ECOLI:DNAB

Species (Taxon ID)	Escherichia coli (strain K12). (83333)
Gene Name(s)	dnaB (synonyms: groP, grpA)
Protein Name(s)	Replicative DNA helicase
External Links
UniProt	P0ACB0
EMBL	K01174 L02312 U00006 U00096 AP009048
PIR	C65213
RefSeq	NP_418476.1 YP_492195.1
PDB	1B79 1JWE
PDBsum	1B79 1JWE
ProteinModelPortal	P0ACB0
SMR	P0ACB0
DIP	DIP-35913N
IntAct	P0ACB0
MINT	MINT-584605
STRING	511145.b4052
SWISS-2DPAGE	P0ACB0
PaxDb	P0ACB0
PRIDE	P0ACB0
EnsemblBacteria	AAC77022 BAE78054
GeneID	12932658 948555
KEGG	ecj:Y75_p3939 eco:b4052
PATRIC	32123643
EchoBASE	EB0232
EcoGene	EG10236
eggNOG	COG0305
HOGENOM	HOG000113196
InParanoid	P0ACB0
KO	K02314
OMA	FIDDKPN
OrthoDB	EOG6T4RW5
PhylomeDB	P0ACB0
BioCyc	EcoCyc:EG10236-MONOMER ECOL316407:JW4012-MONOMER MetaCyc:EG10236-MONOMER
EvolutionaryTrace	P0ACB0
PRO	PR:P0ACB0
Proteomes	UP000000318 UP000000625
Genevestigator	P0ACB0
GO	GO:1990077 GO:0005524 GO:0003677 GO:0003678 GO:0004386 GO:0042802 GO:0006260 GO:0006269 GO:0006268 GO:0010212
Gene3D	1.10.860.10 3.40.50.300
InterPro	IPR003593 IPR007692 IPR007694 IPR007693 IPR016136 IPR027417
Pfam	PF00772 PF03796
SMART	SM00382
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:0043234	protein complex	PMID:8663104^[1]	ECO:0000021		UniProtKB:P0AEF0 UniProtKB:P07013 UniProtKB:P0A8J2 UniProtKB:P17888	C		Fig. 6	complete
	GO:0006261	DNA-dependent DNA replication	PMID:4610569^[2]	ECO:0000314			P		Table 1	complete
	GO:0003924	GTPase activity	PMID:19435286^[3]	ECO:0000269			F		Table 1	complete
	GO:0016887	ATPase activity	PMID:19435286^[3]	ECO:0000269			F		Table 1	complete
involved_in	GO:0006268	DNA unwinding involved in DNA replication	PMID:21873635^[4]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10236 PANTHER:PTN001248911	P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:21873635^[4]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10236 PANTHER:PTN001248911 UniProtKB:P9WMR3	C		Seeded From UniProt	complete
enables	GO:0003678	DNA helicase activity	PMID:21873635^[4]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10236 PANTHER:PTN001248911	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:9562559^[5]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0ACB0	F	occurs_in:(GO:0033202)\|occurs_in:(GO:0043234)\|occurs_in:(GO:0030894)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:7989299^[6]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0ACB0	F	occurs_in:(GO:0033202)\|occurs_in:(GO:0043234)\|occurs_in:(GO:0030894)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:14557266^[7]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0ACB0	F	occurs_in:(GO:0033202)\|occurs_in:(GO:0043234)\|occurs_in:(GO:0030894)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:10404598^[8]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0ACB0	F	occurs_in:(GO:0033202)\|occurs_in:(GO:0043234)\|occurs_in:(GO:0030894)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:10404597^[9]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0ACB0	F	occurs_in:(GO:0033202)\|occurs_in:(GO:0043234)\|occurs_in:(GO:0030894)	Seeded From UniProt	complete
involved_in	GO:0010212	response to ionizing radiation	PMID:24596148^[10]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006268	DNA unwinding involved in DNA replication	PMID:3007474^[11]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006260	DNA replication	PMID:374337^[12]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:15911532^[13]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0004386	helicase activity	PMID:3007474^[11]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003678	DNA helicase activity	PMID:3007474^[11]	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:IPR007692	F		Seeded From UniProt	complete
	GO:0043273	CTPase activity	PMID:19435286^[3]	ECO:0000269			F		figure 1	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
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:0006260	DNA replication	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0235	P		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: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
involved_in	GO:0006269	DNA replication, synthesis of RNA primer	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0639	P		Seeded From UniProt	complete
enables	GO:0004386	helicase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0347	F		Seeded From UniProt	complete
part_of	GO:1990077	primosome complex	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0639	C		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
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Notes

