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BPPH2:GP13

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Species (Taxon ID) Bacillus phage phi29 (Bacteriophage phi-29). (10756)
Gene Name(s) 13
Protein Name(s) Morphogenesis protein 1 (ECO:0000303 with Ref.3)

Gene product 13 (ECO:0000303 with PMID:18394643[1]) gp13 (ECO:0000303 with PMID:18394643[1]) Protein p13 (ECO:0000305) Lysozyme-like glycosidase Probable metalloendopeptidase

External Links
UniProt P15132
EMBL M14782
X04962
EU771092
PIR H25816
RefSeq YP_002004542.1
PDB 3CSQ
3CSR
3CSZ
3CT0
3CT1
3CT5
PDBsum 3CSQ
3CSR
3CSZ
3CT0
3CT1
3CT5
ProteinModelPortal P15132
SMR P15132
MEROPS M23.008
GeneID 6446506
KEGG vg:6446506
OrthoDB VOG090000BY
EvolutionaryTrace P15132
Proteomes UP000001207
GO GO:0098023
GO:0016798
GO:0046872
GO:0008237
GO:0071555
GO:0019835
GO:0042742
GO:0046718
GO:0019076
InterPro IPR011055
SUPFAM SSF51261

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0098015

virus tail

PMID:18394643[1]

ECO:0000279

western blot evidence used in manual assertion

C

Figure 2 shows that Morphogenesis protein 1 (gp13) in Bacillus phage phi29 is a structural component of the phi 29 tail.

complete
CACAO 13807

GO:0098004

virus tail fiber assembly

PMID:18394643[1]

ECO:0000314

P

GP13 is seen as structural component of the phage ϕ29 tail. Figure 2, uses Western Blot Analysis to infer that gp13 is a component of the tail fiber. Loss of gp13 causes the tail tip, results in a shortened tail (missing tail fibers) . This is specified in Table 3, which quantifies assembly of WT and several gp 13 mutants.

complete
CACAO 12592

part_of

GO:0098023

virus tail, tip

PMID:18394643[1]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0003824

catalytic activity

GO_REF:0000037
GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0511
UniProtKB-KW:KW-0081

F

Seeded From UniProt

complete

involved_in

GO:0008152

metabolic process

GO_REF:0000037
GO_REF:0000037
GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0326
UniProtKB-KW:KW-0081
UniProtKB-KW:KW-0511

P

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

enables

GO:0008237

metallopeptidase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0482

F

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-1162
UniProtKB-KW:KW-1160

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

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:0019835

cytolysis

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: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

enables

GO:0046872

metal ion binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0479

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: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:0071555

cell wall organization

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0961

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

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: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:0099002

viral genome ejection through host cell envelope, short tail mechanism

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1244

P

Seeded From UniProt

complete

GO:0098023

virus tail, tip

PMID:18394643[1]

ECO:0005592

immunogold labelling electron microscopy assay evidence used in manual assertion

C

Notes: Figure 3 shows that Morphogenesis protein 1 (gp13) in Bacillus phage phi29 is located at the distal end of the ϕ29 tail knob using an Immuno-gold localization.

complete

Notes

References

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

  1. 1.0 1.1 1.2 1.3 1.4 1.5 Cohen, DN et al. (2008) Multifunctional roles of a bacteriophage phi 29 morphogenetic factor in assembly and infection. J. Mol. Biol. 378 804-17 PubMed GONUTS page