ID VHED_BPIKE STANDARD; PRT; 88 AA. AC P03670; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-JUL-1986, sequence version 1. DT 21-MAR-2006, entry version 33. DE Helix-destabilizing protein (Single-stranded DNA-binding protein) DE (GPV). GN Name=V; OS Bacteriophage IKe. OC Viruses; ssDNA viruses; Inoviridae; Inovirus. OX NCBI_TaxID=10867; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=84010854; PubMed=6312049; RA Peeters B.P.H., Konings R.N.H., Schoenmakers J.G.G.; RT "Characterization of the DNA binding protein encoded by the N-specific RT filamentous Escherichia coli phage IKe. Binding properties of the RT protein and nucleotide sequence of the gene."; RL J. Mol. Biol. 169:197-215(1983). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=85160831; PubMed=3981635; RA Peeters B.P.H., Peters R.M., Schoenmakers J.G.G., Konings R.N.H.; RT "Nucleotide sequence and genetic organization of the genome of the N- RT specific filamentous bacteriophage IKe. Comparison with the genome of RT the F-specific filamentous phages M13, fd and f1."; RL J. Mol. Biol. 181:27-39(1985). RN [3] RP STRUCTURE BY NMR. RX MEDLINE=88004481; PubMed=3308460; RA de Jong E.A., Konings R.N.H., Harmsen B.J., Prinse C.W., Hilbers C.W.; RT "1H-NMR studies on the gene-5-encoded single-stranded DNA binding RT protein of the filamentous bacteriophage IKe. General spectral and RT structural features."; RL Eur. J. Biochem. 167:563-572(1987). RN [4] RP STRUCTURE BY NMR. RX MEDLINE=92135212; PubMed=1734970; RA van Duynhoven J.P.M., Folkers P.J.M., Prinse C.W., Harmsen B.J., RA Konings R.N.H., Hilbers C.W.; RT "Assignment of the 1H NMR spectrum and secondary structure elucidation RT of the single-stranded DNA binding protein encoded by the filamentous RT bacteriophage IKe."; RL Biochemistry 31:1254-1262(1992). RN [5] RP 3D-STRUCTURE MODELING. RX MEDLINE=90104657; PubMed=3270530; RA Brayer G.D.; RT "A preliminary structure for the DNA binding protein from RT bacteriophage IKe."; RL J. Biomol. Struct. Dyn. 4:859-868(1987). CC -!- FUNCTION: Binds to DNA in a highly cooperative manner without CC pronounced sequence specificity. In the presence of single- CC stranded DNA it binds DNA cooperatively to form a helical protein- CC DNA complex. Prevent the conversion during synthesis of the CC single-stranded (progeny) viral DNA back into the double-stranded CC replicative form. GPV is displaced by the coat proteins (on the CC inner bacterial membrane) during phage assembly (By similarity). CC -!- SUBUNIT: Homodimer (By similarity). CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X01914; CAA25988.1; -; Genomic_DNA. DR EMBL; X02139; CAA26069.1; -; Genomic_DNA. DR PIR; A04272; DDBPIK. DR HSSP; P03669; 1VQC. DR InterPro; IPR008994; OB_fold_NA_bd. DR InterPro; IPR012340; OB_NA_bd_sub. DR InterPro; IPR003512; Phage_DNA_bind. DR Pfam; PF02303; Phage_DNA_bind; 1. DR ProDom; PD015272; Phage_DNA_bind; 1. KW DNA replication; DNA-binding. FT CHAIN 1 88 Helix-destabilizing protein. FT /FTId=PRO_0000098199. SQ SEQUENCE 88 AA; 9813 MW; 07074FB935716CB9 CRC64; MLTVEIHDSQ VSVKERSGVS QKSGKPYTIR EQEAYIDLGG VYPALFNFNL EDGQQPYPAG KYRLHPASFK INNFGQVAVG RVLLESVK //