References

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

↑ Ng, JY & Marians, KJ (1996) The ordered assembly of the phiX174-type primosome. I. Isolation and identification of intermediate protein-DNA complexes. J. Biol. Chem. 271 15642-8 PubMed GONUTS page
↑ Wickner, S & Hurwitz, J (1974) Conversion of phiX174 viral DNA to double-stranded form by purified Escherichia coli proteins. Proc. Natl. Acad. Sci. U.S.A. 71 4120-4 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 Roychowdhury, A et al. (2009) Mechanism of NTP hydrolysis by the Escherichia coli primary replicative helicase DnaB protein. 2. Nucleotide and nucleic acid specificities. Biochemistry 48 6730-46 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ San Martin, C et al. (1998) Three-dimensional reconstructions from cryoelectron microscopy images reveal an intimate complex between helicase DnaB and its loading partner DnaC. Structure 6 501-9 PubMed GONUTS page
↑ Bujalowski, W et al. (1994) Oligomeric structure of Escherichia coli primary replicative helicase DnaB protein. J. Biol. Chem. 269 31350-8 PubMed GONUTS page
↑ Mitkova, AV et al. (2003) Mechanism and stoichiometry of interaction of DnaG primase with DnaB helicase of Escherichia coli in RNA primer synthesis. J. Biol. Chem. 278 52253-61 PubMed GONUTS page
↑ Fass, D et al. (1999) Crystal structure of the N-terminal domain of the DnaB hexameric helicase. Structure 7 691-8 PubMed GONUTS page
↑ Weigelt, J et al. (1999) NMR structure of the N-terminal domain of E. coli DnaB helicase: implications for structure rearrangements in the helicase hexamer. Structure 7 681-90 PubMed GONUTS page
↑ Byrne, RT et al. (2014) Evolution of extreme resistance to ionizing radiation via genetic adaptation of DNA repair. Elife 3 e01322 PubMed GONUTS page
↑ ^11.0 ^11.1 ^11.2 LeBowitz, JH & McMacken, R (1986) The Escherichia coli dnaB replication protein is a DNA helicase. J. Biol. Chem. 261 4738-48 PubMed GONUTS page
↑ Hasunuma, K & Sekiguchi, M (1979) Effect of dna mutations on the replication of plasmid pSC101 in Escherichia coli K-12. J. Bacteriol. 137 1095-9 PubMed GONUTS page
↑ Lopez-Campistrous, A et al. (2005) Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell Proteomics 4 1205-9 PubMed GONUTS page

[PMID:8663104-1] Ng, JY & Marians, KJ (1996) The ordered assembly of the phiX174-type primosome. I. Isolation and identification of intermediate protein-DNA complexes. J. Biol. Chem. 271 15642-8 PubMed GONUTS page

[PMID:4610569-2] Wickner, S & Hurwitz, J (1974) Conversion of phiX174 viral DNA to double-stranded form by purified Escherichia coli proteins. Proc. Natl. Acad. Sci. U.S.A. 71 4120-4 PubMed GONUTS page

[PMID:19435286-3] 3.0 ^3.1 ^3.2 Roychowdhury, A et al. (2009) Mechanism of NTP hydrolysis by the Escherichia coli primary replicative helicase DnaB protein. 2. Nucleotide and nucleic acid specificities. Biochemistry 48 6730-46 PubMed GONUTS page

[PMID:21873635-4] 4.0 ^4.1 ^4.2 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:9562559-5] San Martin, C et al. (1998) Three-dimensional reconstructions from cryoelectron microscopy images reveal an intimate complex between helicase DnaB and its loading partner DnaC. Structure 6 501-9 PubMed GONUTS page

[PMID:7989299-6] Bujalowski, W et al. (1994) Oligomeric structure of Escherichia coli primary replicative helicase DnaB protein. J. Biol. Chem. 269 31350-8 PubMed GONUTS page

[PMID:14557266-7] Mitkova, AV et al. (2003) Mechanism and stoichiometry of interaction of DnaG primase with DnaB helicase of Escherichia coli in RNA primer synthesis. J. Biol. Chem. 278 52253-61 PubMed GONUTS page

[PMID:10404598-8] Fass, D et al. (1999) Crystal structure of the N-terminal domain of the DnaB hexameric helicase. Structure 7 691-8 PubMed GONUTS page

[PMID:10404597-9] Weigelt, J et al. (1999) NMR structure of the N-terminal domain of E. coli DnaB helicase: implications for structure rearrangements in the helicase hexamer. Structure 7 681-90 PubMed GONUTS page

[PMID:24596148-10] Byrne, RT et al. (2014) Evolution of extreme resistance to ionizing radiation via genetic adaptation of DNA repair. Elife 3 e01322 PubMed GONUTS page

[PMID:3007474-11] 11.0 ^11.1 ^11.2 LeBowitz, JH & McMacken, R (1986) The Escherichia coli dnaB replication protein is a DNA helicase. J. Biol. Chem. 261 4738-48 PubMed GONUTS page

[PMID:374337-12] Hasunuma, K & Sekiguchi, M (1979) Effect of dna mutations on the replication of plasmid pSC101 in Escherichia coli K-12. J. Bacteriol. 137 1095-9 PubMed GONUTS page

[PMID:15911532-13] Lopez-Campistrous, A et al. (2005) Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell Proteomics 4 1205-9 PubMed GONUTS page

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ECOLI:DNAB

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