ECOLI:DPO3X

Species (Taxon ID)	Escherichia coli (strain K12). (83333)
Gene Name(s)	dnaX (synonyms: dnaZ, dnaZX)
Protein Name(s)	DNA polymerase III subunit tau DNA polymerase III subunit gamma
External Links
UniProt	P06710
EMBL	X04487 X04487 X04275 U82664 U00096 AP009048 M38777
PIR	A25549
RefSeq	NP_415003.1 YP_488761.1
PDB	1JR3 1NJF 1NJG 1XXH 1XXI 2AYA 3GLF 3GLG 3GLH 3GLI
PDBsum	1JR3 1NJF 1NJG 1XXH 1XXI 2AYA 3GLF 3GLG 3GLH 3GLI
ProteinModelPortal	P06710
SMR	P06710
DIP	DIP-9464N
IntAct	P06710
MINT	MINT-1222776
STRING	511145.b0470
BindingDB	P06710
PaxDb	P06710
PRIDE	P06710
EnsemblBacteria	AAC73572 BAE76249
GeneID	12930852 945105
KEGG	ecj:Y75_p0457 eco:b0470
PATRIC	32116097
EchoBASE	EB0241
EcoGene	EG10245
eggNOG	COG2812
HOGENOM	HOG000083934
InParanoid	P06710
KO	K02343
OMA	AMGQGQV
OrthoDB	EOG6WQD76
PhylomeDB	P06710
BioCyc	EcoCyc:EG10245-MONOMER EcoCyc:MONOMER0-2383 ECOL316407:JW0459-MONOMER
EvolutionaryTrace	P06710
PRO	PR:P06710
Proteomes	UP000000318 UP000000625
Genevestigator	P06710
GO	GO:0043846 GO:0005524 GO:0016887 GO:0003677 GO:0030337 GO:0003887 GO:0042802 GO:0017111 GO:0006200 GO:0006260
Gene3D	3.40.50.300
InterPro	IPR003593 IPR001270 IPR008921 IPR022001 IPR022754 IPR012763 IPR021029 IPR027417
Pfam	PF12169 PF12168 PF12170
PRINTS	PR00300
SMART	SM00382
SUPFAM	SSF48019 SSF52540
TIGRFAMs	TIGR02397

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
	GO:0006261	DNA-dependent DNA replication	PMID:4610569^[1]	ECO:0000314			P		Table 1	complete
involved_in	GO:0006261	DNA-dependent DNA replication	PMID:21873635^[2]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG11500 PANTHER:PTN000186208	P		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:24561554^[3]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P06710	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:20223211^[4]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P06710	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:11463787^[5]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P06710-2	F	occurs_in:(GO:0043846)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:11463787^[5]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P06710	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:11101526^[6]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P06710-2	F	occurs_in:(GO:0043846)	Seeded From UniProt	complete
part_of	GO:0043846	DNA polymerase III, clamp loader complex	PMID:8376347^[7]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0030337	DNA polymerase processivity factor activity	PMID:7494000^[8]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0030337	DNA polymerase processivity factor activity	PMID:11525729^[9]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0017111	nucleoside-triphosphatase activity	PMID:11029431^[10]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0016887	ATPase activity	PMID:2681183^[11]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0006260	DNA replication	PMID:391641^[12]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006259	DNA metabolic process	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0030337	P		Seeded From UniProt	complete
involved_in	GO:0006259	DNA metabolic process	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0030337	P		Seeded From UniProt	complete
involved_in	GO:0071897	DNA biosynthetic process	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0003887	P		Seeded From UniProt	complete
involved_in	GO:0071897	DNA biosynthetic process	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0003887	P		Seeded From UniProt	complete
involved_in	GO:0071897	DNA biosynthetic process	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0003887	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:IPR008921	F		Seeded From UniProt	complete
enables	GO:0003887	DNA-directed DNA polymerase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR012763 InterPro:IPR021029 InterPro:IPR022754	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:IPR001270 InterPro:IPR012763	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:IPR008921 InterPro:IPR012763	P		Seeded From UniProt	complete
part_of	GO:0009360	DNA polymerase III complex	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR012763	C		Seeded From UniProt	complete
enables	GO:0003887	DNA-directed DNA polymerase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:2.7.7.7	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
enables	GO:0003887	DNA-directed DNA polymerase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0239	F		Seeded From UniProt	complete
enables	GO:0016740	transferase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0808	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
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:0016779	nucleotidyltransferase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0548	F		Seeded From UniProt	complete
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Notes

