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BPT5:TMP

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Species (Taxon ID) Escherichia phage T5 (Enterobacteria phage T5). (10726)
Gene Name(s) D18-19 (ECO:0000312 with EMBL:AAQ92756.2)
Protein Name(s) Probable tape measure protein (ECO:0000303 with PMID:18348984[1])

Tail protein pb2 (ECO:0000303 with PMID:24198424[2])

External Links
UniProt Q6QGE7
EMBL AY543070
AY692264
AY587007
RefSeq YP_006968.1
ProteinModelPortal Q6QGE7
SMR Q6QGE7
GeneID 2777629
KEGG vg:2777629
OrthoDB VOG0900000A
Proteomes UP000002107
UP000002141
UP000002503
GO GO:0098015
GO:0003824
GO:0019835
GO:0042742
GO:0098932
GO:0085027
GO:0008152
GO:0044694
GO:0099001
GO:0098003

Annotations

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

part_of

GO:0098015

virus tail

PMID:24198424[2]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

GO:0061783

peptidoglycan muralytic activity

PMID:18348984[1]

ECO:0000314

F

According to the paper the protein specifically the C terminus end is involved in the degradation of peptidoglycan . The protein has peptidoglycan hydrolase activity. When mixed with peptidoglycan it was shown to give products and degrade peptidoglycan using it as a substrate. Figure six shows the hydrolytic capability of the protein by comparing it to sonicated ( sonication is a method used to disrupt cell membranes) cells. With the PB2-Cterm we can see that the B galactosidase coming out from the bacteria reached a level 60 percent to that of sonicated cells. Which is further proof of peptidoglycan hyrolysis. The control designed for this part was only adding DDM which didn't end up causing any B galactosidase to come out of the bacteria.

complete
CACAO 13184

involved_in

GO:0085027

entry into host via enzymatic degradation of host anatomical structure

PMID:18348984[1]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0098003

viral tail assembly

PMID:18348984[1]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0008152

metabolic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0081

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:0042742

defense response to bacterium

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0081

P

Seeded From UniProt

complete

involved_in

GO:0098932

disruption by virus of host cell wall peptidoglycan during virus entry

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1236

P

Seeded From UniProt

complete

involved_in

GO:0046718

viral entry into host cell

GO_REF:0000037
GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1160
UniProtKB-KW:KW-1162

P

Seeded From UniProt

complete

involved_in

GO:0098003

viral tail assembly

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1245

P

Seeded From UniProt

complete

involved_in

GO:0099001

viral genome ejection through host cell envelope, long flexible tail mechanism

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1243

P

Seeded From UniProt

complete

involved_in

GO:0019835

cytolysis

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0081

P

Seeded From UniProt

complete

enables

GO:0003824

catalytic activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0081

F

Seeded From UniProt

complete

involved_in

GO:0098994

disruption of host cell envelope during viral entry

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1235

P

Seeded From UniProt

complete

involved_in

GO:0044694

pore-mediated entry of viral genome into host cell

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1172

P

Seeded From UniProt

complete

Notes

References

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

  1. 1.0 1.1 1.2 1.3 Boulanger, P et al. (2008) Phage T5 straight tail fiber is a multifunctional protein acting as a tape measure and carrying fusogenic and muralytic activities. J. Biol. Chem. 283 13556-64 PubMed GONUTS page
  2. 2.0 2.1 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