(data stored in ACNUC7421 zone)

SWISSPROT: 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   11-DEC-2019, entry version 87.
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:11130,
CC         Rhea:RHEA-COMP:11131, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC         ChEBI:CHEBI:83828; 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}.
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   SMR; P0A1G9; -.
DR   PaxDb; P0A1G9; -.
DR   PRIDE; P0A1G9; -.
DR   EnsemblBacteria; AAL19221; AAL19221; STM0264.
DR   GeneID; 1251782; -.
DR   KEGG; stm:STM0264; -.
DR   PATRIC; fig|99287.12.peg.273; -.
DR   eggNOG; ENOG4107RZZ; Bacteria.
DR   eggNOG; COG0847; LUCA.
DR   HOGENOM; HOG000258616; -.
DR   KO; K02342; -.
DR   OMA; FHVYLNP; -.
DR   PhylomeDB; P0A1G9; -.
DR   BioCyc; SENT99287:STM0264-MONOMER; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0044776; C:DNA polymerase III, core complex; 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;
DR   PRODOM; P0A1G9.
DR   SWISS-2DPAGE; P0A1G9.
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   METAL           12
FT                   /note="Divalent metal cation 1; catalytic"
FT                   /evidence="ECO:0000250"
FT   METAL           12
FT                   /note="Divalent metal cation 2; catalytic"
FT                   /evidence="ECO:0000250"
FT   METAL           14
FT                   /note="Divalent metal cation 1; catalytic"
FT                   /evidence="ECO:0000250"
FT   METAL           167
FT                   /note="Divalent metal cation 1; catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         12
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         14
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         61
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         66
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         167
FT                   /note="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
//

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