(data stored in ACNUC10821 zone)

SWISSPROT: C8U1S7_ECO10

ID   C8U1S7_ECO10            Unreviewed;       243 AA.
AC   C8U1S7;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 58.
DE   RecName: Full=DNA polymerase III subunit epsilon {ECO:0000256|RuleBase:RU364087};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU364087};
GN   Name=dnaQ {ECO:0000256|RuleBase:RU364087,
GN   ECO:0000313|EMBL:BAI29085.1};
GN   OrderedLocusNames=ECO103_0209 {ECO:0000313|EMBL:BAI29085.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29085.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29085.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
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
CC       3'-5' exonuclease. {ECO:0000256|RuleBase:RU364087}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC         diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-
CC         COMP:11130, Rhea:RHEA-COMP:11131, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:61560, ChEBI:CHEBI:83828; EC=2.7.7.7;
CC         Evidence={ECO:0000256|RuleBase:RU364087};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU364087};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|RuleBase:RU364087};
CC   -!- SUBUNIT: The DNA polymerase holoenzyme is a complex that contains
CC       10 different types of subunits. These subunits are organized into
CC       3 functionally essential subassemblies: the pol III core, the beta
CC       sliding clamp processivity factor and the clamp-loading complex.
CC       The pol III core (subunits alpha,epsilon and theta) contains the
CC       polymerase and the 3'-5' exonuclease proofreading activities. The
CC       polymerase is tethered to the template via the sliding clamp
CC       processivity factor. The clamp-loading complex assembles the beta
CC       processivity factor onto the primer template and plays a central
CC       role in the organization and communication at the replication
CC       fork. This complex contains delta, delta', psi and chi, and copies
CC       of either or both of two different DnaX proteins, gamma and tau.
CC       {ECO:0000256|RuleBase:RU364087}.
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DR   EMBL; AP010958; BAI29085.1; -; Genomic_DNA.
DR   RefSeq; WP_001297205.1; NC_013353.1.
DR   EnsemblBacteria; BAI29085; BAI29085; ECO103_0209.
DR   KEGG; eoh:ECO103_0209; -.
DR   HOGENOM; HOG000258616; -.
DR   KO; K02342; -.
DR   OMA; FHVYLNP; -.
DR   BioCyc; ECOL585395:ECO103_RS01095-MONOMER; -.
DR   Proteomes; UP000000959; 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   4: Predicted;
DR   PRODOM; C8U1S7.
DR   SWISS-2DPAGE; C8U1S7.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   DNA replication {ECO:0000256|RuleBase:RU364087};
KW   DNA-directed DNA polymerase {ECO:0000256|RuleBase:RU364087};
KW   Exonuclease {ECO:0000256|RuleBase:RU364087};
KW   Hydrolase {ECO:0000256|RuleBase:RU364087};
KW   Magnesium {ECO:0000256|RuleBase:RU364087};
KW   Manganese {ECO:0000256|RuleBase:RU364087};
KW   Metal-binding {ECO:0000256|RuleBase:RU364087};
KW   Nuclease {ECO:0000256|RuleBase:RU364087};
KW   Nucleotidyltransferase {ECO:0000256|RuleBase:RU364087};
KW   Transferase {ECO:0000256|RuleBase:RU364087}.
FT   DOMAIN        7    184       Exonuclease. {ECO:0000259|SMART:SM00479}.
SQ   SEQUENCE   243 AA;  27100 MW;  4211D8E4074220FF CRC64;
     MSTAITRQIV LDTETTGMNQ IGAHYEGHKI IEIGAVEVVN RRLTGNNFHV YLKPDRLVDP
     EAFGVHGIAD EFLLDKPTFA EVADEFMDYI RGAELVIHNA AFDIGFMDYE FSLLKRDIPK
     TNTFCKVTDS LAVARKMFPG KRNSLDALCA RYEIDNSKRT LHGALLDAQI LAEVYLAMTG
     GQTSMAFAME GETQQQQGEA TIQRIVRQAS KLRVVFATDE ELAAHEARLD LVEKKGGSCL
     WRA
//

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