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Protein

Capsid assembly protein Gp31

Gene

31

Organism
Enterobacteria phage T4 (Bacteriophage T4)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Essential for proper capsid assembly. In absence of Gp31 the major capsid protein (Gp23) assembles into 'lumps'. Acts as a co-chaperonin with the host groEL protein.1 Publication

GO - Biological processi

  1. protein folding Source: InterPro
  2. viral capsid assembly Source: CACAO
  3. viral release from host cell Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Viral capsid assembly, Virus exit from host cell

Names & Taxonomyi

Protein namesi
Recommended name:
Capsid assembly protein Gp31
Gene namesi
Name:31
OrganismiEnterobacteria phage T4 (Bacteriophage T4)
Taxonomic identifieri10665 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageCaudoviralesMyoviridaeTevenvirinaeT4likevirus
Virus hostiEscherichia coli [TaxID: 562]
ProteomesiUP000009087 Componenti: Genome

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 111111Capsid assembly protein Gp31PRO_0000165018Add
BLAST

Expressioni

Keywords - Developmental stagei

Early protein

Interactioni

Subunit structurei

Homoheptamer. Forms a stable complex with groEL in the presence of ATP.

Protein-protein interaction databases

DIPiDIP-59724N.

Structurei

Secondary structure

1
111
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi15 – 206Combined sources
Helixi25 – 273Combined sources
Helixi39 – 446Combined sources
Beta strandi45 – 5410Combined sources
Beta strandi68 – 725Combined sources
Helixi73 – 753Combined sources
Beta strandi77 – 793Combined sources
Helixi82 – 854Combined sources
Helixi91 – 933Combined sources
Beta strandi98 – 1025Combined sources
Helixi103 – 1053Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1G31X-ray2.30A/B/C/D/E/F/G1-111[»]
2CGTelectron microscopy8.20O/P/Q/R/S/T/U1-111[»]
SMRiP17313. Positions 5-111.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP17313.

Family & Domainsi

Family and domain databases

Gene3Di2.30.33.40. 1 hit.
InterProiIPR020818. Chaperonin_Cpn10.
IPR011032. GroES-like.
IPR016416. Phage_T4_Gp31_GroEL.
[Graphical view]
PfamiPF00166. Cpn10. 1 hit.
[Graphical view]
PIRSFiPIRSF004380. Phage_GroES_Gp31. 1 hit.
SUPFAMiSSF50129. SSF50129. 1 hit.

Sequencei

Sequence statusi: Complete.

P17313-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEVQQLPIR AVGEYVILVS EPAQAGDEEV TESGLIIGKR VQGEVPELCV
60 70 80 90 100
VHSVGPDVPE GFCEVGDLTS LPVGQIRNVP HPFVALGLKQ PKEIKQKFVT
110
CHYKAIPCLY K
Length:111
Mass (Da):12,079
Last modified:August 1, 1990 - v1
Checksum:iD4F75212CB849EFD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X17657 Genomic DNA. Translation: CAA35651.1.
M37882 Genomic DNA. Translation: AAA32506.1.
X54536 Genomic DNA. Translation: CAA38405.1.
M34502 Genomic DNA. Translation: AAA32510.1.
AF158101 Genomic DNA. Translation: AAD42451.1.
PIRiJT0488. VHBPP4.
RefSeqiNP_049825.1. NC_000866.4.

Genome annotation databases

GeneIDi1258757.
KEGGivg:1258757.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X17657 Genomic DNA. Translation: CAA35651.1.
M37882 Genomic DNA. Translation: AAA32506.1.
X54536 Genomic DNA. Translation: CAA38405.1.
M34502 Genomic DNA. Translation: AAA32510.1.
AF158101 Genomic DNA. Translation: AAD42451.1.
PIRiJT0488. VHBPP4.
RefSeqiNP_049825.1. NC_000866.4.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1G31X-ray2.30A/B/C/D/E/F/G1-111[»]
2CGTelectron microscopy8.20O/P/Q/R/S/T/U1-111[»]
SMRiP17313. Positions 5-111.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-59724N.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi1258757.
KEGGivg:1258757.

Miscellaneous databases

EvolutionaryTraceiP17313.

Family and domain databases

Gene3Di2.30.33.40. 1 hit.
InterProiIPR020818. Chaperonin_Cpn10.
IPR011032. GroES-like.
IPR016416. Phage_T4_Gp31_GroEL.
[Graphical view]
PfamiPF00166. Cpn10. 1 hit.
[Graphical view]
PIRSFiPIRSF004380. Phage_GroES_Gp31. 1 hit.
SUPFAMiSSF50129. SSF50129. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and sequencing of bacteriophage T4 genes between map positions 128.3-130.3."
    Prilipov A.G., Mesyanzhinov V.V., Aebi U., Kellenberger E.
    Nucleic Acids Res. 18:3635-3635(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: D.
  2. "Cloning, sequence, and expression of the temperature-dependent phage T4 capsid assembly gene 31."
    Nivinskas R., Black L.W.
    Gene 73:251-257(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Nucleotide sequence of bacteriophage T4 gene 31 region."
    Raudonikiene A., Nivinskas R.
    Nucleic Acids Res. 18:4280-4280(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Gene rIII is the nearest downstream neighbour of bacteriophage T4 gene 31."
    Raudonikiene A., Nivinskas R.
    Gene 114:85-90(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "Mutational analysis of the phage T4 morphogenetic 31 gene, whose product interacts with the Escherichia coli GroEL protein."
    Keppel F., Lipinska B., Ang D., Georgopoulos C.
    Gene 86:19-25(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS.
  7. "Bacteriophage T4 encodes a co-chaperonin that can substitute for Escherichia coli GroES in protein folding."
    van der Vies S.M., Gatenby A.A., Georgopoulos C.
    Nature 368:654-656(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Structural adaptations in the specialized bacteriophage T4 co-chaperonin Gp31 expand the size of the Anfinsen cage."
    Hunt J.F., van der Vies S.M., Henry L., Deisenhofer J.
    Cell 90:361-371(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).

Entry informationi

Entry nameiVG31_BPT4
AccessioniPrimary (citable) accession number: P17313
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: April 1, 2015
This is version 97 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

External Data

Dasty 3

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 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.