G5P_BPF1
ID G5P_BPF1 Reviewed; 87 AA.
AC P69543; P03669;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=DNA-Binding protein G5P;
DE Short=G5P;
DE AltName: Full=GPV;
DE AltName: Full=Single-stranded DNA-binding protein;
GN Name=V;
OS Enterobacteria phage f1 (Bacteriophage f1).
OC Viruses; Monodnaviria; Loebvirae; Hofneiviricota; Faserviricetes;
OC Tubulavirales; Inoviridae; Inovirus.
OX NCBI_TaxID=10863;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6282703; DOI=10.1016/0378-1119(81)90059-7;
RA Beck E., Zink B.;
RT "Nucleotide sequence and genome organisation of filamentous bacteriophages
RT f1 and fd.";
RL Gene 16:35-58(1981).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7373712; DOI=10.1128/jvi.34.1.40-50.1980;
RA Hill D.F., Petersen G.B.;
RT "Nucleotide sequences in bacteriophage f1 DNA: nucleotide sequence of genes
RT V, VII, and VIII.";
RL J. Virol. 34:40-50(1980).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6292494; DOI=10.1128/jvi.44.1.32-46.1982;
RA Hill D.F., Petersen G.B.;
RT "Nucleotide sequence of bacteriophage f1 DNA.";
RL J. Virol. 44:32-46(1982).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 13-57.
RX PubMed=353810; DOI=10.1073/pnas.75.5.2266;
RA Ravetch J.V., Horiuchi K., Zinder N.D.;
RT "Nucleotide sequence of the recognition site for the restriction-
RT modification enzyme of Escherichia coli B.";
RL Proc. Natl. Acad. Sci. U.S.A. 75:2266-2270(1978).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=8134350; DOI=10.1073/pnas.91.6.2071;
RA Skinner M.M., Zhang H., Leschnitzer D.H., Guan Y., Bellamy H., Sweet R.M.,
RA Gray C.W., Konings R.N.H., Wang A.H.-J., Terwilliger T.C.;
RT "Structure of the gene V protein of bacteriophage f1 determined by
RT multiwavelength X-ray diffraction on the selenomethionyl protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:2071-2075(1994).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF MUTANTS HIS-41 AND PHE-41.
RX PubMed=8011642; DOI=10.1021/bi00191a004;
RA Guan Y., Zhang H., Konings R.N., Hilbers C.W., Terwilliger T.C., Wang A.H.;
RT "Crystal structures of Y41H and Y41F mutants of gene V protein from Ff
RT phage suggest possible protein-protein interactions in the GVP-ssDNA
RT complex.";
RL Biochemistry 33:7768-7778(1994).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANTS ILE-35 AND VAL-47.
RX PubMed=8648642; DOI=10.1006/jmbi.1996.0309;
RA Zhang H., Skinner M.M., Sandberg W.S., Wang A.H.-J., Terwilliger T.C.;
RT "Context dependence of mutational effects in a protein: the crystal
RT structures of the V35I, I47V and V35I/I47V gene V protein core mutants.";
RL J. Mol. Biol. 259:148-159(1996).
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; V00606; CAA23868.1; -; Genomic_DNA.
DR EMBL; J02448; AAA32211.1; -; Genomic_DNA.
DR EMBL; M10677; AAA32226.1; -; Genomic_DNA.
DR PIR; E04271; DDBPF1.
DR PDB; 1AE2; X-ray; 2.00 A; A=1-87.
DR PDB; 1AE3; X-ray; 2.00 A; A=1-86.
DR PDB; 1GKH; X-ray; 1.70 A; A=1-87.
DR PDB; 1GVP; X-ray; 1.60 A; A=1-87.
DR PDB; 1VQA; X-ray; 1.80 A; A=1-87.
DR PDB; 1VQB; X-ray; 1.80 A; A=1-87.
DR PDB; 1VQC; X-ray; 1.80 A; A=1-87.
DR PDB; 1VQD; X-ray; 1.82 A; A=1-87.
DR PDB; 1VQE; X-ray; 1.80 A; A=1-87.
DR PDB; 1VQF; X-ray; 1.80 A; A=1-87.
DR PDB; 1VQG; X-ray; 1.82 A; A=1-87.
DR PDB; 1VQH; X-ray; 1.80 A; A=1-87.
DR PDB; 1VQI; X-ray; 1.80 A; A=1-87.
DR PDB; 1VQJ; X-ray; 1.80 A; A=1-87.
DR PDB; 1YHA; X-ray; 2.50 A; A/B=1-87.
DR PDB; 1YHB; X-ray; 2.20 A; A=1-87.
DR PDBsum; 1AE2; -.
DR PDBsum; 1AE3; -.
DR PDBsum; 1GKH; -.
DR PDBsum; 1GVP; -.
DR PDBsum; 1VQA; -.
DR PDBsum; 1VQB; -.
DR PDBsum; 1VQC; -.
DR PDBsum; 1VQD; -.
DR PDBsum; 1VQE; -.
DR PDBsum; 1VQF; -.
DR PDBsum; 1VQG; -.
DR PDBsum; 1VQH; -.
DR PDBsum; 1VQI; -.
DR PDBsum; 1VQJ; -.
DR PDBsum; 1YHA; -.
DR PDBsum; 1YHB; -.
DR BMRB; P69543; -.
DR SMR; P69543; -.
DR EvolutionaryTrace; P69543; -.
DR Proteomes; UP000002557; Genome.
DR Proteomes; UP000241027; Genome.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0039684; P:rolling circle single-stranded viral DNA replication; IDA:UniProtKB.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR003512; Phage_M13_G5P_DNA-bd.
DR Pfam; PF02303; Phage_DNA_bind; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA replication; DNA-binding.
FT CHAIN 1..87
FT /note="DNA-Binding protein G5P"
FT /id="PRO_0000098195"
FT SITE 16
FT /note="Involved in DNA binding"
FT SITE 21
FT /note="Involved in DNA binding"
FT SITE 26
FT /note="Involved in DNA binding"
FT SITE 34
FT /note="Involved in DNA binding"
FT SITE 41
FT /note="Involved in DNA binding, and in the dimer-dimer
FT interactions of the protein-ssDNA complex"
FT SITE 46
FT /note="Involved in DNA binding"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:1GVP"
FT HELIX 8..10
FT /evidence="ECO:0007829|PDB:1GVP"
FT STRAND 14..19
FT /evidence="ECO:0007829|PDB:1GVP"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:1YHB"
FT STRAND 25..35
FT /evidence="ECO:0007829|PDB:1GVP"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:1GVP"
FT STRAND 43..48
FT /evidence="ECO:0007829|PDB:1GVP"
FT STRAND 58..63
FT /evidence="ECO:0007829|PDB:1GVP"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:1GVP"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:1GVP"
FT STRAND 74..80
FT /evidence="ECO:0007829|PDB:1GVP"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:1GVP"
SQ SEQUENCE 87 AA; 9688 MW; 2FAD178DDC248CF0 CRC64;
MIKVEIKPSQ AQFTTRSGVS RQGKPYSLNE QLCYVDLGNE YPVLVKITLD EGQPAYAPGL
YTVHLSSFKV GQFGSLMIDR LRLVPAK
