ID   G5P_BPPF3               Reviewed;          78 AA.
AC   P03672;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=DNA-Binding protein G5P;
DE            Short=G5P;
DE   AltName: Full=Single-stranded DNA-binding protein;
GN   Name=V;
OS   Pseudomonas phage Pf3 (Bacteriophage Pf3).
OC   Viruses; Monodnaviria; Loebvirae; Hofneiviricota; Faserviricetes;
OC   Tubulavirales; Inoviridae; Tertilicivirus.
OX   NCBI_TaxID=10872;
OH   NCBI_TaxID=287; Pseudomonas aeruginosa.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=New York, and Nijmegen;
RX   PubMed=3928901; DOI=10.1128/jvi.56.1.268-276.1985;
RA   Luiten R.G.M., Putterman D.G., Schoenmakers J.G.G., Konings R.N.H.,
RA   Day L.A.;
RT   "Nucleotide sequence of the genome of Pf3, an IncP-1 plasmid-specific
RT   filamentous bacteriophage of Pseudomonas aeruginosa.";
RL   J. Virol. 56:268-276(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6422463; DOI=10.1073/pnas.81.3.699;
RA   Putterman D.G., Casadevall A., Boyle P.D., Yang H.-L., Frangione B.,
RA   Day L.A.;
RT   "Major coat protein and single-stranded DNA-binding protein of filamentous
RT   virus Pf3.";
RL   Proc. Natl. Acad. Sci. U.S.A. 81:699-703(1984).
RN   [3]
RP   STRUCTURE BY NMR.
RX   PubMed=7556054; DOI=10.1002/j.1460-2075.1995.tb00087.x;
RA   Folmer R.H.A., Nilges M., Konings R.N.H., Hilbers C.W.;
RT   "Solution structure of the single-stranded DNA binding protein of the
RT   filamentous Pseudomonas phage Pf3: similarity to other proteins binding to
RT   single-stranded nucleic acids.";
RL   EMBO J. 14:4132-4142(1995).
CC   -!- FUNCTION: Binds to DNA in a highly cooperative manner without
CC       pronounced sequence specificity. During synthesis of the single-
CC       stranded (progeny) viral DNA, prevents the conversion into the double-
CC       stranded replicative form. G5P is displaced by the capsid protein G8P
CC       during phage assembly on the inner bacterial membrane (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the inovirus G5P protein family. {ECO:0000305}.
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DR   EMBL; K01435; AAA72242.1; -; Genomic_DNA.
DR   EMBL; M19377; AAA88394.1; -; Genomic_DNA.
DR   EMBL; M11912; AAA88385.1; -; Genomic_DNA.
DR   PIR; A04274; DNBPP3.
DR   PIR; S48151; S48151.
DR   RefSeq; NP_040659.1; NC_001418.1.
DR   PDB; 1PFS; NMR; -; A/B=1-78.
DR   PDBsum; 1PFS; -.
DR   SMR; P03672; -.
DR   GeneID; 1260902; -.
DR   KEGG; vg:1260902; -.
DR   EvolutionaryTrace; P03672; -.
DR   Proteomes; UP000001719; Genome.
DR   Proteomes; UP000009090; Genome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.50.140; -; 1.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   SUPFAM; SSF50249; SSF50249; 1.
PE   1: Evidence at protein level;
KW   3D-structure; DNA replication; DNA-binding; Reference proteome.
FT   CHAIN           1..78
FT                   /note="DNA-Binding protein G5P"
FT                   /id="PRO_0000098209"
FT   STRAND          2..15
FT                   /evidence="ECO:0007829|PDB:1PFS"
FT   STRAND          21..29
FT                   /evidence="ECO:0007829|PDB:1PFS"
FT   STRAND          38..43
FT                   /evidence="ECO:0007829|PDB:1PFS"
FT   STRAND          50..62
FT                   /evidence="ECO:0007829|PDB:1PFS"
FT   STRAND          65..70
FT                   /evidence="ECO:0007829|PDB:1PFS"
SQ   SEQUENCE   78 AA;  8903 MW;  65F8EAD34A2910FF CRC64;
     MNIQITFTDS VRQGTSAKGN PYTFQEGFLH LEDKPFPLQC QFFVESVIPA GSYQVPYRIN
     VNNGRPELAF DFKAMKRA