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BPT4:TOPS

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Species (Taxon ID) Enterobacteria phage T4 (Bacteriophage T4). (10665)
Gene Name(s) 60
Protein Name(s) DNA topoisomerase small subunit

Protein Gp60

External Links
UniProt P23992
EMBL M19728
AF158101
X52686
PIR JT0209
RefSeq NP_049618.1
PDB 5NP6
PDBsum 5NP6
ProteinModelPortal P23992
SMR P23992
GeneID 1258779
KEGG vg:1258779
Proteomes UP000009087
GO GO:0005524
GO:0003677
GO:0003918
GO:0006265
Gene3D 3.40.50.670
InterPro IPR001241
IPR013760
IPR013759
IPR031660
PANTHER PTHR10169
Pfam PF16898
SUPFAM SSF56719

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0009330

DNA topoisomerase complex (ATP-hydrolyzing)

PMID:6296073[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

C

In figure 7, gp60 was replaced with a mutant version, amE429 or amE594, and then the protein complex was eluted and run through a gel. Lanes 1-3 are gels of increasingly concentrated fractions of amE492 infected cells. Lane 4 uses the same fraction as lane 3, but eluted with .1M potassium phosphate buffer, as a control for the buffer. Lane 5 is the same fraction as lane 3, but eluted with .3M potassium phosphate buffer. Lane 6 is the same as lane 5, but with .5M potassium phosphate buffer. Lane 6 has the standards for the three proteins in topoisomerase, p39, p52, and p60. Lanes 8 and 9 are the same as lanes 5 and 6, respectively, but using amE594 as the mutant gene 60 instead of amE429. In lanes 5 and 8, p60 is absent (due to the mutation) and p39 is also absent. P52 is evident, meaning it was able to be eluted by the .3M buffer. In lanes 6 and 9, p60 is again absent as is p52, since it had already been eluted out. P39 is evident, as it was eluted out of fraction by .5M buffer. Since both proteins were eluted out by different concentrations of buffer, they were not bound together, which differs from past research that proves them bound together in complex. Therefore, p60 must be capable of binding them together without any conformational change of p39 or p52(both proteins' identities were confirmed after experiment).

complete
CACAO 13106

part_of

GO:0032991

protein-containing complex

PMID:226976[2]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

contributes_to

GO:0003916

DNA topoisomerase activity

PMID:226976[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0003677

DNA binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001241
InterPro:IPR013759

F

Seeded From UniProt

complete

enables

GO:0003918

DNA topoisomerase type II (ATP-hydrolyzing) activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001241
InterPro:IPR013759
InterPro:IPR013760

F

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001241
InterPro:IPR013759
InterPro:IPR013760

F

Seeded From UniProt

complete

involved_in

GO:0006265

DNA topological change

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001241
InterPro:IPR013759

P

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0067

F

Seeded From UniProt

complete

enables

GO:0003677

DNA binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0238

F

Seeded From UniProt

complete

enables

GO:0000166

nucleotide binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0547

F

Seeded From UniProt

complete

enables

GO:0003916

DNA topoisomerase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0799

F

Seeded From UniProt

complete

enables

GO:0016853

isomerase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0413

F

Seeded From UniProt

complete

Notes

References

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

  1. Seasholtz, AF & Greenberg, GR (1983) Identification of bacteriophage T4 gene 60 product and a role for this protein in DNA topoisomerase. J. Biol. Chem. 258 1221-6 PubMed GONUTS page
  2. 2.0 2.1 Stetler, GL et al. (1979) T4 DNA-delay proteins, required for specific DNA replication, form a complex that has ATP-dependent DNA topoisomerase activity. Proc. Natl. Acad. Sci. U.S.A. 76 3737-41 PubMed GONUTS page