ID   TF1_BPSP1               Reviewed;          99 AA.
AC   P04445;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Transcription factor 1;
GN   Name=TF1;
OS   Bacillus phage SP01 (Bacteriophage SP01).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Herelleviridae; Spounavirinae; Okubovirus.
OX   NCBI_TaxID=10685;
OH   NCBI_TaxID=1423; Bacillus subtilis.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=6438630; DOI=10.1073/pnas.81.22.7031;
RA   Greene J.R., Brennan S.M., Andrew D.J., Thompson C.C., Richards S.H.,
RA   Heinrikson R.L., Geiduschek E.P.;
RT   "Sequence of the bacteriophage SP01 gene coding for transcription factor 1,
RT   a viral homologue of the bacterial type II DNA-binding proteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 81:7031-7035(1984).
RN   [2]
RP   MUTAGENESIS.
RX   PubMed=2125081; DOI=10.1016/s0022-2836(99)80004-7;
RA   Sayre M.H., Geiduschek E.P.;
RT   "Effects of mutations at amino acid 61 in the arm of TF1 on its DNA-binding
RT   properties.";
RL   J. Mol. Biol. 216:819-833(1990).
RN   [3]
RP   STRUCTURE BY NMR.
RX   PubMed=8477755; DOI=10.1111/j.1432-1033.1993.tb17830.x;
RA   Reisman J.M., Hsu V.L., Jariel-Encontre I., Lecou C., Sayre M.H.,
RA   Kearns D.R., Parello J.;
RT   "A 1H-NMR study of the transcription factor 1 from Bacillus subtilis phage
RT   SPO1 by selective 2H-labeling. Complete assignment and structural analysis
RT   of the aromatic resonances for a 22-kDa homodimer.";
RL   Eur. J. Biochem. 213:865-873(1993).
RN   [4]
RP   STRUCTURE BY NMR.
RX   PubMed=8913305; DOI=10.1006/jmbi.1996.0573;
RA   Jia X., Grove A., Ivancic M., Hsu V.L., Geiduschek E.P., Kearns D.R.;
RT   "Structure of the Bacillus subtilis phage SPO1-encoded type II DNA-binding
RT   protein TF1 in solution.";
RL   J. Mol. Biol. 263:259-268(1996).
CC   -!- FUNCTION: Selectively binds to and inhibits the transcription of
CC       hydroxymethyluracil-(hmUra)-containing DNA, such as SP01 DNA, by RNA
CC       polymerase in vitro.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the bacterial histone-like protein family.
CC       {ECO:0000305}.
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DR   EMBL; K02381; AAA32599.1; -; Genomic_DNA.
DR   PIR; A02693; DNBP11.
DR   RefSeq; YP_002300416.1; NC_011421.1.
DR   PDB; 1EXE; NMR; -; A/B=1-99.
DR   PDB; 1WTU; NMR; -; A/B=1-99.
DR   PDBsum; 1EXE; -.
DR   PDBsum; 1WTU; -.
DR   SMR; P04445; -.
DR   GeneID; 7009134; -.
DR   KEGG; vg:7009134; -.
DR   EvolutionaryTrace; P04445; -.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR   Gene3D; 4.10.520.10; -; 1.
DR   InterPro; IPR000119; Hist_DNA-bd.
DR   InterPro; IPR020816; Histone-like_DNA-bd_CS.
DR   InterPro; IPR010992; IHF-like_DNA-bd_dom_sf.
DR   PANTHER; PTHR33175; PTHR33175; 1.
DR   Pfam; PF00216; Bac_DNA_binding; 1.
DR   PRINTS; PR01727; DNABINDINGHU.
DR   SMART; SM00411; BHL; 1.
DR   SUPFAM; SSF47729; SSF47729; 1.
DR   PROSITE; PS00045; HISTONE_LIKE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; DNA-binding; Repressor;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..99
FT                   /note="Transcription factor 1"
FT                   /id="PRO_0000105082"
FT   DNA_BIND        61
FT   DNA_BIND        93..94
FT                   /evidence="ECO:0000255"
FT   REGION          52..77
FT                   /note="May be involved in preference for HM-URA DNA"
FT   REGION          90..99
FT                   /note="May be involved in preference for HM-URA DNA"
FT   HELIX           5..14
FT                   /evidence="ECO:0007829|PDB:1EXE"
FT   HELIX           21..38
FT                   /evidence="ECO:0007829|PDB:1EXE"
FT   TURN            45..47
FT                   /evidence="ECO:0007829|PDB:1EXE"
FT   STRAND          49..53
FT                   /evidence="ECO:0007829|PDB:1WTU"
FT   STRAND          63..67
FT                   /evidence="ECO:0007829|PDB:1EXE"
FT   STRAND          76..80
FT                   /evidence="ECO:0007829|PDB:1WTU"
FT   HELIX           83..92
FT                   /evidence="ECO:0007829|PDB:1EXE"
FT   HELIX           94..98
FT                   /evidence="ECO:0007829|PDB:1EXE"
SQ   SEQUENCE   99 AA;  10737 MW;  3F8CD237A46EFC37 CRC64;
     MNKTELIKAI AQDTELTQVS VSKMLASFEK ITTETVAKGD KVQLTGFLNI KPVARQARKG
     FNPQTQEALE IAPSVGVSVK PGESLKKAAE GLKYEDFAK