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BPK1F:FIBER

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Species (Taxon ID) Enterobacteria phage K1F (Bacteriophage K1F). (344021)
Gene Name(s) No Information Provided.
Protein Name(s) Tail spike protein (ECO:0000305)

TSP Endo-N-acetylneuraminidase Endo-N Endo-alpha-sialidase (ECO:0000305) EndoNF G102 C-terminal chaperone protein

External Links
UniProt Q04830
EMBL M63657
AJ505988
DQ111067
AM084414
PIR A36887
RefSeq YP_338127.1
PDB 1V0E
1V0F
3GVJ
3GVK
3GVL
3GW6
3JU4
PDBsum 1V0E
1V0F
3GVJ
3GVK
3GVL
3GW6
3JU4
ProteinModelPortal Q04830
SMR Q04830
DIP DIP-48774N
DrugBank DB03721
DB04265
CAZy GH58
MEROPS S74.001
GeneID 3707741
KEGG vg:3707741
OrthoDB VOG09000089
BRENDA 3.2.1.129
EvolutionaryTrace Q04830
Proteomes UP000001530
UP000001722
GO GO:0098024
GO:0016996
GO:0085027
GO:0008152
GO:0046718
GO:0019062
Gene3D 2.120.10.10
2.40.30.20
3.30.750.60
4.10.1090.10
InterPro IPR023366
IPR024428
IPR024430
IPR024429
IPR001724
IPR005604
IPR030392
IPR011040
Pfam PF12217
PF12218
PF12219
PF13884
PF03906
PRINTS PR00849
SUPFAM SSF50939

Annotations

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

involved_in

GO:0019062

virion attachment to host cell

PMID:20096705[1]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0098024

virus tail, fiber

PMID:20096705[1]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0016996

endo-alpha-(2,8)-sialidase activity

PMID:3546309[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0085027

entry into host via enzymatic degradation of host anatomical structure

PMID:3546309[2]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:20118935[3]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:Q04830

F

Seeded From UniProt

complete

enables

GO:0016996

endo-alpha-(2,8)-sialidase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:3.2.1.129

F

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: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

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: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: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

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: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

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:0098996

disruption of host cell glycocalyx during viral entry

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1238

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

Notes

References

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

  1. 1.0 1.1 Schulz, EC et al. (2010) Structural basis for the recognition and cleavage of polysialic acid by the bacteriophage K1F tailspike protein EndoNF. J. Mol. Biol. 397 341-51 PubMed GONUTS page
  2. 2.0 2.1 Hallenbeck, PC et al. (1987) Purification and properties of a bacteriophage-induced endo-N-acetylneuraminidase specific for poly-alpha-2,8-sialosyl carbohydrate units. J. Biol. Chem. 262 3553-61 PubMed GONUTS page
  3. Schulz, EC et al. (2010) Crystal structure of an intramolecular chaperone mediating triple-beta-helix folding. Nat. Struct. Mol. Biol. 17 210-5 PubMed GONUTS page