ID DPO3B_RICCN Reviewed; 379 AA. AC Q92I37; DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 27-MAR-2024, entry version 110. 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=RC0583; OS Rickettsia conorii (strain ATCC VR-613 / Malish 7). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group. OX NCBI_TaxID=272944; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC VR-613 / Malish 7; RX PubMed=11557893; DOI=10.1126/science.1061471; RA Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V., RA Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.; RT "Mechanisms of evolution in Rickettsia conorii and R. prowazekii."; RL Science 293:2093-2098(2001). 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; AE006914; AAL03121.1; -; Genomic_DNA. DR PIR; G97772; G97772. DR RefSeq; WP_010977217.1; NC_003103.1. DR PDB; 5W7Z; X-ray; 1.70 A; A/B=1-379. DR PDB; 6DM6; X-ray; 2.25 A; A/B=1-379. DR PDBsum; 5W7Z; -. DR PDBsum; 6DM6; -. DR AlphaFoldDB; Q92I37; -. DR SMR; Q92I37; -. DR GeneID; 927682; -. DR KEGG; rco:RC0583; -. DR PATRIC; fig|272944.4.peg.665; -. DR HOGENOM; CLU_038149_4_2_5; -. DR Proteomes; UP000000816; 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 Gene3D; 3.70.10.10; -; 1. DR Gene3D; 3.10.150.10; DNA Polymerase III, subunit A, domain 2; 1. DR InterPro; IPR046938; DNA_clamp_sf. 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 NCBIfam; TIGR00663; dnan; 1. DR PANTHER; PTHR30478:SF0; BETA SLIDING CLAMP; 1. DR PANTHER; PTHR30478; DNA POLYMERASE III SUBUNIT BETA; 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 SUPFAM; SSF55979; DNA clamp; 3. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; DNA replication; DNA-binding; KW DNA-directed DNA polymerase; Nucleotidyltransferase; Transferase. FT CHAIN 1..379 FT /note="Beta sliding clamp" FT /id="PRO_0000105457" FT STRAND 3..7 FT /evidence="ECO:0007829|PDB:5W7Z" FT HELIX 8..21 FT /evidence="ECO:0007829|PDB:5W7Z" FT HELIX 29..31 FT /evidence="ECO:0007829|PDB:5W7Z" FT STRAND 33..39 FT /evidence="ECO:0007829|PDB:5W7Z" FT STRAND 42..48 FT /evidence="ECO:0007829|PDB:5W7Z" FT STRAND 50..59 FT /evidence="ECO:0007829|PDB:5W7Z" FT STRAND 61..64 FT /evidence="ECO:0007829|PDB:5W7Z" FT STRAND 66..71 FT /evidence="ECO:0007829|PDB:5W7Z" FT HELIX 72..79 FT /evidence="ECO:0007829|PDB:5W7Z" FT STRAND 85..91 FT /evidence="ECO:0007829|PDB:5W7Z" FT HELIX 93..95 FT /evidence="ECO:0007829|PDB:6DM6" FT STRAND 97..101 FT /evidence="ECO:0007829|PDB:5W7Z" FT STRAND 104..108 FT /evidence="ECO:0007829|PDB:5W7Z" FT HELIX 113..115 FT /evidence="ECO:0007829|PDB:5W7Z" FT STRAND 125..131 FT /evidence="ECO:0007829|PDB:5W7Z" FT HELIX 132..140 FT /evidence="ECO:0007829|PDB:5W7Z" FT HELIX 143..145 FT /evidence="ECO:0007829|PDB:5W7Z" FT HELIX 153..155 FT /evidence="ECO:0007829|PDB:5W7Z" FT STRAND 156..163 FT /evidence="ECO:0007829|PDB:5W7Z" FT STRAND 166..172 FT /evidence="ECO:0007829|PDB:5W7Z" FT STRAND 174..183 FT /evidence="ECO:0007829|PDB:5W7Z" FT STRAND 191..196 FT /evidence="ECO:0007829|PDB:5W7Z" FT HELIX 197..207 FT /evidence="ECO:0007829|PDB:5W7Z" FT TURN 210..214 FT /evidence="ECO:0007829|PDB:5W7Z" FT STRAND 215..221 FT /evidence="ECO:0007829|PDB:5W7Z" FT STRAND 223..230 FT /evidence="ECO:0007829|PDB:5W7Z" FT TURN 231..233 FT /evidence="ECO:0007829|PDB:5W7Z" FT STRAND 234..239 FT /evidence="ECO:0007829|PDB:5W7Z" FT HELIX 249..251 FT /evidence="ECO:0007829|PDB:5W7Z" FT STRAND 257..263 FT /evidence="ECO:0007829|PDB:5W7Z" FT HELIX 264..275 FT /evidence="ECO:0007829|PDB:5W7Z" FT HELIX 280..282 FT /evidence="ECO:0007829|PDB:6DM6" FT STRAND 285..289 FT /evidence="ECO:0007829|PDB:5W7Z" FT STRAND 291..300 FT /evidence="ECO:0007829|PDB:5W7Z" FT TURN 301..303 FT /evidence="ECO:0007829|PDB:5W7Z" FT STRAND 304..311 FT /evidence="ECO:0007829|PDB:5W7Z" FT HELIX 316..318 FT /evidence="ECO:0007829|PDB:5W7Z" FT STRAND 320..322 FT /evidence="ECO:0007829|PDB:5W7Z" FT STRAND 328..332 FT /evidence="ECO:0007829|PDB:5W7Z" FT HELIX 334..343 FT /evidence="ECO:0007829|PDB:5W7Z" FT STRAND 347..353 FT /evidence="ECO:0007829|PDB:5W7Z" FT STRAND 360..364 FT /evidence="ECO:0007829|PDB:5W7Z" FT STRAND 367..374 FT /evidence="ECO:0007829|PDB:5W7Z" SQ SEQUENCE 379 AA; 42237 MW; 1FBE1A62CE25639C CRC64; MLKLIVETKT LVQSLGFASS VVEKRNVIPE YANIKLSAKD GNLELSSTNM DLYLSQKIAV QVVSEGECTV STKTLNDIVR KLPDSELTLT DLGTTGLEIK GKNCKFNLFT LPVSSFPAMD SINPEASFKI SCTDFAKIIE STKFSISLDE TRYNLNGVYL HIKDKEFCSA STDGHRLSIS WVTLEKQIKN FGVILPQKSA EEILKIVKDP KNINEDIEIL LSSNKIKFIC NENTSMLSKL IDGTFPDYST FIPESSSSKL VINRKMFADS IERIAIITVE KFRAVKLSLS RETLEISAVG EARGNAKEVI NSSQDKESFY EYNSDESLAI GFNPQYLEDV LKAVKSDVVE LYFSDVSAPV LIKFPENPKD IFVVMPVKV //