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BPSFV:FIBER

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Species (Taxon ID) Shigella phage Sf6 (Shigella flexneri bacteriophage VI) (BacteriophageSfVI). (10761)
Gene Name(s) No Information Provided.
Protein Name(s) Tail spike protein (ECO:0000305)

TSP Endo-1,3-alpha-L-rhamnosidase (ECO:0000305) Endorhamnosidase (ECO:0000305)

External Links
UniProt Q9XJP3
EMBL AF128887
PDB 2VBE
2VBK
2VBM
4URR
PDBsum 2VBE
2VBK
2VBM
4URR
ProteinModelPortal Q9XJP3
SMR Q9XJP3
DIP DIP-29798N
EvolutionaryTrace Q9XJP3
GO GO:0098024
GO:0052775
GO:0098995
GO:0085027
GO:0008152
GO:0009405
GO:0019062
Gene3D 2.160.20.10
2.170.14.10
InterPro IPR009093
IPR036730
IPR024535
IPR012334
IPR011050
Pfam PF09008
PF12708
SUPFAM SSF51126
SSF51327

Annotations

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

involved_in

GO:0085027

entry into host via enzymatic degradation of host anatomical structure

PMID:6284[1]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0019062

virion attachment to host cell

PMID:18462681[2]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0098024

virus tail, fiber

PMID:18462681[2]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0052775

endo-1,3-alpha-L-rhamnosidase activity

PMID:12424253[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0009405

pathogenesis

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR009093
InterPro:IPR036730

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: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: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: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

enables

GO:0016798

hydrolase activity, acting on glycosyl bonds

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0326

F

Seeded From UniProt

complete

involved_in

GO:0098995

disruption by virus of host envelope lipopolysaccharide during virus entry

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1237

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-0326

P

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

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

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

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

Notes

References

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

  1. Iwashita, S & Kanegasaki, S (1976) Enzymic and molecular properties of base-plate parts of bacteriophage P22. Eur. J. Biochem. 65 87-94 PubMed GONUTS page
  2. 2.0 2.1 Müller, JJ et al. (2008) An intersubunit active site between supercoiled parallel beta helices in the trimeric tailspike endorhamnosidase of Shigella flexneri Phage Sf6. Structure 16 766-75 PubMed GONUTS page
  3. Freiberg, A et al. (2003) The tailspike protein of Shigella phage Sf6. A structural homolog of Salmonella phage P22 tailspike protein without sequence similarity in the beta-helix domain. J. Biol. Chem. 278 1542-8 PubMed GONUTS page