DNA polymerase III subunit tau - Escherichia coli (strain K12)

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Reviewed, UniProtKB/Swiss-Prot P06710 (DPO3X_ECOLI)

Last modified June 16, 2009. Version 100. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    DNA polymerase III subunit tau
    EC=2.7.7.7
Cleaved into the following chain:
    1- Recommended name:
            DNA polymerase III subunit gamma

Gene names

Name:	dnaX
Synonyms:	dnaZ, dnaZX
Ordered Locus Names:	b0470, JW0459

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length	643 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity. The tau chain serves as a scaffold to help in the dimerizaton of the core complex. The gamma chain seems to interact with the delta subunit to transfer the beta subunit on the DNA.
Catalytic activity	Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).
Subunit structure	The DNA polymerase holoenzyme is a complex that contains 10 different types of subunits. These subunits are organized into 3 functionally essential subassemblies: the pol III core, the beta sliding clamp processivity factor and the clamp-loading complex. The pol III core (subunits alpha,epsilon and theta) contains the polymerase and the 3'-5' exonuclease proofreading activities. The polymerase is tethered to the template via the sliding clamp processivity factor. The clamp-loading complex assembles the beta processivity factor onto the primer template and plays a central role in the organization and communication at the replication fork. This complex contains delta, delta', psi and chi, and copies of either or both of two different dnaX proteins, gamma and tau. The composition of the holoenzyme is, therefore: (alpha,epsilon,theta)[2]-(gamma/tau)[3]-delta,delta', psi,chi-beta[4].
Miscellaneous	The production of the two protein products from this region is due to programmed ribosomal frameshifting.

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Ontologies

Keywords
Biological process	DNA replication
Coding sequence diversity	Ribosomal frameshifting
Ligand	ATP-binding Nucleotide-binding
Molecular function	DNA-directed DNA polymerase Nucleotidyltransferase Transferase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	DNA replication Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	DNA polymerase III complex Inferred from electronic annotation. Source: InterPro
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW DNA binding Inferred from electronic annotation. Source: InterPro DNA-directed DNA polymerase activity Inferred from electronic annotation. Source: UniProtKB-KW nucleoside-triphosphatase activity Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
rplA	P0A7L0	1	EBI-549140,EBI-543771

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 643

643

DNA polymerase III subunit tau

PRO_0000007360

Chain

1 – 431

431

DNA polymerase III subunit gamma

PRO_0000007361

Regions

Nucleotide binding

45 – 52

ATP Potential

Secondary structure

643

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P06710-1 [UniParc].

Last modified January 1, 1988. Version 1.
Checksum: D2028BD99E375150
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FASTA

643

71,138

        10         20         30         40         50         60 
MSYQVLARKW RPQTFADVVG QEHVLTALAN GLSLGRIHHA YLFSGTRGVG KTSIARLLAK 

        70         80         90        100        110        120 
GLNCETGITA TPCGVCDNCR EIEQGRFVDL IEIDAASRTK VEDTRDLLDN VQYAPARGRF 

       130        140        150        160        170        180 
KVYLIDEVHM LSRHSFNALL KTLEEPPEHV KFLLATTDPQ KLPVTILSRC LQFHLKALDV 

       190        200        210        220        230        240 
EQIRHQLEHI LNEEHIAHEP RALQLLARAA EGSLRDALSL TDQAIASGDG QVSTQAVSAM 

       250        260        270        280        290        300 
LGTLDDDQAL SLVEAMVEAN GERVMALINE AAARGIEWEA LLVEMLGLLH RIAMVQLSPA 

       310        320        330        340        350        360 
ALGNDMAAIE LRMRELARTI PPTDIQLYYQ TLLIGRKELP YAPDRRMGVE MTLLRALAFH 

       370        380        390        400        410        420 
PRMPLPEPEV PRQSFAPVAP TAVMTPTQVP PQPQSAPQQA PTVPLPETTS QVLAARQQLQ 

       430        440        450        460        470        480 
RVQGATKAKK SEPAAATRAR PVNNAALERL ASVTDRVQAR PVPSALEKAP AKKEAYRWKA 

       490        500        510        520        530        540 
TTPVMQQKEV VATPKALKKA LEHEKTPELA AKLAAEAIER DPWAAQVSQL SLPKLVEQVA 

       550        560        570        580        590        600 
LNAWKEESDN AVCLHLRSSQ RHLNNRGAQQ KLAEALSMLK GSTVELTIVE DDNPAVRTPL 

