P06710

PR
Gene name
dnaX (dnaZ, dnaZX, b0470, JW0459)
Protein name
DNA polymerase III subunit tau
Names
DNA polymerase III subunit gamma
Species
Escherichia coli (strain K12)
KEGG Pathway
eco:b0470
EC number
2.7.7.7: Nucleotidyltransferases
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

335-542 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

13 structures for P06710

Entry ID Method Resolution Chain Position Source
1JR3 X-ray 270 A A/B/C 1-373 PDB
1NJF X-ray 230 A A/B/C/D 1-243 PDB
1NJG X-ray 220 A A/B 1-243 PDB
1XXH X-ray 345 A B/C/D/G/H/I 1-373 PDB
1XXI X-ray 410 A B/C/D/G/H/I 1-368 PDB
2AYA NMR - A 499-625 PDB
3GLF X-ray 339 A B/C/D/G/H/I 1-373 PDB
3GLG X-ray 325 A B/C/D/G/H/I 1-373 PDB
3GLH X-ray 389 A B/C/D/G/H/I/L/M/N 1-373 PDB
3GLI X-ray 350 A B/C/D/G/H/I 1-373 PDB
5FKU EM 834 A E 500-643 PDB
5FKV EM 800 A E 500-643 PDB
AF-P06710-F1 Predicted AlphaFoldDB

No variants for P06710

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P06710

No associated diseases with P06710

6 regional properties for P06710

Type Name Position InterPro Accession
domain AAA+ ATPase domain 37 - 178 IPR003593
domain DNA polymerase III, subunit gamma/ tau, N-terminal 3 - 356 IPR012763
domain DNA polymerase III, tau subunit, domain V 500 - 640 IPR021029
domain DNA polymerase III subunit tau, DnaB-binding domain IV 417 - 498 IPR022001
domain DNA polymerase III, gamma subunit, domain III 232 - 358 IPR022754
domain DNA polymerase III, subunit gamma/tau, helical lid domain 178 - 242 IPR045085

Functions

Description
EC Number 2.7.7.7 Nucleotidyltransferases
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
DNA polymerase III complex The DNA polymerase III holoenzyme is a complex that contains 10 different types of subunits. These subunits are organized into 3 functionally essential sub-assemblies: the pol III core, the beta sliding clamp processivity factor and the clamp-loading complex. The pol III core carries out 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.
DNA polymerase III, clamp loader complex A heptamer that includes the tau and gamma products of the dnaX gene and the chi/psi subcomplex. Confers structural asymmetry that allows the polymerase to replicate both leading and lagging strands.
replisome A multi-component enzymatic machine at the replication fork which mediates DNA replication. Includes DNA primase, one or more DNA polymerases, DNA helicases, and other proteins.

7 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
ATP hydrolysis activity Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient.
DNA binding Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
DNA polymerase processivity factor activity An enzyme regulator activity that increases the processivity of polymerization by DNA polymerase, by allowing the polymerase to move rapidly along DNA while remaining topologically bound to it.
DNA-directed DNA polymerase activity Catalysis of the reaction: deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1); the synthesis of DNA from deoxyribonucleotide triphosphates in the presence of a DNA template and a 3'hydroxyl group.
identical protein binding Binding to an identical protein or proteins.
ribonucleoside triphosphate phosphatase activity Catalysis of the reaction: a ribonucleoside triphosphate + H2O = a ribonucleoside diphosphate + H+ + phosphate.

2 GO annotations of biological process

Name Definition
DNA replication The cellular metabolic process in which a cell duplicates one or more molecules of DNA. DNA replication begins when specific sequences, known as origins of replication, are recognized and bound by initiation proteins, and ends when the original DNA molecule has been completely duplicated and the copies topologically separated. The unit of replication usually corresponds to the genome of the cell, an organelle, or a virus. The template for replication can either be an existing DNA molecule or RNA.
DNA-templated DNA replication A DNA replication process that uses parental DNA as a template for the DNA-dependent DNA polymerases that synthesize the new strands.

7 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P53034 RfC4 Replication factor C subunit 2 Drosophila melanogaster (Fruit fly) PR
P40938 RFC3 Replication factor C subunit 3 Homo sapiens (Human) PR
P35249 RFC4 Replication factor C subunit 4 Homo sapiens (Human) PR
Q9D0F6 Rfc5 Replication factor C subunit 5 Mus musculus (Mouse) PR
Q8R323 Rfc3 Replication factor C subunit 3 Mus musculus (Mouse) PR
Q99J62 Rfc4 Replication factor C subunit 4 Mus musculus (Mouse) PR
F4JRP8 At4g24790 Protein STICHEL-like 2 Arabidopsis thaliana (Mouse-ear cress) PR
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