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BPT5:FIBL1

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Species (Taxon ID) Escherichia phage T5 (Enterobacteria phage T5). (10726)
Gene Name(s) ltf (ECO:0000305)
Protein Name(s) L-shaped tail fiber protein pb1 (ECO:0000303 with PMID:24198424[1])

LTF Tail protein pb1 (ECO:0000303 with PMID:24198424[1])

External Links
UniProt P13390
EMBL AY543070
AY692264
AY587007
AM084272
PIR S01982
S65934
RefSeq YP_006961.1
PDB 4UW7
4UW8
5AQ5
PDBsum 4UW7
4UW8
5AQ5
GeneID 2777639
KEGG vg:2777639
Proteomes UP000002107
UP000002141
UP000002503
GO GO:0019012
GO:0046718
GO:0019062
InterPro IPR030392
PROSITE PS51688

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0098024

virus tail, fiber

PMID:26805872[2]

ECO:0000315

C

. In these two bacteriophages, LTF function is essential to penetrate the shield of the host’s O-antigens. We also demonstrate that LTF-mediated adsorption becomes superfluous when the non-specific cell protection by O-antigen is missing, allowing the phages to bind directly to their common secondary receptor, the outer membrane protein BtuB.

figure 4. The similarity of the a.a. sequence regions in LTFs of T5-like phages with other viruses are indicated by similar colors.

complete
CACAO 11993

GO:0039638

lipopolysaccharide-mediated virion attachment to host cell

PMID:7045389[3]

ECO:0000315

P

As shown in Figure 1, the L-shaped tail fibers in T5 increase the absorption rate by reversibly binding to LPS on the host. The figure shows mutant hosts with more available O-antigens increase the absorption rate of T5 phage into the host.

complete
CACAO 12043

involved_in

GO:0039638

lipopolysaccharide-mediated virion attachment to host cell

PMID:7045389[3]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0098024

virus tail, fiber

PMID:24198424[1]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0098024

virus tail, fiber

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1230

C

Seeded From UniProt

complete

enables

GO:0016787

hydrolase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0378

F

Seeded From UniProt

complete

enables

GO:0008236

serine-type peptidase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0720

F

Seeded From UniProt

complete

involved_in

GO:0019062

virion attachment to host cell

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1161

P

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

involved_in

GO:0098671

adhesion receptor-mediated virion attachment to host cell

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1233

P

Seeded From UniProt

complete

part_of

GO:0098015

virus tail

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1227

C

Seeded From UniProt

complete

involved_in

GO:0046718

viral entry into host cell

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1160

P

Seeded From UniProt

complete

involved_in

GO:0016032

viral process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0945

P

Seeded From UniProt

complete

enables

GO:0008233

peptidase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0645

F

Seeded From UniProt

complete

involved_in

GO:0006508

proteolysis

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0645

P

Seeded From UniProt

complete

Notes

References

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

  1. 1.0 1.1 1.2 Zivanovic, Y et al. (2014) Insights into bacteriophage T5 structure from analysis of its morphogenesis genes and protein components. J. Virol. 88 1162-74 PubMed GONUTS page
  2. Golomidova, AK et al. (2016) Branched Lateral Tail Fiber Organization in T5-Like Bacteriophages DT57C and DT571/2 is Revealed by Genetic and Functional Analysis. Viruses 8 PubMed GONUTS page
  3. 3.0 3.1 Heller, K & Braun, V (1982) Polymannose O-antigens of Escherichia coli, the binding sites for the reversible adsorption of bacteriophage T5+ via the L-shaped tail fibers. J. Virol. 41 222-7 PubMed GONUTS page