HOLE_ECOLI
ID HOLE_ECOLI Reviewed; 76 AA.
AC P0ABS8; P28689;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=DNA polymerase III subunit theta;
DE EC=2.7.7.7;
GN Name=holE; OrderedLocusNames=b1842, JW1831;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=8505306; DOI=10.1016/s0021-9258(19)50268-x;
RA Studwell-Vaughan P.S., O'Donnell M.;
RT "DNA polymerase III accessory proteins. V. Theta encoded by holE.";
RL J. Biol. Chem. 268:11785-11791(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-23; 44-49 AND
RP 69-73.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8341603; DOI=10.1093/nar/21.14.3281;
RA Carter J.R., Franden M.A., Aebersold R.H., Kim D.R., McHenry C.S.;
RT "Isolation, sequencing and overexpression of the gene encoding the theta
RT subunit of DNA polymerase III holoenzyme.";
RL Nucleic Acids Res. 21:3281-3286(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP REVIEW.
RX PubMed=1575709; DOI=10.1002/bies.950140206;
RA O'Donnell M.;
RT "Accessory protein function in the DNA polymerase III holoenzyme from E.
RT coli.";
RL Bioessays 14:105-111(1992).
CC -!- FUNCTION: DNA polymerase III is a complex, multichain enzyme
CC responsible for most of the replicative synthesis in bacteria. This DNA
CC polymerase also exhibits 3' to 5' exonuclease activity.
CC -!- FUNCTION: The exact function of the theta subunit is unknown.
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 -!- 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].
CC -!- INTERACTION:
CC P0ABS8; P03007: dnaQ; NbExp=13; IntAct=EBI-549182, EBI-549131;
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DR EMBL; L04572; AAA23697.1; -; Genomic_DNA.
DR EMBL; L05381; AAA23982.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74912.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15650.1; -; Genomic_DNA.
DR PIR; S34951; S34951.
DR RefSeq; NP_416356.1; NC_000913.3.
DR RefSeq; WP_000916763.1; NZ_STEB01000009.1.
DR PDB; 1DU2; NMR; -; A=1-76.
DR PDB; 2AE9; NMR; -; A=1-76.
DR PDB; 2AXD; NMR; -; S=1-76.
DR PDB; 2XY8; NMR; -; B=1-76.
DR PDB; 5M1S; EM; 6.70 A; F=10-65.
DR PDBsum; 1DU2; -.
DR PDBsum; 2AE9; -.
DR PDBsum; 2AXD; -.
DR PDBsum; 2XY8; -.
DR PDBsum; 5M1S; -.
DR AlphaFoldDB; P0ABS8; -.
DR BMRB; P0ABS8; -.
DR SMR; P0ABS8; -.
DR BioGRID; 4260361; 41.
DR BioGRID; 851789; 1.
DR ComplexPortal; CPX-1925; DNA polymerase III core complex.
DR DIP; DIP-39982N; -.
DR IntAct; P0ABS8; 29.
DR MINT; P0ABS8; -.
DR STRING; 511145.b1842; -.
DR jPOST; P0ABS8; -.
DR PaxDb; P0ABS8; -.
DR PRIDE; P0ABS8; -.
DR EnsemblBacteria; AAC74912; AAC74912; b1842.
DR EnsemblBacteria; BAA15650; BAA15650; BAA15650.
DR GeneID; 66674268; -.
DR GeneID; 947471; -.
DR KEGG; ecj:JW1831; -.
DR KEGG; eco:b1842; -.
DR PATRIC; fig|511145.12.peg.1920; -.
DR EchoBASE; EB1468; -.
DR eggNOG; ENOG5032S2T; Bacteria.
DR HOGENOM; CLU_176900_0_0_6; -.
DR OMA; FRERYNM; -.
DR PhylomeDB; P0ABS8; -.
DR BioCyc; EcoCyc:EG11505-MON; -.
DR BioCyc; MetaCyc:EG11505-MON; -.
DR EvolutionaryTrace; P0ABS8; -.
DR PRO; PR:P0ABS8; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0009360; C:DNA polymerase III complex; IC:ComplexPortal.
DR GO; GO:0044776; C:DNA polymerase III, core complex; IDA:EcoCyc.
DR GO; GO:0030894; C:replisome; IC:ComplexPortal.
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:0006261; P:DNA-templated DNA replication; IC:ComplexPortal.
DR GO; GO:0006273; P:lagging strand elongation; IDA:ComplexPortal.
DR GO; GO:0006272; P:leading strand elongation; IDA:ComplexPortal.
DR Gene3D; 1.20.58.250; -; 1.
DR InterPro; IPR009052; DNA_pol_III_theta_bac.
DR InterPro; IPR036745; PolIII_theta_sf.
DR Pfam; PF06440; DNA_pol3_theta; 1.
DR SUPFAM; SSF46575; SSF46575; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; DNA replication;
KW DNA-directed DNA polymerase; Nucleotidyltransferase; Reference proteome;
KW Transferase.
FT CHAIN 1..76
FT /note="DNA polymerase III subunit theta"
FT /id="PRO_0000105522"
FT HELIX 5..8
FT /evidence="ECO:0007829|PDB:2AXD"
FT HELIX 11..21
FT /evidence="ECO:0007829|PDB:1DU2"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:1DU2"
FT HELIX 27..30
FT /evidence="ECO:0007829|PDB:2AXD"
FT HELIX 38..43
FT /evidence="ECO:0007829|PDB:1DU2"
FT HELIX 47..53
FT /evidence="ECO:0007829|PDB:1DU2"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:1DU2"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:1DU2"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:2AE9"
SQ SEQUENCE 76 AA; 8846 MW; 3667D87327E96556 CRC64;
MLKNLAKLDQ TEMDKVNVDL AAAGVAFKER YNMPVIAEAV EREQPEHLRS WFRERLIAHR
LASVNLSRLP YEPKLK
