P57337 (DPO3E_BUCAI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DNA polymerase III subunit epsilon
EC=2.7.7.7

Gene names

Name:	dnaQ
Ordered Locus Names:	BU248

Organism

Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon pisum symbiotic bacterium) [Reference proteome] [HAMAP]

Taxonomic identifier

107806 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera › Buchnera aphidicola › Buchnera aphidicola (Acyrthosiphon pisum)

Protein attributes

Sequence length	237 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. The epsilon subunit contain the editing function and is a proofreading 3'-5' exonuclease By similarity.
Catalytic activity	Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).
Cofactor	Binds 2 divalent metal cations. Magnesium or manganese By similarity.
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] By similarity.

Ontologies

Keywords
Biological process	DNA replication
Ligand	Magnesium Manganese Metal-binding
Molecular function	DNA-directed DNA polymerase Exonuclease Hydrolase Nuclease Nucleotidyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA replication Inferred from electronic annotation. Source: UniProtKB-KW nucleic acid phosphodiester bond hydrolysis Inferred from electronic annotation. Source: GOC
Cellular_component	intracellular Inferred from electronic annotation. Source: InterPro
Molecular_function	DNA binding Inferred from electronic annotation. Source: InterPro DNA-directed DNA polymerase activity Inferred from electronic annotation. Source: UniProtKB-KW exonuclease activity Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 237	237	DNA polymerase III subunit epsilon		PRO_0000105480
Sites
	Active site	159	1	Proton acceptor By similarity
	Metal binding	10	1	Divalent metal cation 1; catalytic By similarity
	Metal binding	10	1	Divalent metal cation 2; catalytic By similarity
	Metal binding	12	1	Divalent metal cation 1; catalytic By similarity
	Metal binding	164	1	Divalent metal cation 1; catalytic By similarity
	Binding site	10	1	Substrate By similarity
	Binding site	12	1	Substrate By similarity
	Binding site	64	1	Substrate By similarity
	Binding site	164	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P57337 [UniParc]. Last modified December 1, 2000. Version 1. Checksum: 3E4C4F102C50EBB7	FASTA	237	27,365
	10 20 30 40 50 60 MNRKRTIILD TETTGINQTS LPHINHRIIE IGAVEIIDRC FTGNNFHVYI QPGRSIESGA 70 80 90 100 110 120 LKVHGITNKF LLDKPIFKDI ADSFLNYIKN SILVIHNASF DVGFINQELE ILNKKIKINT 130 140 150 160 170 180 FCSIIDTLKI ARELFPGKKN TLDALCTRYK INKSHRNLHS AIVDSYLLGK LYLLMTGGQD 190 200 210 220 230 SLFSDNTINY KENFKKLKKN IQLKNNTLRI LHPTLKENDL HEKYLQYMKD KSTCLWN

References

[1]	"Genome sequence of the endocellular bacterial symbiont of aphids Buchnera sp. APS." Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H. Nature 407:81-86(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: APS.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000003 Genomic DNA. Translation: BAB12959.1.
RefSeq	NP_240073.1. NC_002528.1.
3D structure databases
ProteinModelPortal	P57337.
SMR	P57337. Positions 5-177.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAB12959; BAB12959; BAB12959.
GeneID	1109688.
KEGG	buc:BU248.
PATRIC	21244020. VBIBucAph127364_0259.
Phylogenomic databases
eggNOG	COG0847.
HOGENOM	HOG000258616.
KO	K02342.
OMA	HGITNEF.
ProtClustDB	CLSK315823.
Enzyme and pathway databases
BioCyc	BAPH107806:GBZJ-248-MONOMER.
Family and domain databases
InterPro	IPR006054. DnaQ. IPR006309. DnaQ_proteo. IPR006055. Exonuclease. IPR013520. Exonuclease_RNaseT/DNA_pol3. IPR012337. RNaseH-like_dom. [Graphical view]
Pfam	PF00929. RNase_T. 1 hit. [Graphical view]
SMART	SM00479. EXOIII. 1 hit. [Graphical view]
SUPFAM	SSF53098. RNaseH_fold. 1 hit.
TIGRFAMs	TIGR00573. dnaq. 1 hit. TIGR01406. dnaQ_proteo. 1 hit.
ProtoNet	Search...

Entry information

Entry name

DPO3E_BUCAI

Accession

Primary (citable) accession number: P57337

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	December 1, 2000
Last modified:	May 29, 2013
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program