DPO3B_SPICI
ID DPO3B_SPICI Reviewed; 363 AA.
AC P34029;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 25-MAY-2022, entry version 79.
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 Spiroplasma citri.
OC Bacteria; Tenericutes; Mollicutes; Entomoplasmatales; Spiroplasmataceae;
OC Spiroplasma.
OX NCBI_TaxID=2133;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=R8A2HP;
RX PubMed=7764984; DOI=10.1007/bf01570187;
RA Ye F., Renaudin J., Bove J.M., Laigret F.;
RT "Cloning and sequencing of the replication origin (oriC) of the Spiroplasma
RT citri chromosome and construction of autonomously replicating artificial
RT plasmids.";
RL Curr. Microbiol. 29:23-29(1994).
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; Z19108; CAA79522.1; -; Genomic_DNA.
DR PIR; S35733; S35733.
DR AlphaFoldDB; P34029; -.
DR SMR; P34029; -.
DR STRING; 2133.SCITRI_002; -.
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; IPR022634; DNA_polIII_beta_N.
DR PANTHER; PTHR30478; PTHR30478; 1.
DR Pfam; PF00712; DNA_pol3_beta; 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..363
FT /note="Beta sliding clamp"
FT /id="PRO_0000105461"
SQ SEQUENCE 363 AA; 41329 MW; C969A39BEFEF26D6 CRC64;
MIVNIKRDKI LDELLKVSRI ISQKTLIPSL LGILIEVKKD KITFTTSDGD TSIKSEIMGN
DLNITRIGSV LIKNKFIVEV IRKIEDEFIT LEVVEGNLIK IKANNFDSVL NTLNSADYPH
LSFETEGKEI IFTSTVLKEI ISQTSFAIGE KEKRIVFNGL NIKTDQNNKE LIITATDSFR
LSCKKIDYSN NYNFDVIIPG KFINEIGRLI SENDQVSELL LIIINCKQKI IEGKYPDTSK
VIRTSFNTSL TINNRAIIKI IERRSVLSNE TMTTIVTLKI KEQKVLVTSF TQEIGNTEEE
IRDFKVEGTD QIIAFNSKYI LDALKAFKTK EITIKMIDER KPLIITANDD QTLQQLVLPI
RSY