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Protein

Uracil-DNA glycosylase inhibitor

Gene

UGI

Organism
Bacillus phage PBS2 (Bacteriophage PBS2)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

This protein binds specifically and reversibly to the host uracil-DNA glycosylase, preventing removal of uracil residues from PBS2 DNA by the host uracil-excision repair system.

Enzyme and pathway databases

SABIO-RKP14739.

Names & Taxonomyi

Protein namesi
Recommended name:
Uracil-DNA glycosylase inhibitor
Gene namesi
Name:UGI
OrganismiBacillus phage PBS2 (Bacteriophage PBS2)
Taxonomic identifieri10684 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageCaudoviralesMyoviridae
Virus hostiBacillus subtilis [TaxID: 1423]

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 8484Uracil-DNA glycosylase inhibitorPRO_0000065722Add
BLAST

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
ungP122954EBI-1025973,EBI-559403From a different organism.

Protein-protein interaction databases

IntActiP14739. 2 interactions.
MINTiMINT-1506611.

Structurei

Secondary structure

1
84
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1210Combined sources
Beta strandi22 – 243Combined sources
Helixi26 – 338Combined sources
Beta strandi41 – 488Combined sources
Turni49 – 524Combined sources
Beta strandi53 – 608Combined sources
Turni62 – 643Combined sources
Beta strandi67 – 737Combined sources
Beta strandi79 – 835Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EUIX-ray3.20C/D1-84[»]
1LQGX-ray2.90C/D1-84[»]
1LQMX-ray3.20B/D/F/H1-84[»]
1UDIX-ray2.70I2-84[»]
1UGHX-ray1.90I3-84[»]
1UGIX-ray1.55A/B/C/D/E/F/G/H1-84[»]
1UUGX-ray2.40B/D1-84[»]
2J8XX-ray2.30B/D1-84[»]
2UGIX-ray2.20A/B1-84[»]
2UUGX-ray2.60C/D1-84[»]
2ZHXX-ray3.10B/D/F/H/J/L/N1-84[»]
4LYLX-ray1.93B/D/F/H/J/L/N/P1-84[»]
ProteinModelPortaliP14739.
SMRiP14739. Positions 1-84.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14739.

Family & Domainsi

Family and domain databases

Gene3Di3.10.450.20. 1 hit.
InterProiIPR024062. Phage_PBS2_Ugi.
[Graphical view]
SUPFAMiSSF54441. SSF54441. 1 hit.

Sequencei

Sequence statusi: Complete.

P14739-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTNLSDIIEK ETGKQLVIQE SILMLPEEVE EVIGNKPESD ILVHTAYDES
60 70 80
TDENVMLLTS DAPEYKPWAL VIQDSNGENK IKML
Length:84
Mass (Da):9,476
Last modified:April 1, 1990 - v1
Checksum:iC07DCF9DB101BC2A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04434 Genomic DNA. Translation: AAA91582.1.
PIRiA32206. QIBPS2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04434 Genomic DNA. Translation: AAA91582.1.
PIRiA32206. QIBPS2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EUIX-ray3.20C/D1-84[»]
1LQGX-ray2.90C/D1-84[»]
1LQMX-ray3.20B/D/F/H1-84[»]
1UDIX-ray2.70I2-84[»]
1UGHX-ray1.90I3-84[»]
1UGIX-ray1.55A/B/C/D/E/F/G/H1-84[»]
1UUGX-ray2.40B/D1-84[»]
2J8XX-ray2.30B/D1-84[»]
2UGIX-ray2.20A/B1-84[»]
2UUGX-ray2.60C/D1-84[»]
2ZHXX-ray3.10B/D/F/H/J/L/N1-84[»]
4LYLX-ray1.93B/D/F/H/J/L/N/P1-84[»]
ProteinModelPortaliP14739.
SMRiP14739. Positions 1-84.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP14739. 2 interactions.
MINTiMINT-1506611.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP14739.

Miscellaneous databases

EvolutionaryTraceiP14739.

Family and domain databases

Gene3Di3.10.450.20. 1 hit.
InterProiIPR024062. Phage_PBS2_Ugi.
[Graphical view]
SUPFAMiSSF54441. SSF54441. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Uracil-DNA glycosylase inhibitor gene of bacteriophage PBS2 encodes a binding protein specific for uracil-DNA glycosylase."
    Wang Z., Mosbaugh D.W.
    J. Biol. Chem. 264:1163-1171(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-5.
  2. "Site-directed mutagenesis and characterization of uracil-DNA glycosylase inhibitor protein. Role of specific carboxylic amino acids in complex formation with Escherichia coli uracil-DNA glycosylase."
    Lundquist A.J., Beger R.D., Bennett S.E., Bolton P.H., Mosbaugh D.W.
    J. Biol. Chem. 272:21408-21419(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  3. "X-ray analysis of a complex of Escherichia coli uracil DNA glycosylase (EcUDG) with a proteinaceous inhibitor. The structure elucidation of a prokaryotic UDG."
    Ravishankar R., Sagar M.B., Roy S., Purnapatre K., Handa P., Varshney U., Vijayan M.
    Nucleic Acids Res. 26:4880-4887(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS).
  4. "Protein mimicry of DNA from crystal structures of the uracil-DNA glycosylase inhibitor protein and its complex with Escherichia coli uracil-DNA glycosylase."
    Putnam C.D., Shroyer M.J.N., Lundquist A.J., Mol C.D., Arvai A.S., Mosbaugh D.W., Tainer J.A.
    J. Mol. Biol. 287:331-346(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS).

Entry informationi

Entry nameiUNGI_BPPB2
AccessioniPrimary (citable) accession number: P14739
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: May 11, 2016
This is version 66 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, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

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.