ID   DPO3E_PASMU             Reviewed;         253 AA.
AC   Q9CPE0;
DT   06-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=DNA polymerase III subunit epsilon;
DE            EC=2.7.7.7;
GN   Name=dnaQ; OrderedLocusNames=PM0106;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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: DNA polymerase III contains a core (composed of alpha, epsilon
CC       and theta chains) that associates with a tau subunit. This core
CC       dimerizes to form the POLIII' complex. PolIII' associates with the
CC       gamma complex (composed of gamma, delta, delta', psi and chi chains)
CC       and with the beta chain to form the complete DNA polymerase III complex
CC       (By similarity). {ECO:0000250}.
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DR   EMBL; AE004439; AAK02190.1; -; Genomic_DNA.
DR   RefSeq; WP_005753391.1; NC_002663.1.
DR   AlphaFoldDB; Q9CPE0; -.
DR   SMR; Q9CPE0; -.
DR   STRING; 747.DR93_1964; -.
DR   EnsemblBacteria; AAK02190; AAK02190; PM0106.
DR   KEGG; pmu:PM0106; -.
DR   PATRIC; fig|272843.6.peg.110; -.
DR   HOGENOM; CLU_047806_2_0_6; -.
DR   OMA; FHVYLNP; -.
DR   Proteomes; UP000000809; 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..253
FT                   /note="DNA polymerase III subunit epsilon"
FT                   /id="PRO_0000105487"
FT   ACT_SITE        163
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         14
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         14
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         14
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         16
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         16
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         63
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         68
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         168
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         168
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   253 AA;  28560 MW;  AEF3C48030D4B64C CRC64;
     MTPVNQPTRQ IVLDTETTGM NQFGAHYEGH CIIEIGAVEM INRRLTGNNF HIYIKPNRPV
     DPDAIKVHGI TDEMLADKPM FNEVAQQFID YIQGAELLIH NAPFDVGFMD YEFKKLNLNI
     NTDAICMVTD TLQMARQMYP GKRNSLDALC DRLGIDNSKR TLHGALLDAE ILADVYLTMT
     GGQTSLFDEN EPEIAVVAVQ EQIQSAVAFS QDLKRLQPNA DELQAHLDYL LLLNKKSKGN
     CLWEKRLAEL KTH