(data stored in ACNUC7421 zone)

SWISSPROT: B7UJB1_ECO27

ID   B7UJB1_ECO27            Unreviewed;       243 AA.
AC   B7UJB1;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   16-JAN-2019, entry version 57.
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:CAS07763.1};
GN   OrderedLocusNames=E2348C_0215 {ECO:0000313|EMBL:CAS07763.1};
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521 {ECO:0000313|EMBL:CAS07763.1, ECO:0000313|Proteomes:UP000008205};
RN   [1] {ECO:0000313|EMBL:CAS07763.1, ECO:0000313|Proteomes:UP000008205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC {ECO:0000313|Proteomes:UP000008205};
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(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; FM180568; CAS07763.1; -; Genomic_DNA.
DR   RefSeq; WP_001339270.1; NC_011601.1.
DR   EnsemblBacteria; CAS07763; CAS07763; E2348C_0215.
DR   KEGG; ecg:E2348C_0215; -.
DR   HOGENOM; HOG000258616; -.
DR   KO; K02342; -.
DR   OMA; FHVYLNP; -.
DR   BioCyc; ECOL574521:E2348C_RS01135-MONOMER; -.
DR   Proteomes; UP000008205; 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; B7UJB1.
DR   SWISS-2DPAGE; B7UJB1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000008205};
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;  27143 MW;  AC1079A01C478BFF CRC64;
     MSTAITRQIV LDTETTGMNQ IGAHYEGHKI IEIGAVEVVN RRLTGNNFHV YLKPDRLVDP
     EAFGVHGIAD EFLLDKPTFA EVADEFMDYI RGAELVIHNA TFDIGFMDYE FSLLKRDIPK
     TNTFCKVTDS LAVARKMFPG KRNSLDALCA RYEIDNSKRT LHGALLDAQI LAEVYLAMTG
     GQTSMAFAME GETQQQQGEA TIQRIVRQAS KLRVVFATDE ELAAHEARLD LVQKKGGTCL
     WRA
//

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