DPO3B_STRPN
ID DPO3B_STRPN Reviewed; 378 AA.
AC O06672;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 131.
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=SP_0002;
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=R801;
RA Gasc A.A.;
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(2001).
RN [3] {ECO:0007744|PDB:2AWA}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS).
RC STRAIN=ATCC BAA-334 / TIGR4;
RG Joint Center For Structural Genomics (JCSG);
RT "Crystal structure of DNA polymerase III, beta chain (EC 2.7.7.7)
RT (np_344555.1) from Streptococcus pneumoniae TIGR4 at 2.50 A resolution.";
RL Submitted (AUG-2005) to the PDB data bank.
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; AF000658; AAC45337.1; -; Genomic_DNA.
DR EMBL; AE005672; AAK74195.1; -; Genomic_DNA.
DR PIR; B95000; B95000.
DR PIR; B97872; B97872.
DR RefSeq; WP_000581157.1; NZ_AKVY01000001.1.
DR PDB; 2AWA; X-ray; 2.50 A; A/B/C/D=1-378.
DR PDBsum; 2AWA; -.
DR AlphaFoldDB; O06672; -.
DR SMR; O06672; -.
DR STRING; 170187.SP_0002; -.
DR DNASU; 929739; -.
DR EnsemblBacteria; AAK74195; AAK74195; SP_0002.
DR GeneID; 66805162; -.
DR KEGG; spn:SP_0002; -.
DR eggNOG; COG0592; Bacteria.
DR OMA; YLIMPVR; -.
DR PhylomeDB; O06672; -.
DR BioCyc; SPNE170187:G1FZB-2-MON; -.
DR EvolutionaryTrace; O06672; -.
DR Proteomes; UP000000585; 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; DNA replication; DNA-binding;
KW DNA-directed DNA polymerase; Nucleotidyltransferase; Transferase.
FT CHAIN 1..378
FT /note="Beta sliding clamp"
FT /id="PRO_0000105472"
FT CONFLICT 17
FT /note="T -> I (in Ref. 1; AAC45337)"
FT /evidence="ECO:0000305"
FT CONFLICT 43
FT /note="I -> V (in Ref. 1; AAC45337)"
FT /evidence="ECO:0000305"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:2AWA"
FT HELIX 8..18
FT /evidence="ECO:0007829|PDB:2AWA"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:2AWA"
FT HELIX 29..32
FT /evidence="ECO:0007829|PDB:2AWA"
FT STRAND 33..38
FT /evidence="ECO:0007829|PDB:2AWA"
FT STRAND 40..48
FT /evidence="ECO:0007829|PDB:2AWA"
FT STRAND 50..59
FT /evidence="ECO:0007829|PDB:2AWA"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:2AWA"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:2AWA"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:2AWA"
FT HELIX 79..88
FT /evidence="ECO:0007829|PDB:2AWA"
FT STRAND 91..99
FT /evidence="ECO:0007829|PDB:2AWA"
FT TURN 100..102
FT /evidence="ECO:0007829|PDB:2AWA"
FT STRAND 103..108
FT /evidence="ECO:0007829|PDB:2AWA"
FT STRAND 111..116
FT /evidence="ECO:0007829|PDB:2AWA"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:2AWA"
FT STRAND 135..138
FT /evidence="ECO:0007829|PDB:2AWA"
FT HELIX 139..149
FT /evidence="ECO:0007829|PDB:2AWA"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:2AWA"
FT HELIX 160..163
FT /evidence="ECO:0007829|PDB:2AWA"
FT STRAND 164..170
FT /evidence="ECO:0007829|PDB:2AWA"
FT TURN 171..173
FT /evidence="ECO:0007829|PDB:2AWA"
FT STRAND 174..180
FT /evidence="ECO:0007829|PDB:2AWA"
FT STRAND 182..191
FT /evidence="ECO:0007829|PDB:2AWA"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:2AWA"
FT HELIX 205..214
FT /evidence="ECO:0007829|PDB:2AWA"
FT STRAND 221..226
FT /evidence="ECO:0007829|PDB:2AWA"
FT STRAND 228..234
FT /evidence="ECO:0007829|PDB:2AWA"
FT STRAND 236..243
FT /evidence="ECO:0007829|PDB:2AWA"
FT HELIX 253..255
FT /evidence="ECO:0007829|PDB:2AWA"
FT STRAND 261..267
FT /evidence="ECO:0007829|PDB:2AWA"
FT HELIX 268..282
FT /evidence="ECO:0007829|PDB:2AWA"
FT STRAND 285..287
FT /evidence="ECO:0007829|PDB:2AWA"
FT STRAND 290..295
FT /evidence="ECO:0007829|PDB:2AWA"
FT STRAND 298..305
FT /evidence="ECO:0007829|PDB:2AWA"
FT TURN 306..308
FT /evidence="ECO:0007829|PDB:2AWA"
FT STRAND 309..315
FT /evidence="ECO:0007829|PDB:2AWA"
FT STRAND 318..323
FT /evidence="ECO:0007829|PDB:2AWA"
FT STRAND 325..329
FT /evidence="ECO:0007829|PDB:2AWA"
FT HELIX 331..339
FT /evidence="ECO:0007829|PDB:2AWA"
FT STRAND 343..351
FT /evidence="ECO:0007829|PDB:2AWA"
FT STRAND 353..355
FT /evidence="ECO:0007829|PDB:2AWA"
FT STRAND 357..363
FT /evidence="ECO:0007829|PDB:2AWA"
FT STRAND 367..372
FT /evidence="ECO:0007829|PDB:2AWA"
SQ SEQUENCE 378 AA; 42073 MW; 5749CB6EE857FFE6 CRC64;
MIHFSINKNL FLQALNTTKR AISSKNAIPI LSTVKIDVTN EGITLIGSNG QISIENFISQ
KNEDAGLLIT SLGSILLEAS FFINVVSSLP DVTLDFKEIE QNQIVLTSGK SEITLKGKDS
EQYPRIQEIS ASTPLILETK LLKKIINETA FAASTQESRP ILTGVHFVLS QHKELKTVAT
DSHRLSQKKL TLEKNSDDFD VVIPSRSLRE FSAVFTDDIE TVEIFFANNQ ILFRSENISF
YTRLLEGNYP DTDRLIPTDF NTTITFNVVN LRQSMERARL LSSATQNGTV KLEIKDGVVS
AHVHSPEVGK VNEEIDTDQV TGEDLTISFN PTYLIDSLKA LNSEKVTISF ISAVRPFTLV
PADTDEDFMQ LITPVRTN
