P43745 (DPO3E_HAEIN) 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:	HI_0137

Organism

Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) [Reference proteome] [HAMAP]

Taxonomic identifier

71421 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus › Haemophilus influenzae

Protein attributes

Sequence length	256 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	DNA polymerase III contains a core (composed of alpha, epsilon and theta chains) that associates with a tau subunit. This core dimerizes to form the POLIII' complex. PolIII' associates with the gamma complex (composed of gamma, delta, delta', psi and chi chains) and with the beta chain to form the complete DNA polymerase III complex 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 – 256	256	DNA polymerase III subunit epsilon		PRO_0000105486
Sites
	Active site	160	1	Proton acceptor By similarity
	Metal binding	11	1	Divalent metal cation 1; catalytic By similarity
	Metal binding	11	1	Divalent metal cation 2; catalytic By similarity
	Metal binding	13	1	Divalent metal cation 1; catalytic By similarity
	Metal binding	165	1	Divalent metal cation 1; catalytic By similarity
	Binding site	11	1	Substrate By similarity
	Binding site	13	1	Substrate By similarity
	Binding site	60	1	Substrate By similarity
	Binding site	65	1	Substrate By similarity
	Binding site	165	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P43745 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 694C9273AD4438D1	FASTA	256	29,133
	10 20 30 40 50 60 MINPNRQIVL DTETTGMNQL GAHYEGHCII EIGAVELINR RYTGNNXHIY IKPDRPXDPD 70 80 90 100 110 120 AIKVHGITDE MLADKPEFKE VAQDFLDYIN GAELLIHNAP FDVGFMDYEF RKLNLNVKTD 130 140 150 160 170 180 DICLVTDTLQ MARQMYPGKR NNLDALCDRL GIDNSKRTLH GALLDAEILA DVYLMMTGGQ 190 200 210 220 230 240 TNLFDEEESV ESGVIRVMQE KTAEEIKSAV DFSHNLKLLQ PTNDELQAHL EFLKMMNKKS 250 GNNCLWDKRF GNNNVH

References

[1]

"Whole-genome random sequencing and assembly of Haemophilus influenzae Rd." Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I. , Glodek A., Kelley J.M., Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., Venter J.C. Science 269:496-512(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L42023 Genomic DNA. Translation: AAC21808.1.
PIR	B64050.
RefSeq	NP_438306.1. NC_000907.1.
3D structure databases
ProteinModelPortal	P43745.
ModBase	Search...
Protein-protein interaction databases
STRING	71421.HI0137.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC21808; AAC21808; HI_0137.
GeneID	951047.
KEGG	hin:HI0137.
PATRIC	20188765. VBIHaeInf48452_0139.
Phylogenomic databases
eggNOG	COG0847.
KO	K02342.
OMA	HGITNEF.
ProtClustDB	PRK05711.
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_HAEIN

Accession

Primary (citable) accession number: P43745

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	May 1, 2013
This is version 87 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program