ID   DPO3B_MYCBO             Reviewed;         402 AA.
AC   O33914; A0A1R3XU10; X2BDQ9;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2003, sequence version 2.
DT   25-MAY-2022, entry version 112.
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=BQ2027_MB0002;
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=233413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA   Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA   Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA   Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA   Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA   Robbe-Austerman S., Gordon S.V.;
RT   "Updated reference genome sequence and annotation of Mycobacterium bovis
RT   AF2122/97.";
RL   Genome Announc. 5:E00157-E00157(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-58.
RC   STRAIN=BCG;
RA   Qin M., Zachariah S., Madiraju M.V.V.S., Rajagopalan M.;
RL   Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
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; LT708304; SIT98337.1; -; Genomic_DNA.
DR   EMBL; U75298; AAB81129.1; -; Genomic_DNA.
DR   RefSeq; NP_853672.1; NC_002945.3.
DR   RefSeq; WP_010950321.1; NC_002945.4.
DR   AlphaFoldDB; O33914; -.
DR   SMR; O33914; -.
DR   EnsemblBacteria; SIT98337; SIT98337; BQ2027_MB0002.
DR   PATRIC; fig|233413.5.peg.2; -.
DR   OMA; YLIMPVR; -.
DR   Proteomes; UP000001419; 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..402
FT                   /note="Beta sliding clamp"
FT                   /id="PRO_0000105443"
SQ   SEQUENCE   402 AA;  42055 MW;  830900921E3E03BE CRC64;
     MDAATTRVGL TDLTFRLLRE SFADAVSWVA KNLPARPAVP VLSGVLLTGS DNGLTISGFD
     YEVSAEAQVG AEIVSPGSVL VSGRLLSDIT RALPNKPVGV HVEGNRVALT CGNARFSLPT
     MPVEDYPTLP TLPEETGLLP AELFAEAISQ VAIAAGRDDT LPMLTGIRVE ILGETVVLAA
     TDRFRLAVRE LKWSASSPDI EAAVLVPAKT LAEAAKAGIG GSDVRLSLGT GPGVGKDGLL
     GISGNGKRST TRLLDAEFPK FRQLLPTEHT AVATMDVAEL IEAIKLVALV ADRGAQVRME
     FADGSVRLSA GADDVGRAEE DLVVDYAGEP LTIAFNPTYL TDGLSSLRSE RVSFGFTTAG
     KPALLRPVSG DDRPVAGLNG NGPFPAVSTD YVYLLMPVRL PG