DPO3E_SALTY
ID DPO3E_SALTY Reviewed; 243 AA.
AC P0A1G9; P14566; Q56055;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=DNA polymerase III subunit epsilon;
DE EC=2.7.7.7;
GN Name=dnaQ; Synonyms=mutD; OrderedLocusNames=STM0264;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
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=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-100 AND 119-132.
RX PubMed=2551891; DOI=10.1128/jb.171.10.5572-5580.1989;
RA Lancy E.D., Lifsics M.R., Kehres D.G., Maurer R.;
RT "Isolation and characterization of mutants with deletions in dnaQ, the gene
RT for the editing subunit of DNA polymerase III in Salmonella typhimurium.";
RL J. Bacteriol. 171:5572-5580(1989).
CC -!- FUNCTION: DNA polymerase III is a complex, multichain enzyme
CC responsible for most of the replicative synthesis in bacteria. The
CC epsilon subunit contains 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; U44090; AAA86422.1; -; Genomic_DNA.
DR EMBL; U77465; AAC44792.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL19221.1; -; Genomic_DNA.
DR EMBL; M26045; AAA27192.2; -; Genomic_DNA.
DR RefSeq; NP_459262.1; NC_003197.2.
DR RefSeq; WP_001670675.1; NC_003197.2.
DR AlphaFoldDB; P0A1G9; -.
DR SMR; P0A1G9; -.
DR STRING; 99287.STM0264; -.
DR PaxDb; P0A1G9; -.
DR EnsemblBacteria; AAL19221; AAL19221; STM0264.
DR GeneID; 1251782; -.
DR KEGG; stm:STM0264; -.
DR PATRIC; fig|99287.12.peg.273; -.
DR HOGENOM; CLU_047806_2_0_6; -.
DR OMA; FHVYLNP; -.
DR PhylomeDB; P0A1G9; -.
DR BioCyc; SENT99287:STM0264-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IBA:GO_Central.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045004; P:DNA replication proofreading; IBA:GO_Central.
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..243
FT /note="DNA polymerase III subunit epsilon"
FT /id="PRO_0000105485"
FT ACT_SITE 162
FT /note="Proton acceptor"
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="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 12
FT /ligand="substrate"
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="substrate"
FT /evidence="ECO:0000250"
FT BINDING 61
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 66
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 167
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 167
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 243 AA; 27225 MW; 25B51587B5DDEA83 CRC64;
MSTAITRQIV LDTETTGMNQ IGAHYEGHKI IEIGAVEVIN RRLTGNNFHV YLKPDRLVDP
EAFGVHGIAD EFLLDKPVFA DVVDEFLDYI RGAELVIHNA SFDIGFMDYE FGLLKRDIPK
TNTFCKVTDS LALARKMFPG KRNSLDALCS RYEIDNSKRT LHGALLDAQI LAEVYLAMTG
GQTSMTFAME GETQRQQGEA TIQRIVRQAS RLRVVFASEE ELAAHESRLD LVQKKGGSCL
WRA
