DPO3E_BUCAI
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 03-AUG-2022, entry version 113.
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; Proteobacteria; 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}.
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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; 107806.10038924; -.
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 OMA; FHVYLNP; -.
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; -; 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 Pfam; PF00929; RNase_T; 1.
DR SMART; SM00479; EXOIII; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR TIGRFAMs; TIGR00573; dnaq; 1.
DR TIGRFAMs; TIGR01406; dnaQ_proteo; 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