References

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

↑ 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
↑ Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Rajagopala, SV et al. (2014) The binary protein-protein interaction landscape of Escherichia coli. Nat. Biotechnol. 32 285-90 PubMed GONUTS page
↑ Park, AY et al. (2010) A single subunit directs the assembly of the Escherichia coli DNA sliding clamp loader. Structure 18 285-92 PubMed GONUTS page
↑ ^5.0 ^5.1 Glover, BP et al. (2001) tau binds and organizes Escherichia coli replication proteins through distinct domains: domain III, shared by gamma and tau, oligomerizes DnaX. J. Biol. Chem. 276 35842-6 PubMed GONUTS page
↑ Pritchard, AE et al. (2000) A novel assembly mechanism for the DNA polymerase III holoenzyme DnaX complex: association of deltadelta' with DnaX(4) forms DnaX(3)deltadelta'. EMBO J. 19 6536-45 PubMed GONUTS page
↑ Blinkova, A et al. (1993) The Escherichia coli DNA polymerase III holoenzyme contains both products of the dnaX gene, tau and gamma, but only tau is essential. J. Bacteriol. 175 6018-27 PubMed GONUTS page
↑ Olson, MW et al. (1995) DnaX complex of Escherichia coli DNA polymerase III holoenzyme. The chi psi complex functions by increasing the affinity of tau and gamma for delta.delta' to a physiologically relevant range. J. Biol. Chem. 270 29570-7 PubMed GONUTS page
↑ Jeruzalmi, D et al. (2001) Crystal structure of the processivity clamp loader gamma (gamma) complex of E. coli DNA polymerase III. Cell 106 429-41 PubMed GONUTS page
↑ Walker, JR et al. (2000) Escherichia coli DNA polymerase III tau- and gamma-subunit conserved residues required for activity in vivo and in vitro. J. Bacteriol. 182 6106-13 PubMed GONUTS page
↑ Tsuchihashi, Z & Kornberg, A (1989) ATP interactions of the tau and gamma subunits of DNA polymerase III holoenzyme of Escherichia coli. J. Biol. Chem. 264 17790-5 PubMed GONUTS page
↑ Henson, JM et al. (1979) Isolation and characterization of dnaX and dnaY temperature-sensitive mutants of Escherichia coli. Genetics 92 1041-59 PubMed GONUTS page

[PMID:4610569-1] 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:21873635-2] 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:24561554-3] Rajagopala, SV et al. (2014) The binary protein-protein interaction landscape of Escherichia coli. Nat. Biotechnol. 32 285-90 PubMed GONUTS page

[PMID:20223211-4] Park, AY et al. (2010) A single subunit directs the assembly of the Escherichia coli DNA sliding clamp loader. Structure 18 285-92 PubMed GONUTS page

[PMID:11463787-5] 5.0 ^5.1 Glover, BP et al. (2001) tau binds and organizes Escherichia coli replication proteins through distinct domains: domain III, shared by gamma and tau, oligomerizes DnaX. J. Biol. Chem. 276 35842-6 PubMed GONUTS page

[PMID:11101526-6] Pritchard, AE et al. (2000) A novel assembly mechanism for the DNA polymerase III holoenzyme DnaX complex: association of deltadelta' with DnaX(4) forms DnaX(3)deltadelta'. EMBO J. 19 6536-45 PubMed GONUTS page

[PMID:8376347-7] Blinkova, A et al. (1993) The Escherichia coli DNA polymerase III holoenzyme contains both products of the dnaX gene, tau and gamma, but only tau is essential. J. Bacteriol. 175 6018-27 PubMed GONUTS page

[PMID:7494000-8] Olson, MW et al. (1995) DnaX complex of Escherichia coli DNA polymerase III holoenzyme. The chi psi complex functions by increasing the affinity of tau and gamma for delta.delta' to a physiologically relevant range. J. Biol. Chem. 270 29570-7 PubMed GONUTS page

[PMID:11525729-9] Jeruzalmi, D et al. (2001) Crystal structure of the processivity clamp loader gamma (gamma) complex of E. coli DNA polymerase III. Cell 106 429-41 PubMed GONUTS page

[PMID:11029431-10] Walker, JR et al. (2000) Escherichia coli DNA polymerase III tau- and gamma-subunit conserved residues required for activity in vivo and in vitro. J. Bacteriol. 182 6106-13 PubMed GONUTS page

[PMID:2681183-11] Tsuchihashi, Z & Kornberg, A (1989) ATP interactions of the tau and gamma subunits of DNA polymerase III holoenzyme of Escherichia coli. J. Biol. Chem. 264 17790-5 PubMed GONUTS page

[PMID:391641-12] Henson, JM et al. (1979) Isolation and characterization of dnaX and dnaY temperature-sensitive mutants of Escherichia coli. Genetics 92 1041-59 PubMed GONUTS page

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ECOLI:DPO3X

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