DPO3B_BORBU
ID DPO3B_BORBU Reviewed; 385 AA.
AC P33761; O51397;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 25-MAY-2022, entry version 121.
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=BB_0438;
OS Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS (Borrelia burgdorferi).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX NCBI_TaxID=224326;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=212;
RX PubMed=8341609; DOI=10.1093/nar/21.14.3323;
RA Old I.G., Margarita D., Saint-Girons I.;
RT "Nucleotide sequence of the Borrelia burgdorferi dnaN gene encoding the
RT beta subunit of DNA polymerase III.";
RL Nucleic Acids Res. 21:3323-3323(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX PubMed=9403685; DOI=10.1038/37551;
RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA Smith H.O., Venter J.C.;
RT "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL Nature 390:580-586(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
RC STRAIN=212;
RX PubMed=8359672; DOI=10.1111/j.1574-6968.1993.tb06369.x;
RA Old I.G., Margarita D., Saint-Girons I.;
RT "Unique genetic arrangement in the dnaA region of the Borrelia burgdorferi
RT linear chromosome: nucleotide sequence of the dnaA gene.";
RL FEMS Microbiol. Lett. 111:109-114(1993).
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; U04527; AAA58942.1; -; Genomic_DNA.
DR EMBL; AE000783; AAB91514.1; -; Genomic_DNA.
DR PIR; E70154; E70154.
DR RefSeq; NP_212572.1; NC_001318.1.
DR PDB; 6DJ8; X-ray; 2.05 A; A/B=1-385.
DR PDBsum; 6DJ8; -.
DR AlphaFoldDB; P33761; -.
DR SMR; P33761; -.
DR STRING; 224326.BB_0438; -.
DR PRIDE; P33761; -.
DR EnsemblBacteria; AAB91514; AAB91514; BB_0438.
DR GeneID; 56567869; -.
DR KEGG; bbu:BB_0438; -.
DR PATRIC; fig|224326.49.peg.829; -.
DR HOGENOM; CLU_038149_2_1_12; -.
DR OMA; KIACSLI; -.
DR Proteomes; UP000001807; 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 SMART; SM00480; POL3Bc; 1.
DR TIGRFAMs; TIGR00663; dnan; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; DNA replication; DNA-binding;
KW DNA-directed DNA polymerase; Nucleotidyltransferase; Reference proteome;
KW Transferase.
FT CHAIN 1..385
FT /note="Beta sliding clamp"
FT /id="PRO_0000105425"
FT CONFLICT 86
FT /note="N -> S (in Ref. 2; AAB91514)"
FT /evidence="ECO:0000305"
FT HELIX 2..4
FT /evidence="ECO:0007829|PDB:6DJ8"
FT STRAND 5..10
FT /evidence="ECO:0007829|PDB:6DJ8"
FT HELIX 11..21
FT /evidence="ECO:0007829|PDB:6DJ8"
FT HELIX 22..24
FT /evidence="ECO:0007829|PDB:6DJ8"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:6DJ8"
FT STRAND 36..42
FT /evidence="ECO:0007829|PDB:6DJ8"
FT STRAND 45..51
FT /evidence="ECO:0007829|PDB:6DJ8"
FT STRAND 53..62
FT /evidence="ECO:0007829|PDB:6DJ8"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:6DJ8"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:6DJ8"
FT HELIX 75..84
FT /evidence="ECO:0007829|PDB:6DJ8"
FT TURN 85..87
FT /evidence="ECO:0007829|PDB:6DJ8"
FT STRAND 88..96
FT /evidence="ECO:0007829|PDB:6DJ8"
FT TURN 97..100
FT /evidence="ECO:0007829|PDB:6DJ8"
FT STRAND 101..106
FT /evidence="ECO:0007829|PDB:6DJ8"
FT STRAND 118..122
FT /evidence="ECO:0007829|PDB:6DJ8"
FT HELIX 127..132
FT /evidence="ECO:0007829|PDB:6DJ8"
FT STRAND 142..148
FT /evidence="ECO:0007829|PDB:6DJ8"
FT HELIX 149..159
FT /evidence="ECO:0007829|PDB:6DJ8"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:6DJ8"
FT TURN 170..173
FT /evidence="ECO:0007829|PDB:6DJ8"
FT STRAND 174..179
FT /evidence="ECO:0007829|PDB:6DJ8"
FT STRAND 184..190
FT /evidence="ECO:0007829|PDB:6DJ8"
FT STRAND 192..203
FT /evidence="ECO:0007829|PDB:6DJ8"
FT STRAND 210..213
FT /evidence="ECO:0007829|PDB:6DJ8"
FT HELIX 215..223
FT /evidence="ECO:0007829|PDB:6DJ8"
FT STRAND 226..234
FT /evidence="ECO:0007829|PDB:6DJ8"
FT STRAND 236..243
FT /evidence="ECO:0007829|PDB:6DJ8"
FT STRAND 246..251
FT /evidence="ECO:0007829|PDB:6DJ8"
FT HELIX 260..263
FT /evidence="ECO:0007829|PDB:6DJ8"
FT STRAND 269..275
FT /evidence="ECO:0007829|PDB:6DJ8"
FT HELIX 276..286
FT /evidence="ECO:0007829|PDB:6DJ8"
FT HELIX 287..289
FT /evidence="ECO:0007829|PDB:6DJ8"
FT STRAND 295..300
FT /evidence="ECO:0007829|PDB:6DJ8"
FT STRAND 302..310
FT /evidence="ECO:0007829|PDB:6DJ8"
FT TURN 312..314
FT /evidence="ECO:0007829|PDB:6DJ8"
FT STRAND 317..323
FT /evidence="ECO:0007829|PDB:6DJ8"
FT STRAND 326..331
FT /evidence="ECO:0007829|PDB:6DJ8"
FT STRAND 334..339
FT /evidence="ECO:0007829|PDB:6DJ8"
FT HELIX 340..347
FT /evidence="ECO:0007829|PDB:6DJ8"
FT STRAND 352..359
FT /evidence="ECO:0007829|PDB:6DJ8"
FT STRAND 365..368
FT /evidence="ECO:0007829|PDB:6DJ8"
FT STRAND 374..379
FT /evidence="ECO:0007829|PDB:6DJ8"
SQ SEQUENCE 385 AA; 44641 MW; 87CE040D369BD0A5 CRC64;
MLHNTFFICE TNQIMNEIEK AKGIILNRNM NDIWSALLIE VKKSNLIIKS TDRNIFFEST
ISIVSETDFK VLINASNFYD AVKAFNFYKK IKIVFNENNS KLEIMGELND EKEEYEDHLK
EPTFSYEEIE NYNYDMVNED YTFGIEIKQK SFKKVINRIA FSAHLDESKN VLNGVYFSKD
EDSKLLLVST NGHRMSICKT EVIVEEDVNF IVPVKIFNFL KHLMSGEGMV KIKFSDKKFY
VEFDNYKIAC SLINGNYPDY KSIIPKEQKN KSLVSLGILK DRLARVNLYV DKSRKLVLTF
SELQLKLLGE DLITGRKGEF FIKDPNYLYD GADEVMAINI SYFVEAISVF ETSKIEIQFN
SGNVLKLSEP ENFNFTHLIM PMSLG
