G5P_BPM13
ID G5P_BPM13 Reviewed; 87 AA.
AC P69544; P03669;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=DNA-Binding protein G5P;
DE Short=G5P;
DE AltName: Full=Single-stranded DNA-binding protein;
GN Name=V;
OS Enterobacteria phage M13 (Bacteriophage M13).
OC Viruses; Monodnaviria; Loebvirae; Hofneiviricota; Faserviricetes;
OC Tubulavirales; Inoviridae; Inovirus.
OX NCBI_TaxID=1977402;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6254849; DOI=10.1016/0378-1119(80)90093-1;
RA van Wezenbeek P.M.G.F., Hulsebos T.J.M., Schoenmakers J.G.G.;
RT "Nucleotide sequence of the filamentous bacteriophage M13 DNA genome:
RT comparison with phage fd.";
RL Gene 11:129-148(1980).
RN [2]
RP PROTEIN SEQUENCE OF 1-19 AND 87.
RX PubMed=4605212; DOI=10.1016/s0006-291x(74)80016-1;
RA Cuypers T., van der Ouderaa F.J., de Jong W.W.;
RT "The amino acid sequence of gene 5 protein of bacteriophage M13.";
RL Biochem. Biophys. Res. Commun. 59:557-563(1974).
RN [3]
RP STRUCTURE BY NMR.
RX PubMed=1761038; DOI=10.1111/j.1432-1033.1991.tb16382.x;
RA Folkers P.J.M., van Duynhoven J.P.M., Jonker A.J., Harmsen B.J.M.,
RA Konings R.N.;
RT "Sequence-specific 1H-NMR assignment and secondary structure of the Tyr-
RT 41-->His mutant of the single-stranded DNA binding protein, gene V protein,
RT encoded by the filamentous bacteriophage M13.";
RL Eur. J. Biochem. 202:349-360(1991).
RN [4]
RP STRUCTURE BY NMR OF MUTANT HIS-41.
RX PubMed=2307226; DOI=10.1016/0014-5793(90)80621-o;
RA van Duynhoven J.P., Folkers P.J., Stassen A.P., Harmsen B.J., Konings R.N.,
RA Hilbers C.W.;
RT "Structure of the DNA binding wing of the gene-V encoded single-stranded
RT DNA binding protein of the filamentous bacteriophage M13.";
RL FEBS Lett. 261:1-4(1990).
RN [5]
RP STRUCTURE BY NMR OF MUTANT HIS-41.
RX PubMed=8107108; DOI=10.1006/jmbi.1994.1132;
RA Folkers P.J.M., Nilges M., Folmer R.H.A., Konings R.N.H., Hilbers C.W.;
RT "The solution structure of the Tyr41-->His mutant of the single-stranded
RT DNA binding protein encoded by gene V of the filamentous bacteriophage
RT M13.";
RL J. Mol. Biol. 236:229-246(1994).
RN [6]
RP STRUCTURE BY NMR OF MUTANT HIS-41.
RX PubMed=7556200; DOI=10.1111/j.1432-1033.1995.tb20837.x;
RA Prompers J.J., Folmer R.H.A., Nilges M., Folkers P.J.M., Konings R.N.H.,
RA Hilbers C.W.;
RT "Refined solution structure of the Tyr41-->His mutant of the M13 gene V
RT protein. A comparison with the crystal structure.";
RL Eur. J. Biochem. 232:506-514(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.
CC -!- SUBUNIT: Homodimer.
CC -!- SIMILARITY: Belongs to the inovirus G5P protein family. {ECO:0000305}.
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DR EMBL; V00604; CAA23858.1; -; Genomic_DNA.
DR PIR; C04271; DDBPM3.
DR PDB; 2GVA; NMR; -; A/B=1-87.
DR PDB; 2GVB; NMR; -; A/B=1-87.
DR PDBsum; 2GVA; -.
DR PDBsum; 2GVB; -.
DR BMRB; P69544; -.
DR SMR; P69544; -.
DR EvolutionaryTrace; P69544; -.
DR Proteomes; UP000002111; 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; Direct protein sequencing; DNA replication; DNA-binding;
KW Reference proteome.
FT CHAIN 1..87
FT /note="DNA-Binding protein G5P"
FT /id="PRO_0000098196"
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 3..5
FT /evidence="ECO:0007829|PDB:2GVA"
FT HELIX 8..10
FT /evidence="ECO:0007829|PDB:2GVA"
FT STRAND 19..25
FT /evidence="ECO:0007829|PDB:2GVA"
FT STRAND 29..35
FT /evidence="ECO:0007829|PDB:2GVA"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:2GVA"
FT STRAND 43..49
FT /evidence="ECO:0007829|PDB:2GVA"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:2GVA"
FT STRAND 58..64
FT /evidence="ECO:0007829|PDB:2GVA"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:2GVA"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:2GVB"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:2GVA"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:2GVA"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:2GVA"
SQ SEQUENCE 87 AA; 9688 MW; 2FAD178DDC248CF0 CRC64;
MIKVEIKPSQ AQFTTRSGVS RQGKPYSLNE QLCYVDLGNE YPVLVKITLD EGQPAYAPGL
YTVHLSSFKV GQFGSLMIDR LRLVPAK
