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BPHK7:CAPSD

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Species (Taxon ID) Enterobacteria phage HK97 (Bacteriophage HK97). (37554)
Gene Name(s) 5
Protein Name(s) Major capsid protein (ECO:0000303 with PMID:17098191[1])

Gene product 5 (ECO:0000305) gp5 (ECO:0000305) Major head protein (ECO:0000303 with PMID:7723019[2]) Scaffolding domain delta

External Links
UniProt P49861
EMBL U18319
AF069529
PIR S54392
RefSeq NP_037701.1
PDB 1IF0
1OHG
2FRP
2FS3
2FSY
2FT1
2FTE
2GP1
3DDX
3E8K
3J1A
3QPR
PDBsum 1IF0
1OHG
2FRP
2FS3
2FSY
2FT1
2FTE
2GP1
3DDX
3E8K
3J1A
3QPR
ProteinModelPortal P49861
SMR P49861
DIP DIP-29163N
GeneID 1262530
KEGG vg:1262530
EvolutionaryTrace P49861
PMAP-CutDB P49861
Proteomes UP000002576
GO GO:0039620
GO:0019076
InterPro IPR006444
IPR024455
Pfam PF05065
TIGRFAMs TIGR01554

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0046797

viral procapsid maturation

PMID:24889236[3]

ECO:0000315

P

HK97 delta domain is necessary for proper procapsid assembly. HK97 delta domain comprises the first 102 amino acids of the major capsid protein, is present during procapsid assembly, and is cleaved during capsid maturation. In Figure 2A, HK97 lacking the delta domain was found to have become insoluble. Figure 2B shows similar results, with delta-less HK97 present only in the pellet fraction (as marked by a circle). Figure 2C shows expression of a full-length HK97 protein plasmid (protease-) and delta-less HK97. Full-length HK97 is shown to properly form capsomers and proheads—signs of proper assembly— while the lack of bands for the delta-less HK97 show there is no formation of capsomers or proheads. From this, we can conclude that the delta-domain of HK97 is necessary for formation of a properly folded, soluble procapsid head.

complete
CACAO 13109

part_of

GO:0019028

viral capsid

PMID:11000116[4]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:24361271[5]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P49861

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:22748764[6]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P49861

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:19204733[7]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P49861

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:18940605[8]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P49861

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:17098191[1]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P49861

F

Seeded From UniProt

complete

part_of

GO:0019028

viral capsid

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0167

C

Seeded From UniProt

complete

part_of

GO:0039620

T=7 icosahedral viral capsid

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1145

C

Seeded From UniProt

complete

part_of

GO:0019012

virion

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0946
UniProtKB-SubCell:SL-0274

C

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 1.0 1.1 Gan, L et al. (2006) Capsid conformational sampling in HK97 maturation visualized by X-ray crystallography and cryo-EM. Structure 14 1655-65 PubMed GONUTS page
  2. Duda, RL et al. (1995) Structural transitions during bacteriophage HK97 head assembly. J. Mol. Biol. 247 618-35 PubMed GONUTS page
  3. Oh, B et al. (2014) The delta domain of the HK97 major capsid protein is essential for assembly. Virology 456-457 171-8 PubMed GONUTS page
  4. Wikoff, WR et al. (2000) Topologically linked protein rings in the bacteriophage HK97 capsid. Science 289 2129-33 PubMed GONUTS page
  5. Veesler, D et al. (2014) Architecture of a dsDNA viral capsid in complex with its maturation protease. Structure 22 230-7 PubMed GONUTS page
  6. Veesler, D et al. (2012) Maturation in action: CryoEM study of a viral capsid caught during expansion. Structure 20 1384-90 PubMed GONUTS page
  7. Gertsman, I et al. (2009) An unexpected twist in viral capsid maturation. Nature 458 646-50 PubMed GONUTS page
  8. Lee, KK et al. (2008) Virus capsid expansion driven by the capture of mobile surface loops. Structure 16 1491-502 PubMed GONUTS page