DPO3E_BUCBP
ID DPO3E_BUCBP Reviewed; 245 AA.
AC Q89AN3;
DT 30-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2003, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=DNA polymerase III subunit epsilon;
DE EC=2.7.7.7;
GN Name=dnaQ; OrderedLocusNames=bbp_230;
OS Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=224915;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bp;
RX PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT "Reductive genome evolution in Buchnera aphidicola.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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; AE016826; AAO26958.1; -; Genomic_DNA.
DR RefSeq; WP_011091359.1; NC_004545.1.
DR AlphaFoldDB; Q89AN3; -.
DR SMR; Q89AN3; -.
DR STRING; 224915.bbp_230; -.
DR EnsemblBacteria; AAO26958; AAO26958; bbp_230.
DR GeneID; 56470772; -.
DR KEGG; bab:bbp_230; -.
DR eggNOG; COG0847; Bacteria.
DR HOGENOM; CLU_047806_2_0_6; -.
DR OMA; FHVYLNP; -.
DR OrthoDB; 1985371at2; -.
DR Proteomes; UP000000601; 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..245
FT /note="DNA polymerase III subunit epsilon"
FT /id="PRO_0000105482"
FT ACT_SITE 161
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 11
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 11
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 11
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 13
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 13
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 60
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 65
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 166
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 166
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 245 AA; 28519 MW; 866B40B552C5027B CRC64;
MKKYDRKIVL DIETTGMNPA GCFYKNHKII EIGAVEMINN VFTGNNFHSY IQPNRLIDKQ
SFKIHGITDN FLLDKPKFHE ISVKFLEYIT NSDLIIHNAK FDVGFINYEL NMINSDKRKI
SDYCNVVDTL PLARQLFPGK KNSLDALCNR YKINVSHRDF HSALIDAKLL AKVYTFMTSF
QQSISIFDKN SNLNSIQKNA KLDSRVPFRS TLLLATKDEL QQHMKYLKYV KQETGNCVWL
EDKYN
