ID GP167_BPPH2 Reviewed; 130 AA.
AC P16517; B3VMQ4;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 08-NOV-2023, entry version 82.
DE RecName: Full=DNA replication protein 16.7;
DE AltName: Full=Gene product 16.7;
DE Short=gp16.7;
DE AltName: Full=Protein p16.7;
GN Name=16.7;
OS Bacillus phage phi29 (Bacteriophage phi-29).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Salasmaviridae; Picovirinae; Salasvirus; Salasvirus phi29.
OX NCBI_TaxID=2884424;
OH NCBI_TaxID=1423; Bacillus subtilis.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3007295; DOI=10.1016/0378-1119(85)90053-8;
RA Garvey K.J., Yoshikawa H., Ito J.;
RT "The complete sequence of the Bacillus phage phi 29 right early region.";
RL Gene 40:301-309(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Villegas A.P., Lingohr E.J., Ceyssens P.-J., Kropinski A.M.;
RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION.
RX PubMed=10921898; DOI=10.1093/emboj/19.15.4182;
RA Meijer W.J., Lewis P.J., Errington J., Salas M.;
RT "Dynamic relocalization of phage phi 29 DNA during replication and the role
RT of the viral protein p16.7.";
RL EMBO J. 19:4182-4190(2000).
RN [4]
RP CHARACTERIZATION, INDUCTION, FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=11169113; DOI=10.1046/j.1365-2958.2001.02260.x;
RA Meijer W.J., Serna-Rico A., Salas M.;
RT "Characterization of the bacteriophage phi29-encoded protein p16.7: a
RT membrane protein involved in phage DNA replication.";
RL Mol. Microbiol. 39:731-746(2001).
RN [5]
RP DNA-BINDING, AND FUNCTION.
RX PubMed=11741949; DOI=10.1074/jbc.m109312200;
RA Serna-Rico A., Salas M., Meijer W.J.;
RT "The Bacillus subtilis phage phi 29 protein p16.7, involved in phi 29 DNA
RT replication, is a membrane-localized single-stranded DNA-binding protein.";
RL J. Biol. Chem. 277:6733-6742(2002).
RN [6]
RP FUNCTION.
RX PubMed=17526715; DOI=10.1128/jb.00402-07;
RA Alcorlo M., Gonzalez-Huici V., Hermoso J.M., Meijer W.J., Salas M.;
RT "The phage phi29 membrane protein p16.7, involved in DNA replication, is
RT required for efficient ejection of the viral genome.";
RL J. Bacteriol. 189:5542-5549(2007).
RN [7]
RP SUBUNIT, DNA-BINDING, AND MUTAGENESIS OF TRP-116 AND ASN-120.
RX PubMed=17426023; DOI=10.1074/jbc.m611778200;
RA Munoz-Espin D., Fuertes M.A., Jimenez M., Villar L., Alonso C., Rivas G.,
RA Salas M., Meijer W.J.;
RT "Structural and functional analysis of phi29 p16.7C dimerization mutants:
RT identification of a novel aromatic cage dimerization motif.";
RL J. Biol. Chem. 282:16521-16531(2007).
RN [8] {ECO:0007744|PDB:1ZAE, ECO:0007744|PDB:2BNK}
RP STRUCTURE BY NMR OF 63-130, AND SUBUNIT.
RX PubMed=15772069; DOI=10.1074/jbc.m501687200;
RA Asensio J.L., Albert A., Munoz-Espin D., Gonzalez C., Hermoso J.,
RA Villar L., Jimenez-Barbero J., Salas M., Meijer W.J.;
RT "Structure of the functional domain of phi29 replication organizer:
RT insights into oligomerization and dna binding.";
RL J. Biol. Chem. 280:20730-20739(2005).
RN [9] {ECO:0007744|PDB:2C5R}
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 64-130 IN COMPLEX WITH DNA, AND
RP DNA-BINDING.
RX PubMed=16275651; DOI=10.1074/jbc.c500429200;
RA Albert A., Munoz-Espin D., Jimenez M., Asensio J.L., Hermoso J.A.,
RA Salas M., Meijer W.J.;
RT "Structural basis for membrane anchorage of viral phi29 DNA during
RT replication.";
RL J. Biol. Chem. 280:42486-42488(2005).
CC -!- FUNCTION: Binds to the long stretches of ssDNA of the viral DNA
CC replication intermediates created during the protein-primed mechanism
CC of replication of the viral genome and attaches the viral DNA to the
CC membrane of the infected cells (PubMed:11741949) (PubMed:11169113).
CC Required for the redistribution of replicating viral DNA from the
CC initial replication site to membrane-associated sites surrounding the
CC nucleoid (PubMed:10921898). Required for the second pull step of DNA
CC ejection (PubMed:17526715). {ECO:0000269|PubMed:10921898,
CC ECO:0000269|PubMed:11169113, ECO:0000269|PubMed:11741949,
CC ECO:0000269|PubMed:17526715}.
