(data stored in ACNUC10821 zone)

SWISSPROT: C8U2F6_ECO10

ID   C8U2F6_ECO10            Unreviewed;       643 AA.
AC   C8U2F6;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   16-JAN-2019, entry version 60.
DE   RecName: Full=DNA polymerase III subunit gamma/tau {ECO:0000256|RuleBase:RU364063};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU364063};
GN   Name=dnaX {ECO:0000256|RuleBase:RU364063,
GN   ECO:0000313|EMBL:BAI29314.1};
GN   OrderedLocusNames=ECO103_0446 {ECO:0000313|EMBL:BAI29314.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29314.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29314.1, 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.
CC       This DNA polymerase also exhibits 3' to 5' exonuclease activity.
CC       {ECO:0000256|RuleBase:RU364063}.
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:RU364063};
CC   -!- SUBUNIT: DNA polymerase III contains a core (composed of alpha,
CC       epsilon and theta chains) that associates with a tau subunit. This
CC       core dimerizes to form the POLIII' complex. PolIII' associates
CC       with the gamma complex (composed of gamma, delta, delta', psi and
CC       chi chains) and with the beta chain to form the complete DNA
CC       polymerase III complex. {ECO:0000256|RuleBase:RU364063}.
CC   -!- SIMILARITY: Belongs to the DnaX/STICHEL family.
CC       {ECO:0000256|RuleBase:RU364063}.
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DR   EMBL; AP010958; BAI29314.1; -; Genomic_DNA.
DR   RefSeq; WP_000122008.1; NC_013353.1.
DR   EnsemblBacteria; BAI29314; BAI29314; ECO103_0446.
DR   KEGG; eoh:ECO103_0446; -.
DR   HOGENOM; HOG000083934; -.
DR   KO; K02343; -.
DR   OMA; YALHQGN; -.
DR   BioCyc; ECOL585395:ECO103_RS02335-MONOMER; -.
DR   Proteomes; UP000000959; Chromosome.
DR   GO; GO:0009360; C:DNA polymerase III complex; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.300.150; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR001270; ClpA/B.
DR   InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR   InterPro; IPR022001; DNA_pol3_tau_IV.
DR   InterPro; IPR022754; DNA_pol_III_gamma-3.
DR   InterPro; IPR012763; DNA_pol_III_sug/sutau.
DR   InterPro; IPR021029; DNA_pol_III_tau_dom-5.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038249; PolIII_tau_C_sf.
DR   Pfam; PF12169; DNA_pol3_gamma3; 1.
DR   Pfam; PF12168; DNA_pol3_tau_4; 1.
DR   Pfam; PF12170; DNA_pol3_tau_5; 1.
DR   PRINTS; PR00300; CLPPROTEASEA.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF48019; SSF48019; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR02397; dnaX_nterm; 1.
PE   3: Inferred from homology;
DR   PRODOM; C8U2F6.
DR   SWISS-2DPAGE; C8U2F6.
KW   ATP-binding {ECO:0000256|RuleBase:RU364063};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   DNA replication {ECO:0000256|RuleBase:RU364063};
KW   DNA-directed DNA polymerase {ECO:0000256|RuleBase:RU364063};
KW   Elongation factor {ECO:0000313|EMBL:BAI29314.1};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU364063};
KW   Nucleotidyltransferase {ECO:0000256|RuleBase:RU364063};
KW   Protein biosynthesis {ECO:0000313|EMBL:BAI29314.1};
KW   Transferase {ECO:0000256|RuleBase:RU364063}.
FT   DOMAIN       37    178       AAA. {ECO:0000259|SMART:SM00382}.
SQ   SEQUENCE   643 AA;  71082 MW;  D21E1CF889106141 CRC64;
     MSYQVLARKW RPQTFADVVG QEHVLTALAN GLSLGRIHHA YLFSGTRGVG KTSIARLLAK
     GLNCETGITA TPCGVCDNCR EIEQGRFVDL IEIDAASRTK VEDTRDLLDN VQYAPARGRF
     KVYLIDEVHM LSRHSFNALL KTLEEPPEHV KFLLATTDPQ KLPVTILSRC LQFHLKALDV
     EQIRHQLEHI LNEEHIAHEP RALQLLARAA EGSLRDALSL TDQAIASGDG QVSTQAVSAM
     LGTLDDDQAL SLVEAMVEAN GERVMALINE AAARGIEWEA LLVEMLGLLH RIAMVQLSPA
     ALGNDMAAIE LRMRELARTI PPTDIQLYYQ TLLIGRKELP YAPDRRMGVE MTLLRALAFH
     PRMPLPEPEV PRQSFAPVAP TAVMTPTQVP PQPQSAPQQA PTVPLPETTS QVLAARQQLQ
     RVQGATKAKK SEPAAATRAR PVNNAALERL ASVTDRVQAR PVPSALEKAP AKKEAYRWKA
     TTPVMQQKEV VATPKALKKA LEHEKTPELA AKLAAEAIER DAWAAQVSQL SLPKLVEQVA
     LNAWKEESDN AVCLHLRSSQ RHLNNRGAQQ KLAEALSTLK GSTVELTIVE DDNPAVRTPL
     EWRQAIYEEK LAQARESIIA DNNIQTLRRF FDAELDEESI RPI
//

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