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HOLE_SHIFL
ID   HOLE_SHIFL              Reviewed;          76 AA.
AC   P0ABT1; P28689;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=DNA polymerase III subunit theta;
DE            EC=2.7.7.7;
GN   Name=holE; OrderedLocusNames=SF1852.1, S1918;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
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 (By similarity).
CC       {ECO:0000250}.
CC   -!- FUNCTION: The exact function of the theta subunit is unknown.
CC       {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: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] (By similarity). {ECO:0000250}.
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DR   EMBL; AE005674; AAN43412.2; -; Genomic_DNA.
DR   EMBL; AE014073; AAP17234.1; -; Genomic_DNA.
DR   RefSeq; NP_707705.2; NC_004337.2.
DR   RefSeq; WP_000916763.1; NZ_WPGW01000041.1.
DR   AlphaFoldDB; P0ABT1; -.
DR   BMRB; P0ABT1; -.
DR   SMR; P0ABT1; -.
DR   STRING; 198214.SF1853; -.
DR   EnsemblBacteria; AAN43412; AAN43412; SF1853.
DR   EnsemblBacteria; AAP17234; AAP17234; S1918.
DR   GeneID; 1023376; -.
DR   GeneID; 66674268; -.
DR   KEGG; sfl:SF1853; -.
DR   KEGG; sfx:S1918; -.
DR   PATRIC; fig|198214.7.peg.2206; -.
DR   HOGENOM; CLU_176900_0_0_6; -.
DR   OMA; FRERYNM; -.
DR   OrthoDB; 1980210at2; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; 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:0006260; P:DNA replication; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   DNA replication; DNA-directed DNA polymerase; Nucleotidyltransferase;
KW   Reference proteome; Transferase.
FT   CHAIN           1..76
FT                   /note="DNA polymerase III subunit theta"
FT                   /id="PRO_0000105525"
SQ   SEQUENCE   76 AA;  8846 MW;  3667D87327E96556 CRC64;
     MLKNLAKLDQ TEMDKVNVDL AAAGVAFKER YNMPVIAEAV EREQPEHLRS WFRERLIAHR
     LASVNLSRLP YEPKLK
 
 
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