ID   DPO3B_SALTY             Reviewed;         366 AA.
AC   P26464; O50240;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 3.
DT   03-AUG-2022, entry version 125.
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=STM3837;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=LT2;
RA   Amini F., Blinkova A., Walker J.R.;
RL   Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-62.
RX   PubMed=3040670; DOI=10.1128/jb.169.9.3976-3981.1987;
RA   Skovgaard O., Hansen F.G.;
RT   "Comparison of dnaA nucleotide sequences of Escherichia coli, Salmonella
RT   typhimurium, and Serratia marcescens.";
RL   J. Bacteriol. 169:3976-3981(1987).
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; AF034747; AAB87631.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL22696.1; -; Genomic_DNA.
DR   EMBL; M17352; AAA02816.1; -; Unassigned_DNA.
DR   RefSeq; NP_462737.1; NC_003197.2.
DR   RefSeq; WP_000673478.1; NC_003197.2.
DR   AlphaFoldDB; P26464; -.
DR   SMR; P26464; -.
DR   STRING; 99287.STM3837; -.
DR   PaxDb; P26464; -.
DR   PRIDE; P26464; -.
DR   EnsemblBacteria; AAL22696; AAL22696; STM3837.
DR   GeneID; 1255364; -.
DR   KEGG; stm:STM3837; -.
DR   PATRIC; fig|99287.12.peg.4064; -.
DR   HOGENOM; CLU_038149_4_2_6; -.
DR   OMA; YLIMPVR; -.
DR   PhylomeDB; P26464; -.
DR   BioCyc; SENT99287:STM3837-MON; -.
DR   Proteomes; UP000001014; 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:0006271; P:DNA strand elongation involved in DNA replication; IBA:GO_Central.
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; Reference proteome; Transferase.
FT   CHAIN           1..366
FT                   /note="Beta sliding clamp"
FT                   /id="PRO_0000105459"
FT   CONFLICT        41
FT                   /note="T -> A (in Ref. 3; AAA02816)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   366 AA;  40548 MW;  575FD8F13D928742 CRC64;
     MKFTVEREHL LKPLQQVSGP LGGRPTLPIL GNLLLQVADG TLSLTGTDLE MEMVARVTLS
     QPHEPGATTV PARKFFDICR GLPEGAEIAV QLEGDRMLVR SGRSRFSLST LPAADFPNLD
     DWQSEVEFTL PQATMKRLIE STQFSMAHQD VRYYLNGMLF ETEGSELRTV ATDGHRLAVC
     SMPLEASLPS HSVIVPRKGV IELMRMLDGG ENPLRVQIGS NNIRAHVGDF IFTSKLVDGR
     FPDYRRVLPK NPDKHLEAGC DILKQAFARA AILSNEKFRG VRLYVSENQL KITANNPEQE
     EAEEILDVSY GGTEMEIGFN VSYVLDVLNA LKCETVRIML TDSVSSVQIE DAASQSAAYV
     VMPMRL