(data stored in SCRATCH zone)

SWISSPROT: Q47TU0_THEFY

ID   Q47TU0_THEFY            Unreviewed;       379 AA.
AC   Q47TU0;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 105.
DE   RecName: Full=Beta sliding clamp {ECO:0000256|PIRNR:PIRNR000804};
GN   OrderedLocusNames=Tfu_0086 {ECO:0000313|EMBL:AAZ54124.1};
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ54124.1, ECO:0000313|Proteomes:UP000000434};
RN   [1] {ECO:0000313|Proteomes:UP000000434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YX {ECO:0000313|Proteomes:UP000000434};
RX   PubMed=17209016; DOI=10.1128/JB.01899-06;
RA   Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M.,
RA   DiBartolo G., Martinez M., Lapidus A., Lucas S., Copeland A.,
RA   Richardson P., Wilson D.B., Kyrpides N.;
RT   "Genome sequence and analysis of the soil cellulolytic actinomycete
RT   Thermobifida fusca YX.";
RL   J. Bacteriol. 189:2477-2486(2007).
CC   -!- FUNCTION: Confers DNA tethering and processivity to DNA
CC       polymerases and other proteins. Acts as a clamp, forming a ring
CC       around DNA (a reaction catalyzed by the clamp-loading complex)
CC       which diffuses in an ATP-independent manner freely and
CC       bidirectionally along dsDNA. Initially characterized for its
CC       ability to contact the catalytic subunit of DNA polymerase III
CC       (Pol III), a complex, multichain enzyme responsible for most of
CC       the replicative synthesis in bacteria; Pol III exhibits 3'-5'
CC       exonuclease proofreading activity. The beta chain is required for
CC       initiation of replication as well as for processivity of DNA
CC       replication. {ECO:0000256|PIRNR:PIRNR000804}.
CC   -!- SUBUNIT: Forms a ring-shaped head-to-tail homodimer around DNA.
CC       {ECO:0000256|PIRNR:PIRNR000804}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR000804,
CC       ECO:0000256|SAAS:SAAS00729396}.
CC   -!- SIMILARITY: Belongs to the beta sliding clamp family.
CC       {ECO:0000256|PIRNR:PIRNR000804, ECO:0000256|SAAS:SAAS00859809}.
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DR   EMBL; CP000088; AAZ54124.1; -; Genomic_DNA.
DR   RefSeq; WP_011290533.1; NC_007333.1.
DR   STRING; 269800.Tfu_0086; -.
DR   DNASU; 3579721; -.
DR   EnsemblBacteria; AAZ54124; AAZ54124; Tfu_0086.
DR   KEGG; tfu:Tfu_0086; -.
DR   eggNOG; ENOG4105CZ8; Bacteria.
DR   eggNOG; COG0592; LUCA.
DR   HOGENOM; HOG000071793; -.
DR   KO; K02338; -.
DR   OMA; DRNIFFE; -.
DR   OrthoDB; 1040142at2; -.
DR   BioCyc; TFUS269800:G1G4Q-87-MONOMER; -.
DR   Proteomes; UP000000434; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0009360; C:DNA polymerase III complex; IEA:InterPro.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR   CDD; cd00140; beta_clamp; 1.
DR   InterPro; IPR001001; DNA_polIII_beta.
DR   InterPro; IPR022635; DNA_polIII_beta_C.
DR   InterPro; IPR022637; DNA_polIII_beta_cen.
DR   InterPro; IPR022634; DNA_polIII_beta_N.
DR   PANTHER; PTHR30478; PTHR30478; 1.
DR   Pfam; PF00712; DNA_pol3_beta; 1.
DR   Pfam; PF02767; DNA_pol3_beta_2; 1.
DR   Pfam; PF02768; DNA_pol3_beta_3; 1.
DR   PIRSF; PIRSF000804; DNA_pol_III_b; 1.
DR   SMART; SM00480; POL3Bc; 1.
DR   TIGRFAMs; TIGR00663; dnan; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q47TU0.
DR   SWISS-2DPAGE; Q47TU0.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000434};
KW   Cytoplasm {ECO:0000256|PIRNR:PIRNR000804,
KW   ECO:0000256|SAAS:SAAS00729481};
KW   DNA replication {ECO:0000256|PIRNR:PIRNR000804,
KW   ECO:0000256|SAAS:SAAS00729460};
KW   DNA-binding {ECO:0000256|SAAS:SAAS00859811};
KW   DNA-directed DNA polymerase {ECO:0000256|PIRNR:PIRNR000804,
KW   ECO:0000256|SAAS:SAAS00729479};
KW   Nucleotidyltransferase {ECO:0000256|PIRNR:PIRNR000804,
KW   ECO:0000256|SAAS:SAAS00729386};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000434};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000804,
KW   ECO:0000256|SAAS:SAAS00729371}.
FT   DOMAIN        1    121       DNA_pol3_beta. {ECO:0000259|Pfam:
FT                                PF00712}.
FT   DOMAIN      131    249       DNA_pol3_beta_2. {ECO:0000259|Pfam:
FT                                PF02767}.
FT   DOMAIN      256    377       DNA_pol3_beta_3. {ECO:0000259|Pfam:
FT                                PF02768}.
SQ   SEQUENCE   379 AA;  41089 MW;  2EBA0798C13D95B8 CRC64;
     MKFRVDRDAF ADAVTWTARA LPARPAVPVL AGMRLEVADT ASDTLRLSGF DYEVSAQASV
     DVHAEEAGSV LVPGRLLAEI VRTLPPHPVE FHVEGSRALL TCGNARFTLL TLPLEDYPTL
     PAMPRTIGSA PADVFATAVR QVLPSTSRDD TLPMLTGVHL TFRGDTILLA ATDRYRIAVR
     EMWWKPEEVD IDTSALVPAR TLGDFSRSLT GGNVDIALST SDSRGAGEGM IGFEHDGKRT
     TTRLIDSDFV SYESRFPTEF AAQADVPVAP LAEAVKRVAL VADRSTPVRL SFTSSEVVLE
     AGSGDDAQAL EALEVNFEGE PMRIAFNPQY FLDGLTNVET ERAFLRFVAP TRPAVITGTP
     AKEGGKPDFR YLVMPLRLA
//

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