GenomeNet

Database: UniProt
Entry: A0A1D8AT51_9BACT
LinkDB: A0A1D8AT51_9BACT
Original site: A0A1D8AT51_9BACT 
ID   A0A1D8AT51_9BACT        Unreviewed;       374 AA.
AC   A0A1D8AT51;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Beta sliding clamp {ECO:0000256|PIRNR:PIRNR000804};
GN   Name=dnaN {ECO:0000313|EMBL:AOS44088.1};
GN   ORFNames=Verru16b_01149 {ECO:0000313|EMBL:AOS44088.1};
OS   Lacunisphaera limnophila.
OC   Bacteria; Verrucomicrobiota; Opitutae; Opitutales; Opitutaceae;
OC   Lacunisphaera.
OX   NCBI_TaxID=1838286 {ECO:0000313|EMBL:AOS44088.1, ECO:0000313|Proteomes:UP000095228};
RN   [1] {ECO:0000313|EMBL:AOS44088.1, ECO:0000313|Proteomes:UP000095228}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IG16b {ECO:0000313|EMBL:AOS44088.1,
RC   ECO:0000313|Proteomes:UP000095228};
RA   Rast P., Gloeckner I., Jogler M., Boedeker C., Jeske O., Wiegand S.,
RA   Reinhardt R., Schumann P., Rohde M., Spring S., Gloeckner F.O., Jogler C.;
RT   "Three novel species with peptidoglycan cell walls form the new genus
RT   Lacunisphaera gen. nov. in the family Opitutaceae of the verrucomicrobial
RT   subdivision 4.";
RL   Submitted (JUN-2016) 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}.
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; CP016094; AOS44088.1; -; Genomic_DNA.
DR   RefSeq; WP_069961380.1; NZ_CP016094.1.
DR   AlphaFoldDB; A0A1D8AT51; -.
DR   STRING; 1838286.Verru16b_01149; -.
DR   KEGG; obg:Verru16b_01149; -.
DR   PATRIC; fig|1838286.3.peg.1155; -.
DR   OrthoDB; 8421503at2; -.
DR   Proteomes; UP000095228; 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; 3.70.10.10; -; 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-binding {ECO:0000256|ARBA:ARBA00023125};
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:UP000095228};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000804}.
FT   DOMAIN          1..119
FT                   /note="DNA polymerase III beta sliding clamp N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00712"
FT   DOMAIN          129..252
FT                   /note="DNA polymerase III beta sliding clamp central"
FT                   /evidence="ECO:0000259|Pfam:PF02767"
FT   DOMAIN          255..372
FT                   /note="DNA polymerase III beta sliding clamp C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02768"
SQ   SEQUENCE   374 AA;  40882 MW;  3B8B2558895900DE CRC64;
     MKFKINRDHF SNGLAQVLNV VGSKAAMPIL SNVLIEAEKD HISLTTTNLD LGIRCRIKAE
     VKEGGSITLP VKRLATIVRE LPNVDVSFDS TPNHQAKIAS GGSNFRIMGI GAEEFPKLPD
     SNDDKSHTLD QGELATMLGN VAYAQSTDET RYILNGVYFS FKDGKLALVA TDGRRLALVS
     KDLAVPAAAS GAIILPAKTV AELLRLLGKG EKLTIAFNER RAAFQIETGK EAGGLTDSIF
     LFSKVVEGNY PNYQQVIPKE THQRIKLERE LFLQCVHRAA LVTSEKSNSV KIKVTSNLLE
     ITASSPDFGE AHESMAISYS GPDLQVAFNP QFVMDPLRAL TKDEVFFELK DEVSPGVFKT
     LESFVCVIMP VRLS
//
DBGET integrated database retrieval system