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P17313 (VG31_BPT4) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Capsid assembly protein Gp31
Gene names
Name:31
OrganismEnterobacteria phage T4 (Bacteriophage T4) [Reference proteome]
Taxonomic identifier10665 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageCaudoviralesMyoviridaeTevenvirinaeT4likevirus
Virus hostEscherichia coli [TaxID: 562]

Protein attributes

Sequence length111 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.7

Subunit structure

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

Ontologies

Keywords
   Biological processViral capsid assembly
Virus exit from host cell
   Developmental stageEarly protein
   Molecular functionChaperone
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processprotein folding

Inferred from electronic annotation. Source: InterPro

viral capsid assembly

Inferred from direct assay PubMed 416025. Source: CACAO

viral release from host cell

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 111111Capsid assembly protein Gp31
PRO_0000165018

Secondary structure

.................... 111
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P17313 [UniParc].

Last modified August 1, 1990. Version 1.
Checksum: D4F75212CB849EFD

FASTA11112,079
        10         20         30         40         50         60 
MSEVQQLPIR AVGEYVILVS EPAQAGDEEV TESGLIIGKR VQGEVPELCV VHSVGPDVPE 

        70         80         90        100        110 
GFCEVGDLTS LPVGQIRNVP HPFVALGLKQ PKEIKQKFVT CHYKAIPCLY K 

« Hide

References

« Hide 'large scale' references
[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(1990) [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(1988) [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(1990) [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(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"Bacteriophage T4 genome."
Miller E.S., Kutter E., Mosig G., Arisaka F., Kunisawa T., Ruger W.
Microbiol. Mol. Biol. Rev. 67:86-156(2003) [PubMed] [Europe PMC] [Abstract]
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(1990) [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(1994) [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(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRVHBPP4. JT0488.
RefSeqNP_049825.1. NC_000866.4.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1G31X-ray2.30A/B/C/D/E/F/G1-111[»]
2CGTelectron microscopy8.20O/P/Q/R/S/T/U1-111[»]
ProteinModelPortalP17313.
SMRP17313. Positions 5-111.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-59724N.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1258757.

Family and domain databases

Gene3D2.30.33.40. 1 hit.
InterProIPR020818. Chaperonin_Cpn10.
IPR011032. GroES-like.
IPR016416. Phage_T4_Gp31_GroEL.
[Graphical view]
PfamPF00166. Cpn10. 1 hit.
[Graphical view]
PIRSFPIRSF004380. Phage_GroES_Gp31. 1 hit.
SUPFAMSSF50129. SSF50129. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP17313.

Entry information

Entry nameVG31_BPT4
AccessionPrimary (citable) accession number: P17313
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: July 9, 2014
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references