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Protein

DNA replication protein 16.7

Gene

16.7

Organism
Bacillus phage phi29 (Bacteriophage phi-29)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Binds to the long stretches of ssDNA of the viral DNA replication intermediates created during the protein-primed mechanism of replication of the viral genome and attaches the viral DNA to the membrane of the infected cells (PubMed:11741949) (PubMed:11169113). Required for the redistribution of replicating viral DNA from the initial replication site to membrane-associated sites surrounding the nucleoid (PubMed:10921898). Required for the second pull step of DNA ejection (PubMed:17526715).4 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei113 – 1131Involved in dimerization1 Publication
Sitei116 – 1161Involved in dimerization1 Publication
Sitei120 – 1201Involved in oligomerization and DNA binding1 Publication

GO - Molecular functioni

GO - Biological processi

  • viral DNA genome replication Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

DNA replication, Viral DNA replication

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
DNA replication protein 16.7
Alternative name(s):
Gene product 16.7
Short name:
gp16.7
Protein p16.7
Gene namesi
Name:16.7
OrganismiBacillus phage phi29 (Bacteriophage phi-29)
Taxonomic identifieri10756 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageCaudoviralesPodoviridaePicovirinaePhi29likevirus
Virus hostiBacillus subtilis [TaxID: 1423]
Proteomesi
  • UP000001207 Componenti: Genome

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei1 – 2020HelicalSequence analysis1 PublicationAdd
BLAST

GO - Cellular componenti

  • host cell membrane Source: UniProtKB
  • host cell plasma membrane Source: UniProtKB-KW
  • integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Host cell membrane, Host membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi116 – 1161W → A: Loss of dimerization. Loss of DNA-binding activity. 1 Publication
Mutagenesisi120 – 1201N → W: No effect on dimerization, but unable to form higher order oligomers at elevated protein concentrations. Loss of DNA-binding activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 130130DNA replication protein 16.7PRO_0000106613Add
BLAST

Expressioni

Inductioni

Expressed abundantly in the early phase of the viral replicative cycle, especially at early infection times.1 Publication

Keywords - Developmental stagei

Early protein

Interactioni

Subunit structurei

Homodimer (PubMed:11169113, PubMed:17426023) (PubMed:15772069); homooligomer (PubMed:17426023). Interacts with DNA; one dsDNA binding subunit is constituted by three p16.7. dimers (PubMed:16275651, PubMed:17426023).4 Publications

Structurei

Secondary structure

1
130
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi72 – 8110Combined sources
Helixi88 – 958Combined sources
Helixi103 – 11917Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZAENMR-A/B63-130[»]
2BNKX-ray2.90A/B64-130[»]
2C5RX-ray2.90A/B/C/D/E/F64-130[»]
ProteinModelPortaliP16517.
SMRiP16517. Positions 66-129.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP16517.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni70 – 13061DNA-binding1 PublicationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili30 – 6031Sequence analysis1 PublicationAdd
BLAST

Sequence similaritiesi

Belongs to the phi29likevirus gp16.7 family.Curated

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Family and domain databases

InterProiIPR009595. Phage_DNA_replic_GP16.7.
[Graphical view]
PfamiPF06720. Phi-29_GP16_7. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P16517-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEAILMIGVL ALCVIFLLSG RNNKKKQEAR ELEDYLEDLN KRVVQRTQIL
60 70 80 90 100
SELNEVISNR SIDKTVNLSA CEVAVLDLYE QSNIRIPSDI IEDLVNQRLQ
110 120 130
SEQEVLNYIE TQRTYWKLEN QKKLYRGSLK
Length:130
Mass (Da):15,185
Last modified:August 1, 1990 - v1
Checksum:i38D2E3FE57C48951
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14430 Genomic DNA. Translation: AAA88352.1.
EU771092 Genomic DNA. Translation: ACE96041.1.
PIRiJN0033.
RefSeqiYP_002004547.1. NC_011048.1.

Genome annotation databases

GeneIDi6446517.
KEGGivg:6446517.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14430 Genomic DNA. Translation: AAA88352.1.
EU771092 Genomic DNA. Translation: ACE96041.1.
PIRiJN0033.
RefSeqiYP_002004547.1. NC_011048.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZAENMR-A/B63-130[»]
2BNKX-ray2.90A/B64-130[»]
2C5RX-ray2.90A/B/C/D/E/F64-130[»]
ProteinModelPortaliP16517.
SMRiP16517. Positions 66-129.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi6446517.
KEGGivg:6446517.

Miscellaneous databases

EvolutionaryTraceiP16517.

Family and domain databases

InterProiIPR009595. Phage_DNA_replic_GP16.7.
[Graphical view]
PfamiPF06720. Phi-29_GP16_7. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The complete sequence of the Bacillus phage phi 29 right early region."
    Garvey K.J., Yoshikawa H., Ito J.
    Gene 40:301-309(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Villegas A.P., Lingohr E.J., Ceyssens P.-J., Kropinski A.M.
    Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Dynamic relocalization of phage phi 29 DNA during replication and the role of the viral protein p16.7."
    Meijer W.J., Lewis P.J., Errington J., Salas M.
    EMBO J. 19:4182-4190(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  4. "Characterization of the bacteriophage phi29-encoded protein p16.7: a membrane protein involved in phage DNA replication."
    Meijer W.J., Serna-Rico A., Salas M.
    Mol. Microbiol. 39:731-746(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, INDUCTION, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT.
  5. "The Bacillus subtilis phage phi 29 protein p16.7, involved in phi 29 DNA replication, is a membrane-localized single-stranded DNA-binding protein."
    Serna-Rico A., Salas M., Meijer W.J.
    J. Biol. Chem. 277:6733-6742(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: DNA-BINDING, FUNCTION.
  6. "The phage phi29 membrane protein p16.7, involved in DNA replication, is required for efficient ejection of the viral genome."
    Alcorlo M., Gonzalez-Huici V., Hermoso J.M., Meijer W.J., Salas M.
    J. Bacteriol. 189:5542-5549(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Structural and functional analysis of phi29 p16.7C dimerization mutants: identification of a novel aromatic cage dimerization motif."
    Munoz-Espin D., Fuertes M.A., Jimenez M., Villar L., Alonso C., Rivas G., Salas M., Meijer W.J.
    J. Biol. Chem. 282:16521-16531(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, DNA-BINDING, MUTAGENESIS OF TRP-116 AND ASN-120.
  8. "Structure of the functional domain of phi29 replication organizer: insights into oligomerization and dna binding."
    Asensio J.L., Albert A., Munoz-Espin D., Gonzalez C., Hermoso J., Villar L., Jimenez-Barbero J., Salas M., Meijer W.J.
    J. Biol. Chem. 280:20730-20739(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 63-130, SUBUNIT.
  9. "Structural basis for membrane anchorage of viral phi29 DNA during replication."
    Albert A., Munoz-Espin D., Jimenez M., Asensio J.L., Hermoso J.A., Salas M., Meijer W.J.
    J. Biol. Chem. 280:42486-42488(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 64-130 IN COMPLEX WITH DNA, DNA-BINDING.

Entry informationi

Entry nameiGP167_BPPH2
AccessioniPrimary (citable) accession number: P16517
Secondary accession number(s): B3VMQ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: June 8, 2016
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.