ID DPO3E_BUCAI Reviewed; 237 AA. AC P57337; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 1. DT 27-MAR-2024, entry version 119. DE RecName: Full=DNA polymerase III subunit epsilon; DE EC=2.7.7.7; GN Name=dnaQ; OrderedLocusNames=BU248; OS Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon OS pisum symbiotic bacterium). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Erwiniaceae; Buchnera. OX NCBI_TaxID=107806; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=APS; RX PubMed=10993077; DOI=10.1038/35024074; RA Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.; RT "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera RT sp. APS."; RL Nature 407:81-86(2000). CC -!- FUNCTION: DNA polymerase III is a complex, multichain enzyme CC responsible for most of the replicative synthesis in bacteria. The CC epsilon subunit contain the editing function and is a proofreading 3'- CC 5' exonuclease (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, CC ChEBI:CHEBI:173112; EC=2.7.7.7; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC Note=Binds 2 divalent metal cations. Magnesium or manganese. CC {ECO:0000250}; CC -!- SUBUNIT: The DNA polymerase holoenzyme is a complex that contains 10 CC different types of subunits. These subunits are organized into 3 CC functionally essential subassemblies: the pol III core, the beta CC sliding clamp processivity factor and the clamp-loading complex. The CC pol III core (subunits alpha,epsilon and theta) contains the polymerase CC and the 3'-5' exonuclease proofreading activities. The polymerase is CC tethered to the template via the sliding clamp processivity factor. The CC clamp-loading complex assembles the beta processivity factor onto the CC primer template and plays a central role in the organization and CC communication at the replication fork. This complex contains delta, CC delta', psi and chi, and copies of either or both of two different DnaX CC proteins, gamma and tau. The composition of the holoenzyme is, CC therefore: (alpha,epsilon,theta)[2]-(gamma/tau)[3]-delta,delta', CC psi,chi-beta[4] (By similarity). {ECO:0000250}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BA000003; BAB12959.1; -; Genomic_DNA. DR RefSeq; NP_240073.1; NC_002528.1. DR RefSeq; WP_010896025.1; NC_002528.1. DR AlphaFoldDB; P57337; -. DR SMR; P57337; -. DR STRING; 563178.BUAP5A_243; -. DR EnsemblBacteria; BAB12959; BAB12959; BAB12959. DR KEGG; buc:BU248; -. DR PATRIC; fig|107806.10.peg.259; -. DR eggNOG; COG0847; Bacteria. DR HOGENOM; CLU_047806_2_0_6; -. DR Proteomes; UP000001806; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW. DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW. DR CDD; cd06131; DNA_pol_III_epsilon_Ecoli_like; 1. DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1. DR InterPro; IPR006054; DnaQ. DR InterPro; IPR006309; DnaQ_proteo. DR InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3. DR InterPro; IPR012337; RNaseH-like_sf. DR InterPro; IPR036397; RNaseH_sf. DR NCBIfam; TIGR00573; dnaq; 1. DR NCBIfam; TIGR01406; dnaQ_proteo; 1. DR PANTHER; PTHR30231; DNA POLYMERASE III SUBUNIT EPSILON; 1. DR PANTHER; PTHR30231:SF43; DNA POLYMERASE III SUBUNIT EPSILON; 1. DR Pfam; PF00929; RNase_T; 1. DR SMART; SM00479; EXOIII; 1. DR SUPFAM; SSF53098; Ribonuclease H-like; 1. PE 3: Inferred from homology; KW DNA replication; DNA-directed DNA polymerase; Exonuclease; Hydrolase; KW Magnesium; Manganese; Metal-binding; Nuclease; Nucleotidyltransferase; KW Reference proteome; Transferase. FT CHAIN 1..237 FT /note="DNA polymerase III subunit epsilon" FT /id="PRO_0000105480" FT ACT_SITE 159 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT BINDING 10 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 10 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="2" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 10 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 12 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 12 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 64 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 164 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 164 FT /ligand="substrate" FT /evidence="ECO:0000250" SQ SEQUENCE 237 AA; 27365 MW; 3E4C4F102C50EBB7 CRC64; MNRKRTIILD TETTGINQTS LPHINHRIIE IGAVEIIDRC FTGNNFHVYI QPGRSIESGA LKVHGITNKF LLDKPIFKDI ADSFLNYIKN SILVIHNASF DVGFINQELE ILNKKIKINT FCSIIDTLKI ARELFPGKKN TLDALCTRYK INKSHRNLHS AIVDSYLLGK LYLLMTGGQD SLFSDNTINY KENFKKLKKN IQLKNNTLRI LHPTLKENDL HEKYLQYMKD KSTCLWN //