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 01-NOV-1997 (REL. 35, LAST ANNOTATION UPDATE) DE HELIX-DESTABILIZING PROTEIN (DNA-BINDING PROTEIN) (GPV). GN V. OS BACTERIOPHAGE IKE. OC VIRUSES; SSDNA VIRUSES; INOVIRIDAE; INOVIRUS. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 84010854. 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. 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. 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. 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 MODELLING. RX MEDLINE; 90104657. 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 This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- 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; G14958; -. DR EMBL; X02139; G14945; -. DR EMBL; K02750; G215064; -. DR PIR; A04272; DDBPIK. DR HSSP; P03669; 1VQC. KW DNA-BINDING; DNA REPLICATION. SQ SEQUENCE 88 AA; 9813 MW; 060F563D CRC32; MLTVEIHDSQ VSVKERSGVS QKSGKPYTIR EQEAYIDLGG VYPALFNFNL EDGQQPYPAG KYRLHPASFK INNFGQVAVG RVLLESVK //