G5P_BPFD
ID G5P_BPFD Reviewed; 87 AA.
AC P69542; P03669;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 76.
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 fd (Bacteriophage fd).
OC Viruses; Monodnaviria; Loebvirae; Hofneiviricota; Faserviricetes;
OC Tubulavirales; Inoviridae; Inovirus.
OX NCBI_TaxID=2847073;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=478 / Heidelberg;
RX PubMed=745987; DOI=10.1093/nar/5.12.4495;
RA Beck E., Sommer R., Auerswald E.A., Kurz C., Zink B., Osterburg G.,
RA Schaller H., Sugimoto K., Sugisaki H., Okamoto T., Takanami M.;
RT "Nucleotide sequence of bacteriophage fd DNA.";
RL Nucleic Acids Res. 5:4495-4503(1978).
RN [2]
RP PROTEIN SEQUENCE.
RX PubMed=4605211; DOI=10.1016/0014-5793(74)80246-2;
RA Nakashima Y., Dunker A.K., Marvin D.A., Konigsberg W.;
RT "The amino acid sequence of a DNA binding protein, the gene 5 product of fd
RT filamentous bacteriophage.";
RL FEBS Lett. 40:290-292(1974).
RN [3]
RP SEQUENCE REVISION.
RA Nakashima Y., Dunker A.K., Marvin D.A., Konigsberg W.;
RL FEBS Lett. 43:125-125(1974).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX PubMed=6264986; DOI=10.1016/s0006-3495(80)84931-9;
RA McPherson A., Jurnak F., Wang A., Kolpak F., Rich A., Molineux I.,
RA Fitzgerald P.;
RT "The structure of a DNA unwinding protein and its complexes with
RT oligodeoxynucleotides by X-ray diffraction.";
RL Biophys. J. 32:155-173(1980).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX PubMed=6684697; DOI=10.1016/s0022-2836(83)80065-5;
RA Brayer G.D., McPherson A.;
RT "Refined structure of the gene 5 DNA binding protein from bacteriophage
RT fd.";
RL J. Mol. Biol. 169:565-596(1983).
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; J02451; AAA32305.1; -; Genomic_DNA.
DR PIR; A04271; DDBPFD.
DR RefSeq; YP_009111299.1; NC_025824.1.
DR PDB; 2GN5; X-ray; 2.30 A; A=1-87.
DR PDBsum; 2GN5; -.
DR BMRB; P69542; -.
DR SMR; P69542; -.
DR GeneID; 22475000; -.
DR KEGG; vg:22475000; -.
DR EvolutionaryTrace; P69542; -.
DR Proteomes; UP000001836; 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.
FT CHAIN 1..87
FT /note="DNA-Binding protein G5P"
FT /id="PRO_0000098194"
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 TURN 24..26
FT /evidence="ECO:0007829|PDB:2GN5"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:2GN5"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:2GN5"
SQ SEQUENCE 87 AA; 9688 MW; 2FAD178DDC248CF0 CRC64;
MIKVEIKPSQ AQFTTRSGVS RQGKPYSLNE QLCYVDLGNE YPVLVKITLD EGQPAYAPGL
YTVHLSSFKV GQFGSLMIDR LRLVPAK