BPSPP:Q38152

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	ECO:0000315			F		Fig 4, Table 1.	complete CACAO 11623
	GO:0006268	DNA unwinding involved in DNA replication	PMID:18157148	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	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	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
edit table

References

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