Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

DNA-Binding protein G5P

Gene

V

Organism
Enterobacteria phage f1 (Bacteriophage f1)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Binds to DNA in a highly cooperative manner without pronounced sequence specificity. During synthesis of the single-stranded (progeny) viral DNA, prevents the conversion into the double-stranded replicative form. G5P is displaced by the capsid protein G8P during phage assembly on the inner bacterial membrane (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei16 – 161Involved in DNA binding
Sitei21 – 211Involved in DNA binding
Sitei26 – 261Involved in DNA binding
Sitei34 – 341Involved in DNA binding
Sitei41 – 411Involved in DNA binding, and in the dimer-dimer interactions of the protein-ssDNA complex
Sitei46 – 461Involved in DNA binding

GO - Molecular functioni

GO - Biological processi

  • rolling circle single-stranded viral DNA replication Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

DNA replication

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
DNA-Binding protein G5P
Short name:
G5P
Alternative name(s):
GPV
Single-stranded DNA-binding protein
Gene namesi
Name:V
OrganismiEnterobacteria phage f1 (Bacteriophage f1)
Taxonomic identifieri10863 [NCBI]
Taxonomic lineageiVirusesssDNA virusesInoviridaeInovirus
Virus hostiEscherichia coli [TaxID: 562]
Proteomesi
  • UP000002557 Componenti: Genome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 8787DNA-Binding protein G5PPRO_0000098195Add
BLAST

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

1
87
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 63Combined sources
Helixi8 – 103Combined sources
Beta strandi14 – 196Combined sources
Beta strandi21 – 233Combined sources
Beta strandi25 – 3511Combined sources
Beta strandi38 – 414Combined sources
Beta strandi43 – 486Combined sources
Beta strandi58 – 636Combined sources
Helixi65 – 673Combined sources
Beta strandi68 – 703Combined sources
Beta strandi74 – 807Combined sources
Beta strandi83 – 853Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AE2X-ray2.00A1-87[»]
1AE3X-ray2.00A1-86[»]
1GKHX-ray1.70A1-87[»]
1GPVmodel-A/B1-87[»]
1GVPX-ray1.60A1-87[»]
1VQAX-ray1.80A1-87[»]
1VQBX-ray1.80A1-87[»]
1VQCX-ray1.80A1-87[»]
1VQDX-ray1.82A1-87[»]
1VQEX-ray1.80A1-87[»]
1VQFX-ray1.80A1-87[»]
1VQGX-ray1.82A1-87[»]
1VQHX-ray1.80A1-87[»]
1VQIX-ray1.80A1-87[»]
1VQJX-ray1.80A1-87[»]
1YHAX-ray2.50A/B1-87[»]
1YHBX-ray2.20A1-87[»]
ProteinModelPortaliP69543.
SMRiP69543. Positions 1-87.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP69543.

Family & Domainsi

Sequence similaritiesi

Belongs to the inovirus G5P protein family.Curated

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
InterProiIPR012340. NA-bd_OB-fold.
IPR003512. Phage_M13_G5P_DNA-bd.
[Graphical view]
PfamiPF02303. Phage_DNA_bind. 1 hit.
[Graphical view]
ProDomiPD015272. Phage_DNA_bind. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF50249. SSF50249. 1 hit.

Sequencei

Sequence statusi: Complete.

P69543-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIKVEIKPSQ AQFTTRSGVS RQGKPYSLNE QLCYVDLGNE YPVLVKITLD
60 70 80
EGQPAYAPGL YTVHLSSFKV GQFGSLMIDR LRLVPAK
Length:87
Mass (Da):9,688
Last modified:July 21, 1986 - v1
Checksum:i2FAD178DDC248CF0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00606 Genomic DNA. Translation: CAA23868.1.
J02448 Genomic DNA. Translation: AAA32211.1.
M10677 Genomic DNA. Translation: AAA32226.1.
PIRiE04271. DDBPF1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00606 Genomic DNA. Translation: CAA23868.1.
J02448 Genomic DNA. Translation: AAA32211.1.
M10677 Genomic DNA. Translation: AAA32226.1.
PIRiE04271. DDBPF1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AE2X-ray2.00A1-87[»]
1AE3X-ray2.00A1-86[»]
1GKHX-ray1.70A1-87[»]
1GPVmodel-A/B1-87[»]
1GVPX-ray1.60A1-87[»]
1VQAX-ray1.80A1-87[»]
1VQBX-ray1.80A1-87[»]
1VQCX-ray1.80A1-87[»]
1VQDX-ray1.82A1-87[»]
1VQEX-ray1.80A1-87[»]
1VQFX-ray1.80A1-87[»]
1VQGX-ray1.82A1-87[»]
1VQHX-ray1.80A1-87[»]
1VQIX-ray1.80A1-87[»]
1VQJX-ray1.80A1-87[»]
1YHAX-ray2.50A/B1-87[»]
1YHBX-ray2.20A1-87[»]
ProteinModelPortaliP69543.
SMRiP69543. Positions 1-87.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP69543.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
InterProiIPR012340. NA-bd_OB-fold.
IPR003512. Phage_M13_G5P_DNA-bd.
[Graphical view]
PfamiPF02303. Phage_DNA_bind. 1 hit.
[Graphical view]
ProDomiPD015272. Phage_DNA_bind. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF50249. SSF50249. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Nucleotide sequence and genome organisation of filamentous bacteriophages f1 and fd."
    Beck E., Zink B.
    Gene 16:35-58(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Nucleotide sequences in bacteriophage f1 DNA: nucleotide sequence of genes V, VII, and VIII."
    Hill D.F., Petersen G.B.
    J. Virol. 34:40-50(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Nucleotide sequence of bacteriophage f1 DNA."
    Hill D.F., Petersen G.B.
    J. Virol. 44:32-46(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Nucleotide sequence of the recognition site for the restriction-modification enzyme of Escherichia coli B."
    Ravetch J.V., Horiuchi K., Zinder N.D.
    Proc. Natl. Acad. Sci. U.S.A. 75:2266-2270(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 13-57.
  5. "Structure of the gene V protein of bacteriophage f1 determined by multiwavelength X-ray diffraction on the selenomethionyl protein."
    Skinner M.M., Zhang H., Leschnitzer D.H., Guan Y., Bellamy H., Sweet R.M., Gray C.W., Konings R.N.H., Wang A.H.-J., Terwilliger T.C.
    Proc. Natl. Acad. Sci. U.S.A. 91:2071-2075(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
  6. "Crystal structures of Y41H and Y41F mutants of gene V protein from Ff phage suggest possible protein-protein interactions in the GVP-ssDNA complex."
    Guan Y., Zhang H., Konings R.N., Hilbers C.W., Terwilliger T.C., Wang A.H.
    Biochemistry 33:7768-7778(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF MUTANTS HIS-41 AND PHE-41.
  7. "Context dependence of mutational effects in a protein: the crystal structures of the V35I, I47V and V35I/I47V gene V protein core mutants."
    Zhang H., Skinner M.M., Sandberg W.S., Wang A.H.-J., Terwilliger T.C.
    J. Mol. Biol. 259:148-159(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANTS ILE-35 AND VAL-47.

Entry informationi

Entry nameiG5P_BPF1
AccessioniPrimary (citable) accession number: P69543
Secondary accession number(s): P03669
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: April 13, 2016
This is version 58 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

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.