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ECOLI:DPO3X

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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

Notes

References

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

  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
  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
  3. Rajagopala, SV et al. (2014) The binary protein-protein interaction landscape of Escherichia coli. Nat. Biotechnol. 32 285-90 PubMed GONUTS page
  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
  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
  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
  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
  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
  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
  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
  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
  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