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 29-SEP-2021, entry version 110.
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; Salasmaviridae; 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}.
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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; 3.30.70.3560; -; 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:0007829|PDB:2FIP"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:2FIP"
FT STRAND 22..27
FT /evidence="ECO:0007829|PDB:2FIP"
FT HELIX 31..53
FT /evidence="ECO:0007829|PDB:2FIP"
FT HELIX 63..74
FT /evidence="ECO:0007829|PDB:2FIP"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:2FIP"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:2FIP"
FT HELIX 90..100
FT /evidence="ECO:0007829|PDB:2FIP"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:2FIO"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:2FIP"
FT HELIX 117..123
FT /evidence="ECO:0007829|PDB:2FIO"
SQ SEQUENCE 125 AA; 15133 MW; DF8407CC27886120 CRC64;
MPKTQRGIYH NLKESEYVAS NTDVTFFFSS ELYLNKFLDG YQEYRKKFNK KIERVAVTPW
NMDMLADITF YSEVEKRGFH AWLKGDNATW REVHVYALRI MTKPNTLDWS RIQKPRLRER
RKSMV
