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DPO3B_RICFE
ID   DPO3B_RICFE             Reviewed;         379 AA.
AC   Q4ULS3;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Beta sliding clamp;
DE            Short=Beta clamp;
DE            Short=Sliding clamp;
DE   AltName: Full=Beta-clamp processivity factor;
DE   AltName: Full=DNA polymerase III beta sliding clamp subunit;
DE   AltName: Full=DNA polymerase III subunit beta;
GN   Name=dnaN; OrderedLocusNames=RF_0649;
OS   Rickettsia felis (strain ATCC VR-1525 / URRWXCal2) (Rickettsia azadi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=315456;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-1525 / URRWXCal2;
RX   PubMed=15984913; DOI=10.1371/journal.pbio.0030248;
RA   Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E.,
RA   Parinello H., Claverie J.-M., Raoult D.;
RT   "The genome sequence of Rickettsia felis identifies the first putative
RT   conjugative plasmid in an obligate intracellular parasite.";
RL   PLoS Biol. 3:1-12(2005).
CC   -!- FUNCTION: Confers DNA tethering and processivity to DNA polymerases and
CC       other proteins. Acts as a clamp, forming a ring around DNA (a reaction
CC       catalyzed by the clamp-loading complex) which diffuses in an ATP-
CC       independent manner freely and bidirectionally along dsDNA. Initially
CC       characterized for its ability to contact the catalytic subunit of DNA
CC       polymerase III (Pol III), a complex, multichain enzyme responsible for
CC       most of 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:0000250|UniProtKB:P0A988}.
CC   -!- SUBUNIT: Forms a ring-shaped head-to-tail homodimer around DNA which
CC       binds and tethers DNA polymerases and other proteins to the DNA. The
CC       DNA replisome complex has a single clamp-loading complex (3 tau and 1
CC       each of delta, delta', psi and chi subunits) which binds 3 Pol III
CC       cores (1 core on the leading strand and 2 on the lagging strand) each
CC       with a beta sliding clamp dimer. Additional proteins in the replisome
CC       are other copies of gamma, psi and chi, Ssb, DNA helicase and RNA
CC       primase. {ECO:0000250|UniProtKB:P0A988}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0A988}.
CC   -!- SIMILARITY: Belongs to the beta sliding clamp family. {ECO:0000305}.
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DR   EMBL; CP000053; AAY61500.1; -; Genomic_DNA.
DR   RefSeq; WP_011270979.1; NC_007109.1.
DR   AlphaFoldDB; Q4ULS3; -.
DR   SMR; Q4ULS3; -.
DR   STRING; 315456.RF_0649; -.
DR   EnsemblBacteria; AAY61500; AAY61500; RF_0649.
DR   KEGG; rfe:RF_0649; -.
DR   eggNOG; COG0592; Bacteria.
DR   HOGENOM; CLU_038149_4_2_5; -.
DR   OMA; YLIMPVR; -.
DR   OrthoDB; 1040142at2; -.
DR   Proteomes; UP000008548; 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-KW.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
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;
KW   Cytoplasm; DNA replication; DNA-binding; DNA-directed DNA polymerase;
KW   Nucleotidyltransferase; Transferase.
FT   CHAIN           1..379
FT                   /note="Beta sliding clamp"
FT                   /id="PRO_0000280791"
SQ   SEQUENCE   379 AA;  42265 MW;  F37B275460DE1F79 CRC64;
     MLKLIVETKT LVQSLGFASS VVEKRNVIPE YANIKLSAKD GNLELSSTNM DLYLSQKIAV
     QVVSEGELTV STKTLNDIVR KLPDSELTLT DLGTTGLEIK GKNCKFNLFT LPVSSFPPMD
     SINPEASFKI SCTDFAKIIE STKFSISLDE TRYNLNGVYL HIKDKEFCSA STDGHRLSIS
     WVTLEKQIKN FGVILPQKSA EEILKIVKDP KNINEDIEIL LSSNKIKFIC NENTIMLSKL
     IDGTFPDYSA FIPESSSSKL VINRKIFADS IERIAIITVE KFRAVKLSLS RETLEISAVG
     EARGNAKEVI NSSQDKESFY EYNSDESLAI GFNPQYLEDV LKAVKSDLVE LYFSDVSAPV
     LIKFPENPKD IFVVMPVKV
 
 
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