
CC       ECO:0000269|PubMed:2107318, ECO:0000269|PubMed:21614197,
CC       ECO:0000269|PubMed:8617213, ECO:0000269|PubMed:9784366}.
CC   -!- SUBUNIT: Interacts with host RNA polymerase (via C-terminus)
CC       (PubMed:8617213, PubMed:8799127, PubMed:9784366). Interacts with DNA;
CC       binds to the A2b, A2c and A3 promoters (PubMed:8617213). Interacts (via
CC       C-terminus) with the histone-like protein p6 (PubMed:12426390).
CC       {ECO:0000269|PubMed:12426390, ECO:0000269|PubMed:8617213,
CC       ECO:0000269|PubMed:8799127, ECO:0000269|PubMed:9784366}.
CC   -!- SIMILARITY: Belongs to the phi29likevirus late genes activator p4
CC       family. {ECO:0000305}.
DR   EMBL; J02479; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; V01155; CAA24482.1; -; Genomic_DNA.
DR   EMBL; EU771092; ACE96025.1; -; Genomic_DNA.
DR   PIR; C93439; ERBP49.
DR   RefSeq; YP_002004531.1; NC_011048.1.
DR   PDB; 2FIO; X-ray; 2.70 A; A/B=2-124.
DR   PDB; 2FIP; X-ray; 2.00 A; A/B/C/D/E/F=2-116.
DR   PDBsum; 2FIO; -.
DR   PDBsum; 2FIP; -.
DR   SMR; P03682; -.
DR   GeneID; 6446523; -.
DR   KEGG; vg:6446523; -.
DR   EvolutionaryTrace; P03682; -.
DR   Proteomes; UP000001207; Genome.
DR   GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR   GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:InterPro.
DR   GO; GO:0016987; F:sigma factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   Gene3D; 1.10.274.40; -; 1.
DR   InterPro; IPR038246; Phi-29-like_sf.
DR   InterPro; IPR008771; Phi-29_GP4.
DR   Pfam; PF05464; Phi-29_GP4; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; DNA-binding; Early protein; Reference proteome;
KW   Repressor; Sigma factor; Transcription; Transcription regulation.
FT   CHAIN           1..125
FT                   /note="Late genes activator p4"
FT                   /id="PRO_0000106560"
FT   DNA_BIND        77..96
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255"
FT   SITE            120
FT                   /note="Interaction with host RNA polymerase and activation
FT                   of the phi29 late A3 promoter"
FT                   /evidence="ECO:0000269|PubMed:8799127"
FT   MUTAGEN         116
FT                   /note="R->E: No effect on transcription activation from the
FT                   A3 promoter and on transcription repression from the A2c
FT                   promoter. No effect on the interaction with host RNAP."
FT                   /evidence="ECO:0000269|PubMed:8617213"
FT   MUTAGEN         117
FT                   /note="L->A: 60% loss of transcription activation from the
FT                   A3 promoter and 60% loss of transcription repression from
FT                   the A2c promoter. Poor interaction with host RNAP."
FT                   /evidence="ECO:0000269|PubMed:8617213"
FT   MUTAGEN         119
FT                   /note="E->Q: No effect on transcription activation from the
FT                   A3 promoter and on transcription repression from the A2c
FT                   promoter. No effect on the interaction with host RNAP."
FT                   /evidence="ECO:0000269|PubMed:8617213"
FT   MUTAGEN         120
FT                   /note="R->Q: 80% loss of transcription activation from the
FT                   A3 promoter and 80% loss of transcription repression from
FT                   the A2c promoter. Complete loss of interaction with host
FT                   RNAP."
FT                   /evidence="ECO:0000269|PubMed:8617213"
FT   HELIX           12..14
FT                   /evidence="ECO:0000244|PDB:2FIP"
FT   STRAND          18..20
FT                   /evidence="ECO:0000244|PDB:2FIP"
FT   STRAND          22..27
FT                   /evidence="ECO:0000244|PDB:2FIP"
FT   HELIX           31..53
FT                   /evidence="ECO:0000244|PDB:2FIP"
FT   HELIX           63..74
FT                   /evidence="ECO:0000244|PDB:2FIP"
FT   STRAND          81..83
FT                   /evidence="ECO:0000244|PDB:2FIP"
FT   STRAND          86..88
FT                   /evidence="ECO:0000244|PDB:2FIP"
FT   HELIX           90..100
FT                   /evidence="ECO:0000244|PDB:2FIP"
FT   STRAND          103..105
FT                   /evidence="ECO:0000244|PDB:2FIO"
FT   STRAND          110..112
FT                   /evidence="ECO:0000244|PDB:2FIP"
FT   HELIX           117..123
FT                   /evidence="ECO:0000244|PDB:2FIO"
SQ   SEQUENCE   125 AA;  15133 MW;  DF8407CC27886120 CRC64;
     MPKTQRGIYH NLKESEYVAS NTDVTFFFSS ELYLNKFLDG YQEYRKKFNK KIERVAVTPW
     NMDMLADITF YSEVEKRGFH AWLKGDNATW REVHVYALRI MTKPNTLDWS RIQKPRLRER
     RKSMV
//
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