ID   DPO3E_BUCAP             Reviewed;         233 AA.
AC   Q08880;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   27-MAR-2024, entry version 140.
DE   RecName: Full=DNA polymerase III subunit epsilon;
DE            EC=2.7.7.7;
GN   Name=dnaQ; Synonyms=mutD; OrderedLocusNames=BUsg_240;
OS   Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=198804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9000520; DOI=10.1016/s0014-5793(96)01361-0;
RA   Huang Y., Braithwaite D.K., Ito J.;
RT   "Evolution of dnaQ, the gene encoding the editing 3' to 5' exonuclease
RT   subunit of DNA polymerase III holoenzyme in Gram-negative bacteria.";
RL   FEBS Lett. 400:94-98(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sg;
RX   PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-179.
RX   PubMed=7507875; DOI=10.1016/0378-1119(93)90003-l;
RA   Munson M.A., Baumann L., Baumann P.;
RT   "Buchnera aphidicola (a prokaryotic endosymbiont of aphids) contains a
RT   putative 16S rRNA operon unlinked to the 23S rRNA-encoding gene: sequence
RT   determination, and promoter and terminator analysis.";
RL   Gene 137:171-178(1993).
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   -!- SEQUENCE CAUTION:
CC       Sequence=AAM67799.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; U77464; AAC44791.1; -; Genomic_DNA.
DR   EMBL; AE013218; AAM67799.1; ALT_INIT; Genomic_DNA.
DR   EMBL; L18927; AAA17435.1; -; Genomic_DNA.
DR   PIR; I40594; I40594.
DR   AlphaFoldDB; Q08880; -.
DR   SMR; Q08880; -.
DR   STRING; 198804.BUsg_240; -.
DR   KEGG; bas:BUsg_240; -.
DR   eggNOG; COG0847; Bacteria.
DR   HOGENOM; CLU_047806_2_0_6; -.
DR   Proteomes; UP000000416; 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   Transferase.
FT   CHAIN           1..233
FT                   /note="DNA polymerase III subunit epsilon"
FT                   /id="PRO_0000105481"
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:0000250"
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   233 AA;  27170 MW;  F722E4C65DB1E583 CRC64;
     MNNTQRIIVL DTETTGMNSV GPPYLNHRII EIGAIEIINR RFTGKKFHTY IKPNRLIESD
     ASKIHGITDD FLSDKPSFKD IAKDFFNYIK NSELIIHNAS FDVGFINQEF SMLTKKIQDI
     SNFCNIIDTL KIARKLFPGK KNTLDALCMR YKIKNSHRVL HGAILDAFLL GKLYLLMTSG
     QESIIFNKNI QNERNFRYIK KSITKKHRFL KIIKANKTEL KLHNEYLKFL KEK
//