ID A0A248YGX6_9ACTN Unreviewed; 377 AA.
AC A0A248YGX6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Beta sliding clamp {ECO:0000256|PIRNR:PIRNR000804};
GN ORFNames=CIK06_00010 {ECO:0000313|EMBL:ASW52914.1};
OS Plantactinospora sp. KBS50.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Plantactinospora.
OX NCBI_TaxID=2024580 {ECO:0000313|EMBL:ASW52914.1, ECO:0000313|Proteomes:UP000216795};
RN [1] {ECO:0000313|EMBL:ASW52914.1, ECO:0000313|Proteomes:UP000216795}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KBS50 {ECO:0000313|EMBL:ASW52914.1,
RC ECO:0000313|Proteomes:UP000216795};
RA Juboi H., Hwang S.S., Yeo T.C., Nissom P.M.;
RT "Genome sequencing and analysis of secondary metabolite biosynthetic
RT capabilities of Plantactinospora sp. KBS50.";
RL Submitted (AUG-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; CP022961; ASW52914.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A248YGX6; -.
DR KEGG; plk:CIK06_00010; -.
DR OrthoDB; 468978at2; -.
DR Proteomes; UP000216795; 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-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:UP000216795};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000804}.
FT DOMAIN 1..118
FT /note="DNA polymerase III beta sliding clamp N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00712"
FT DOMAIN 127..247
FT /note="DNA polymerase III beta sliding clamp central"
FT /evidence="ECO:0000259|Pfam:PF02767"
FT DOMAIN 250..373
FT /note="DNA polymerase III beta sliding clamp C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02768"
SQ SEQUENCE 377 AA; 39387 MW; 2EC120A9868B54D7 CRC64;
MKFRVERDAL ADAVAWTAKS LPSRPSVPVL AGVLLRVSEG TLQVSGFDYE VSSQVTVDVH
GDADGAALVS GRLLAEITKA LPAKPVDIAA VGAHLELVCG SARFTLPTMP VEDYPTLPEM
PESAGTIDAA AFATAVAQVA IAAGRDETLP MMTGVRLELN GGNLVMLATD RYRLAMRELP
WQPDDAEISM NALVPARTLN DTAKTLGPLG GEVTLALAHG GAGEGMIGFA GGTRRTTSRL
LDGANYPPVR SLFPATSNAQ AQVAVAALVE VVKRVALVAE RTTPVLLSFS SDGLVVEAGG
TEEARASEAM DATFTGEPMT IGFNPQYLID GLQNLGSATA VLSFVDAFKP AVISPASEDG
EVVPGYRYLI MPIRVTR
//
