ID VHED_BPIKE STANDARD; PRT; 88 AA. AC P03670; DT 21-JUL-1986 (Rel. 01, Created) DT 21-JUL-1986 (Rel. 01, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Helix-destabilizing protein (Single-stranded DNA binding protein) DE (GPV). GN V. OS Bacteriophage IKe. OC Viruses; ssDNA viruses; Inoviridae; Inovirus. OX NCBI_TaxID=10867; RN [1] RP SEQUENCE FROM N.A. 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 RT N-specific filamentous Escherichia coli phage IKe. Binding properties RT of the protein and nucleotide sequence of the gene."; RL J. Mol. Biol. 169:197-215(1983). RN [2] RP SEQUENCE FROM N.A. 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 RT elucidation of the single-stranded DNA binding protein encoded by the RT filamentous 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; -. DR EMBL; X02139; CAA26069.1; -. DR PIR; A04272; DDBPIK. DR HSSP; P03669; 1VQC. DR InterPro; IPR003512; Phage_DNA_bind. DR Pfam; PF02303; Phage_DNA_bind; 1. DR ProDom; PD015272; Phage_DNA_bind; 1. KW DNA-binding; DNA replication. SQ SEQUENCE 88 AA; 9813 MW; 07074FB935716CB9 CRC64; MLTVEIHDSQ VSVKERSGVS QKSGKPYTIR EQEAYIDLGG VYPALFNFNL EDGQQPYPAG KYRLHPASFK INNFGQVAVG RVLLESVK //