ID   DPO3B_PSEPU             Reviewed;         367 AA.
AC   P0A121; P13455;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 66.
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;
OS   Pseudomonas putida (Arthrobacter siderocapsulatus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=TN2100;
RX   PubMed=2540413; DOI=10.1007/bf00427033;
RA   Fujita M.Q., Yoshikawa H., Ogasawara N.;
RT   "Structure of the dnaA region of Pseudomonas putida: conservation among
RT   three bacteria, Bacillus subtilis, Escherichia coli and P. putida.";
RL   Mol. Gen. Genet. 215:381-387(1989).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X14791; CAA32894.1; -; Genomic_DNA.
DR   PIR; JV0002; DJPS3P.
DR   RefSeq; WP_003253156.1; NZ_SPUU01000003.1.
DR   AlphaFoldDB; P0A121; -.
DR   SMR; P0A121; -.
DR   STRING; 1240350.AMZE01000066_gene3195; -.
DR   PATRIC; fig|303.175.peg.35; -.
DR   eggNOG; COG0592; Bacteria.
DR   OMA; YLIMPVR; -.
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..367
FT                   /note="Beta sliding clamp"
FT                   /id="PRO_0000105455"
SQ   SEQUENCE   367 AA;  40719 MW;  FE65ABBAD685FEAD CRC64;
     MHFTIQREAL LKPLQLVAGV VERRQTLPVL SNVLLVVQGQ QLSLTGTDLE VELVGRVQLE
     EPAEPGEITV PARKLMDICK SLPNDALIDI KVDEQKLLVK AGRSRFTLST LPANDFPTVE
     EGPGSLTCNL EQSKLRRLIE RTSFAMAQQD VRYYLNGMLL EVSRNTLRAV STDGHRLALC
     SMSAPIEQED RHQVIVPRKG ILELARLLTD PEGMVSIVLG QHHIRATTGE FTFTSKLVDG
     KFPDYERVLP KGGDKLVVGD RQALREAFSR TAILSNEKYR GIRLQLAAGQ LKIQANNPEQ
     EEAEEEISVD YEGSSLEIGF NVSYLLDVLG VMTTEQVRLI LSDSNSSALL QEAGNDDSSY
     VVMPMRL