GONUTS has been updated to MW1.31 Most things seem to be working but be sure to report problems.

Have any questions? Please email us at ecoliwiki@gmail.com

BPSPP:Q38152

From GONUTS
Jump to: navigation, search
Species (Taxon ID) Bacillus phage SPP1 (Bacteriophage SPP1). (10724)
Gene Name(s) No Information Provided.
Protein Name(s) Uncharacterized protein (ECO:0000313 with EMBL:CAA66496.1)
External Links
UniProt Q38152
EMBL X97918
PIR T42342
T42343
RefSeq NP_690733.1
PDB 3BGW
3BH0
PDBsum 3BGW
3BH0
ProteinModelPortal Q38152
SMR Q38152
DIP DIP-46406N
GeneID 955307
KEGG vg:955307
KO K02314
EvolutionaryTrace Q38152
Proteomes UP000002559
GO GO:0005524
GO:0003677
GO:0003678
GO:0006260
Gene3D 1.10.860.10
3.40.50.300
InterPro IPR007692
IPR007694
IPR007693
IPR016136
IPR027417
Pfam PF00772
PF03796
SUPFAM SSF48024
SSF52540
TIGRFAMs TIGR00665
PROSITE PS51199

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0036121

double-stranded DNA-dependent ATP-dependent DNA helicase activity

PMID:18157148[1]

ECO:0000315

F

Fig 4, Table 1.

complete
CACAO 11623

GO:0006268

DNA unwinding involved in DNA replication

PMID:18157148[1]

ECO:0000315

P

Figure 4 shows the effect of mutated residues on the protein and how the mutations effect the binding ability of the protein to primase using gel electrophoresus. Helicase binds to and unwinds the DNA prior to replication, and in complex with primase, puts down the DNA primer to initiate replication. When mutated the protein does no properly function and complex with primase to activate primase and initiate replication. Table 1 shows the series of deletions and mutations done to assess the helicase and ATPase activity in the presence and absence primase. DeltaN92 is the first series of deletions performed, deleting amino acids 1 to 92, this mutation decreased the DNA unwinding ability of the protein from 100% to 66% activity. DeltaN112 deleted amino acids 1-112. This deletion caused the DNA unwinding ability of helicase to stop almost completely, with a drop from 100% activity to 3% activity with this deletion. The double point mutation mt1 changed the amino acids I121A and E122A, resulting in a decrease in helicase activity to 7%.

complete
CACAO 11918

Contributes to

GO:1990077

primosome complex

PMID:18157148[1]

ECO:0000314

C

figure 1 shows the hexameric structure of the SPP1 helicase, determined with x-ray crystallography. Helicase binds to and unwinds the DNA prior to replication, and in complex with primase, puts down the DNA primer to initiate replication. Figure 4d shows the binding of primase and helicase into a complex by gel shift, in the presence of primase the helicase complexes with the primase and migrates more slowly and a shorter distacne through the gel than in the absence of primase. Only the full length helicase is able to form a complex with primase. Helicase binds to and unwinds the DNA prior to replication, and in complex with primase, puts down the DNA primer to initiate replication. When mutated the protein does no properly function and complex with primase to activate primase and initiate replication. Table 1 shows the series of deletions and mutations done to assess the helicase and ATPase activity in the presence and absence primase. In the presence of primase, the ATPase activity more than doubles (1 to 2.3) and the helicase activity quadruples (1 to 4.6).

complete
CACAO 12080

enables

GO:0042802

identical protein binding

PMID:18157148[1]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:Q38152

F

Seeded From UniProt

complete

involved_in

GO:0032508

DNA duplex unwinding

GO_REF:0000108

ECO:0000366

evidence based on logical inference from automatic annotation used in automatic assertion

GO:0003678

P

Seeded From UniProt

complete

enables

GO:0003677

DNA binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR007692

F

Seeded From UniProt

complete

enables

GO:0003678

DNA helicase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR007692
InterPro:IPR007693
InterPro:IPR007694
InterPro:IPR036185

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:IPR007692
InterPro:IPR007693
InterPro:IPR007694
InterPro:IPR036185

F

Seeded From UniProt

complete

involved_in

GO:0006260

DNA replication

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR007692
InterPro:IPR007693
InterPro:IPR007694
InterPro:IPR036185

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 Wang, G et al. (2008) The structure of a DnaB-family replicative helicase and its interactions with primase. Nat. Struct. Mol. Biol. 15 94-100 PubMed GONUTS page