CC -!- SUBUNIT: Homodimer (PubMed:11169113, PubMed:17426023)
CC (PubMed:15772069); homooligomer (PubMed:17426023). Interacts with DNA;
CC one dsDNA binding subunit is constituted by three p16.7. dimers
CC (PubMed:16275651, PubMed:17426023). {ECO:0000269|PubMed:11169113,
CC ECO:0000269|PubMed:15772069, ECO:0000269|PubMed:16275651,
CC ECO:0000269|PubMed:17426023}.
CC -!- SUBCELLULAR LOCATION: Host cell membrane {ECO:0000255,
CC ECO:0000269|PubMed:11169113}; Single-pass membrane protein
CC {ECO:0000255, ECO:0000269|PubMed:11169113}.
CC -!- INDUCTION: Expressed abundantly in the early phase of the viral
CC replicative cycle, especially at early infection times.
CC {ECO:0000269|PubMed:11169113}.
CC -!- SIMILARITY: Belongs to the phi29likevirus gp16.7 family. {ECO:0000305}.
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DR EMBL; M14430; AAA88352.1; -; Genomic_DNA.
DR EMBL; EU771092; ACE96041.1; -; Genomic_DNA.
DR PIR; JN0033; JN0033.
DR RefSeq; YP_002004547.1; NC_011048.1.
DR PDB; 1ZAE; NMR; -; A/B=63-130.
DR PDB; 2BNK; X-ray; 2.90 A; A/B=64-130.
DR PDB; 2C5R; X-ray; 2.90 A; A/B/C/D/E/F=64-130.
DR PDBsum; 1ZAE; -.
DR PDBsum; 2BNK; -.
DR PDBsum; 2C5R; -.
DR SMR; P16517; -.
DR GeneID; 6446517; -.
DR KEGG; vg:6446517; -.
DR OrthoDB; 15728at10239; -.
DR EvolutionaryTrace; P16517; -.
DR Proteomes; UP000001207; Genome.
DR GO; GO:0033644; C:host cell membrane; IDA:UniProtKB.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0039693; P:viral DNA genome replication; IDA:UniProtKB.
DR Gene3D; 1.10.8.600; Phage phi29 replication organiser protein p16.7-like; 1.
DR InterPro; IPR009595; Phage_DNA_replic_GP16.7.
DR InterPro; IPR037211; Phage_DNA_replic_GP16.7_sf.
DR Pfam; PF06720; Phi-29_GP16_7; 1.
DR SUPFAM; SSF140713; Phage replication organizer domain; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; DNA replication; DNA-binding; Early protein;
KW Host cell membrane; Host membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Viral DNA replication.
FT CHAIN 1..130
FT /note="DNA replication protein 16.7"
FT /id="PRO_0000106613"
FT TRANSMEM 1..20
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:17426023"
FT REGION 70..130
FT /note="DNA-binding"
FT /evidence="ECO:0000269|PubMed:17426023"
FT COILED 30..60
FT /evidence="ECO:0000255, ECO:0000269|PubMed:17426023"
FT SITE 113
FT /note="Involved in dimerization"
FT /evidence="ECO:0000269|PubMed:17426023"
FT SITE 116
FT /note="Involved in dimerization"
FT /evidence="ECO:0000269|PubMed:17426023"
FT SITE 120
FT /note="Involved in oligomerization and DNA binding"
FT /evidence="ECO:0000269|PubMed:17426023"
FT MUTAGEN 116
FT /note="W->A: Loss of dimerization. Loss of DNA-binding
FT activity."
FT /evidence="ECO:0000269|PubMed:17426023"
FT MUTAGEN 120
FT /note="N->W: No effect on dimerization, but unable to form
FT higher order oligomers at elevated protein concentrations.
FT Loss of DNA-binding activity."
FT /evidence="ECO:0000269|PubMed:17426023"
FT HELIX 72..81
FT /evidence="ECO:0007829|PDB:2BNK"
FT HELIX 88..95
FT /evidence="ECO:0007829|PDB:2BNK"
FT HELIX 103..119
FT /evidence="ECO:0007829|PDB:2BNK"
SQ SEQUENCE 130 AA; 15185 MW; 38D2E3FE57C48951 CRC64;
MEAILMIGVL ALCVIFLLSG RNNKKKQEAR ELEDYLEDLN KRVVQRTQIL SELNEVISNR
SIDKTVNLSA CEVAVLDLYE QSNIRIPSDI IEDLVNQRLQ SEQEVLNYIE TQRTYWKLEN
QKKLYRGSLK
//
