DPO3B_RICTY
ID DPO3B_RICTY Reviewed; 381 AA.
AC Q68WW0;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 95.
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=RT0405;
OS Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=257363;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-144 / Wilmington;
RX PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA Yu X.-J., Walker D.H., Weinstock G.M.;
RT "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT of other Rickettsiae.";
RL J. Bacteriol. 186:5842-5855(2004).
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; AE017197; AAU03882.1; -; Genomic_DNA.
DR RefSeq; WP_011190866.1; NC_006142.1.
DR PDB; 6D46; X-ray; 2.00 A; A=1-381.
DR PDB; 6DJK; X-ray; 1.85 A; A=1-381.
DR PDBsum; 6D46; -.
DR PDBsum; 6DJK; -.
DR AlphaFoldDB; Q68WW0; -.
DR SMR; Q68WW0; -.
DR STRING; 257363.RT0405; -.
DR PRIDE; Q68WW0; -.
DR EnsemblBacteria; AAU03882; AAU03882; RT0405.
DR KEGG; rty:RT0405; -.
DR eggNOG; COG0592; Bacteria.
DR HOGENOM; CLU_038149_4_2_5; -.
DR OMA; YLIMPVR; -.
DR OrthoDB; 1040142at2; -.
DR Proteomes; UP000000604; 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..381
FT /note="Beta sliding clamp"
FT /id="PRO_0000280792"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:6DJK"
FT HELIX 8..21
FT /evidence="ECO:0007829|PDB:6DJK"
FT HELIX 30..32
FT /evidence="ECO:0007829|PDB:6DJK"
FT STRAND 33..39
FT /evidence="ECO:0007829|PDB:6DJK"
FT STRAND 42..48
FT /evidence="ECO:0007829|PDB:6DJK"
FT STRAND 50..59
FT /evidence="ECO:0007829|PDB:6DJK"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:6DJK"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:6DJK"
FT HELIX 72..79
FT /evidence="ECO:0007829|PDB:6DJK"
FT STRAND 85..92
FT /evidence="ECO:0007829|PDB:6DJK"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:6DJK"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:6DJK"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:6DJK"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:6DJK"
FT STRAND 125..131
FT /evidence="ECO:0007829|PDB:6DJK"
FT HELIX 132..140
FT /evidence="ECO:0007829|PDB:6DJK"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:6DJK"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:6D46"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:6DJK"
FT STRAND 156..163
FT /evidence="ECO:0007829|PDB:6DJK"
FT STRAND 166..172
FT /evidence="ECO:0007829|PDB:6DJK"
FT STRAND 174..183
FT /evidence="ECO:0007829|PDB:6DJK"
FT STRAND 191..196
FT /evidence="ECO:0007829|PDB:6DJK"
FT HELIX 197..208
FT /evidence="ECO:0007829|PDB:6DJK"
FT TURN 210..214
FT /evidence="ECO:0007829|PDB:6DJK"
FT STRAND 215..221
FT /evidence="ECO:0007829|PDB:6DJK"
FT STRAND 223..230
FT /evidence="ECO:0007829|PDB:6DJK"
FT TURN 231..233
FT /evidence="ECO:0007829|PDB:6DJK"
FT STRAND 234..239
FT /evidence="ECO:0007829|PDB:6DJK"
FT HELIX 248..251
FT /evidence="ECO:0007829|PDB:6DJK"
FT STRAND 257..263
FT /evidence="ECO:0007829|PDB:6DJK"
FT HELIX 264..275
FT /evidence="ECO:0007829|PDB:6DJK"
FT HELIX 280..282
FT /evidence="ECO:0007829|PDB:6DJK"
FT STRAND 285..289
FT /evidence="ECO:0007829|PDB:6DJK"
FT STRAND 291..300
FT /evidence="ECO:0007829|PDB:6DJK"
FT TURN 301..303
FT /evidence="ECO:0007829|PDB:6DJK"
FT STRAND 304..311
FT /evidence="ECO:0007829|PDB:6DJK"
FT HELIX 316..318
FT /evidence="ECO:0007829|PDB:6DJK"
FT STRAND 320..322
FT /evidence="ECO:0007829|PDB:6DJK"
FT STRAND 328..332
FT /evidence="ECO:0007829|PDB:6DJK"
FT HELIX 334..343
FT /evidence="ECO:0007829|PDB:6DJK"
FT STRAND 347..353
FT /evidence="ECO:0007829|PDB:6DJK"
FT STRAND 358..360
FT /evidence="ECO:0007829|PDB:6DJK"
FT STRAND 362..366
FT /evidence="ECO:0007829|PDB:6DJK"
FT STRAND 369..376
FT /evidence="ECO:0007829|PDB:6DJK"
SQ SEQUENCE 381 AA; 42822 MW; 29166F7F3A3F56B4 CRC64;
MLKLIVETKT LVQSLGFARS VVEKRNVIPE YANIKLSAKD GNLELSSTNM DLYLSQKIAV
QVLSEGEITV STQTLSDIVR KLPDSELTLT ELDIMKLEIK GQNCQFNLFT LPVSSFPAMD
SIKPEVSFKI SCADFAKIIE STKFSISLDE TRYNLNGIYL HIKDKEFFAA STDGHRLSIS
WITLEEKIKN FGVILPQKSA EEILKIVKDL KNIHEDIEIL LSSNKIKFIC NENTILLSKL
IDGTFPDYSA FIPKSSISKL VINRKIFADS IERIAIITVE KFRAIKLSLS RKTLEISAVG
EARGNAKEII TASQDKESFY EYNCDESLVI GFNPQYLEDV LKAVKSNLVE LYFSDISASA
PVLIKFPQNP KDIFVIMPVK V
