ID A0A238WUE1_9RHOB Unreviewed; 372 AA.
AC A0A238WUE1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Beta sliding clamp {ECO:0000256|ARBA:ARBA00021035, ECO:0000256|PIRNR:PIRNR000804};
GN ORFNames=SAMN06265370_107121 {ECO:0000313|EMBL:SNR50023.1};
OS Puniceibacterium sediminis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Puniceibacterium.
OX NCBI_TaxID=1608407 {ECO:0000313|EMBL:SNR50023.1, ECO:0000313|Proteomes:UP000198417};
RN [1] {ECO:0000313|EMBL:SNR50023.1, ECO:0000313|Proteomes:UP000198417}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29052 {ECO:0000313|EMBL:SNR50023.1,
RC ECO:0000313|Proteomes:UP000198417};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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:0000256|PIRNR:PIRNR000804}.
CC -!- SUBUNIT: Forms a ring-shaped head-to-tail homodimer around DNA.
CC {ECO:0000256|PIRNR:PIRNR000804}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|PIRNR:PIRNR000804}.
CC -!- SIMILARITY: Belongs to the beta sliding clamp family.
CC {ECO:0000256|ARBA:ARBA00010752, ECO:0000256|PIRNR:PIRNR000804}.
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DR EMBL; FZNN01000007; SNR50023.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A238WUE1; -.
DR OrthoDB; 8421503at2; -.
DR Proteomes; UP000198417; Unassembled WGS sequence.
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-UniRule.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
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 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|PIRNR:PIRNR000804};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW ECO:0000256|PIRNR:PIRNR000804};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW ECO:0000256|PIRNR:PIRNR000804};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|PIRNR:PIRNR000804};
KW Reference proteome {ECO:0000313|Proteomes:UP000198417};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000804}.
FT DOMAIN 1..120
FT /note="DNA polymerase III beta sliding clamp N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00712"
FT DOMAIN 132..249
FT /note="DNA polymerase III beta sliding clamp central"
FT /evidence="ECO:0000259|Pfam:PF02767"
FT DOMAIN 252..371
FT /note="DNA polymerase III beta sliding clamp C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02768"
SQ SEQUENCE 372 AA; 40645 MW; 601C9E60A8F98B5D CRC64;
MKFSMERGTL LKAVSQAQSV VERRNTIPIL ANVLIEADGA SVQFRATDLD IEVLDKATAM
VERPGATTVS AVTLHEIVRK LPDGALVTLT EEAATGRLTV EAGRSNFSLA TLPKEDFPVM
ASSEYSANFT APAKVLRRLF DKSKFAISTE ETRYYLNGVY MHTADGDGGR KLRCVATDGH
RLARIDADLP AGAEDMPGVI VPRKTVGELR KLLEDDDMDI AVSVSETKIR FATPDITLTS
KVIDGTFPDY TRVIPQGNTR RLEVDAAEFA KAVDRVATVS SERSRAVKLS LDEDRLILSV
NAPDSGAAEE ELAVAYSDER LEIGFNAKYL LEIASQVDRE NAVFMFNSSG DPTLMREGND
MSAVYVVMPM RV
//
