ID   DPO3B_STAES             Reviewed;         377 AA.
AC   Q8CQK6;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 101.
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=SE_0002;
OS   Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12228 / FDA PCI 1200;
RX   PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA   Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA   Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA   Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT   "Genome-based analysis of virulence genes in a non-biofilm-forming
RT   Staphylococcus epidermidis strain (ATCC 12228).";
RL   Mol. Microbiol. 49:1577-1593(2003).
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; AE015929; AAO03599.1; -; Genomic_DNA.
DR   RefSeq; NP_763557.1; NC_004461.1.
DR   RefSeq; WP_001831813.1; NZ_WBME01000012.1.
DR   AlphaFoldDB; Q8CQK6; -.
DR   SMR; Q8CQK6; -.
DR   STRING; 176280.SE_0002; -.
DR   EnsemblBacteria; AAO03599; AAO03599; SE_0002.
DR   GeneID; 50017416; -.
DR   KEGG; sep:SE_0002; -.
DR   PATRIC; fig|176280.10.peg.2; -.
DR   eggNOG; COG0592; Bacteria.
DR   HOGENOM; CLU_038149_2_0_9; -.
DR   OMA; YLIMPVR; -.
DR   Proteomes; UP000001411; 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..377
FT                   /note="Beta sliding clamp"
FT                   /id="PRO_0000105469"
SQ   SEQUENCE   377 AA;  42102 MW;  4188F2AFFD3BCBDD CRC64;
     MMEFTIKRDY FINQLNDTLK AISPRTTLPI LTGIKIDAKE NEVILTGSDS EISIEITIPK
     QVDGEEIVEI TETGSVVLPG RFFVDIIKKL PGKEVKLSTN EQFQTLITSG HSEFNLSGLD
     PDQYPLLPEV SRDDAIQLSV KVLKNIIAQT NFAVSTSETR PVLTGVNWLI QDNELICTAT
     DSHRLAVRKL QLEDESENKN VIIPGKALSE LNKIMSDSDE DIDIFFASNQ VLFRVGNINF
     ISRLLEGHYP DTTRLFPENY EIKLGINNGD FYHAIDRASL LAREGGNNVI KLSTGNELVE
     LSSTSPEIGT VKEEVNANDV EGGNLKISFN SKYMMDALKA IDNDEVEVEF FGTMKPFILK
     PKDDDSVTQL ILPIRTY