       610        620        630        640 
EWRQAIYEEK LAQARESIIA DNNIQTLRRF FDAELDEESI RPI

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The adjacent dnaZ and dnaX genes of Escherichia coli are contained within one continuous open reading frame." Flower A.M., McHenry C.S. Nucleic Acids Res. 14:8091-8101(1986) [PubMed: 3534795] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12 / JM109 / ATCC 53323.
[2]	"Nucleotide sequence of the Escherichia coli replication gene dnaZX." Yin K.-C., Blinkowa A.L., Walker J.R. Nucleic Acids Res. 14:6541-6549(1986) [PubMed: 3018672] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Sequence of minutes 4-25 of Escherichia coli." Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W. Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"Programmed ribosomal frameshifting generates the Escherichia coli DNA polymerase III gamma subunit from within the tau subunit reading frame." Blinkowa A.L., Walker J.R. Nucleic Acids Res. 18:1725-1729(1990) [PubMed: 2186364] [Abstract] Cited for: RIBOSOMAL FRAMESHIFT.
[7]	"The gamma subunit of DNA polymerase III holoenzyme of Escherichia coli is produced by ribosomal frameshifting." Flower A.M., McHenry C.S. Proc. Natl. Acad. Sci. U.S.A. 87:3713-3717(1990) [PubMed: 2187190] [Abstract] Cited for: RIBOSOMAL FRAMESHIFT.
[8]	"Translational frameshifting generates the gamma subunit of DNA polymerase III holoenzyme." Tsuchihashi Z., Kornberg A. Proc. Natl. Acad. Sci. U.S.A. 87:2516-2520(1990) [PubMed: 2181440] [Abstract] Cited for: RIBOSOMAL FRAMESHIFT.
[9]	"Accessory protein function in the DNA polymerase III holoenzyme from E. coli." O'Donnell M. Bioessays 14:105-111(1992) [PubMed: 1575709] [Abstract] Cited for: REVIEW.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

X04487 Genomic DNA. Translation: CAA28174.1.
X04487 Genomic DNA. Translation: CAA28175.1. Different initiation.
X04275 Genomic DNA. Translation: CAA27827.1.
U82664 Genomic DNA. Translation: AAB40224.1.
U00096 Genomic DNA. Translation: AAC73572.1.
AP009048 Genomic DNA. Translation: BAE76249.1.
M38777 Genomic DNA. Translation: AAA23457.1.

PIR

DJEC3G. A25549.

RefSeq

AP_001119.1.
NP_415003.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1JR3	X-ray	2.70	A/B/C	1-373	[»]
1NJF	X-ray	2.30	A/B/C/D	1-243	[»]
1NJG	X-ray	2.20	A/B	1-243	[»]
1XXH	X-ray	3.45	B/C/D/G/H/I	1-373	[»]
1XXI	X-ray	4.10	B/C/D/G/H/I	1-368	[»]
2AYA	NMR	-	A	499-625	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:9464N.

IntAct

P06710. 21 interactions.

2-D gel databases

ECO2DBASE

H052.0. 6TH EDITION.
H080.0. 6TH EDITION.

Genome annotation databases

GeneID

945105.

GenomeReviews

Gene locus JW0459 in contig AP009048_GR.
Gene locus b0470 in contig U00096_GR.

KEGG

ecj:JW0459.
eco:b0470.

Organism-specific databases

EchoBASE

EB0241.

EcoGene

EG10245. dnaX.

CMR

Search...

Phylogenomic databases

HOGENOM

P06710.

OMA

P06710. HAADGSM.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10245-MON.
EcoCyc:MON0-2383.

Family and domain databases

InterPro

IPR003593. ATPase_AAA+_core.
IPR003959. ATPase_AAA_core.
IPR001270. Chaprnin_clpA/B.
IPR012763. DnaX_N.
[Graphical view]

Pfam

PF00004. AAA. 1 hit.
[Graphical view]

PRINTS

PR00300. CLPPROTEASEA.

SMART

SM00382. AAA. 1 hit.
[Graphical view]

TIGRFAMs

TIGR02397. dnaX_nterm. 1 hit.

ProtoNet

Search...

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Entry information

Entry name

DPO3X_ECOLI

Accession

Primary (citable) accession number: P06710
Secondary accession number(s): Q2MBV7, Q47721

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	January 1, 1988
Last modified:	June 16, 2009
This is version 100 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2-D gel databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents