ID A0A2I2L0I8_9ACTN Unreviewed; 395 AA.
AC A0A2I2L0I8;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Beta sliding clamp {ECO:0000256|PIRNR:PIRNR000804};
GN Name=dnaN {ECO:0000313|EMBL:SNQ51420.1};
GN ORFNames=FRACA_70036 {ECO:0000313|EMBL:SNQ51420.1};
OS Frankia canadensis.
OC Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia.
OX NCBI_TaxID=1836972 {ECO:0000313|EMBL:SNQ51420.1, ECO:0000313|Proteomes:UP000234331};
RN [1] {ECO:0000313|EMBL:SNQ51420.1, ECO:0000313|Proteomes:UP000234331}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FRACA_ARgP5 {ECO:0000313|EMBL:SNQ51420.1};
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; FZMO01000536; SNQ51420.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I2L0I8; -.
DR OrthoDB; 468978at2; -.
DR Proteomes; UP000234331; 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; 3.10.150.10; DNA Polymerase III, subunit A, domain 2; 3.
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:UP000234331};
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 129..257
FT /note="DNA polymerase III beta sliding clamp central"
FT /evidence="ECO:0000259|Pfam:PF02767"
FT DOMAIN 260..365
FT /note="DNA polymerase III beta sliding clamp C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02768"
SQ SEQUENCE 395 AA; 41423 MW; 7ED1171B90845440 CRC64;
MKFRVERDEF TEAVAWTART LPSRPTTQLQ VLSGLLLDAT GPMLKVAAYD YEVAAQSTVH
ATVSEEGRAL VNGKLLAEIT RALPAAPVDL AIDGTRLVIT CGNARFALPM LPVDDYPGLP
GMPPVTGHIE GSAFAAAVAQ VAIAAGRDDT LPVLTGVRIE IEGDTLTLAA TDRYRLAVRT
LKWRPTEEST GEDDAAGAPV TVALVPARTL LDTAKSLSGA GVEVSIALGT GPSGETLAGF
AGSTRQTTTR LLEGQFPPYR KLLPDSSPLI AQLEIAPLQE AVRRVALVAA KTAPVQLLFS
PDHLVLEAGT GGEAQATETL PLTYDGPELA VAFNPSYLLD ALGALESDVV RIGFASADDP
TVAANKPAIL TGKAADEDGE LPDYRYLLMP IRLNG
//