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Database: UniProt
Entry: D6GSV8_FILAD
LinkDB: D6GSV8_FILAD
Original site: D6GSV8_FILAD 
ID   D6GSV8_FILAD            Unreviewed;       363 AA.
AC   D6GSV8;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 2.
DT   27-MAR-2024, entry version 69.
DE   RecName: Full=Beta sliding clamp {ECO:0000256|ARBA:ARBA00021035, ECO:0000256|PIRNR:PIRNR000804};
GN   Name=dnaN {ECO:0000313|EMBL:EFE27943.2};
GN   OrderedLocusNames=HMPREF0389_01195 {ECO:0000313|EMBL:EFE27943.2};
OS   Filifactor alocis (strain ATCC 35896 / CCUG 47790 / D40 B5) (Fusobacterium
OS   alocis).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Filifactor.
OX   NCBI_TaxID=546269 {ECO:0000313|EMBL:EFE27943.2, ECO:0000313|Proteomes:UP000007468};
RN   [1] {ECO:0000313|Proteomes:UP000007468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35896 / D40 B5 {ECO:0000313|Proteomes:UP000007468};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ward D., Earl A., Feldgarden M., Young S.K., Gargeya S., Zeng Q.,
RA   Alvarado L., Berlin A., Bochicchio J., Chapman S.B., Chen Z., Freedman E.,
RA   Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D.,
RA   Howarth C., Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., White J., Yandava C., Izard J.,
RA   Blanton J.M., Baranova O.V., Tanner A.C., Dewhirst F.E., Haas B.,
RA   Nusbaum C., Birren B.;
RT   "The genome sequence of Filifactor alocis strain ATCC 35896.";
RL   Submitted (DEC-2010) 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|ARBA:ARBA00002266,
CC       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; CP002390; EFE27943.2; -; Genomic_DNA.
DR   AlphaFoldDB; D6GSV8; -.
DR   STRING; 546269.HMPREF0389_01195; -.
DR   KEGG; faa:HMPREF0389_01195; -.
DR   PATRIC; fig|546269.5.peg.3; -.
DR   eggNOG; COG0592; Bacteria.
DR   HOGENOM; CLU_038149_2_1_9; -.
DR   OrthoDB; 8421503at2; -.
DR   Proteomes; UP000007468; 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-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:UP000007468};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000804}.
FT   DOMAIN          2..118
FT                   /note="DNA polymerase III beta sliding clamp N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00712"
FT   DOMAIN          129..240
FT                   /note="DNA polymerase III beta sliding clamp central"
FT                   /evidence="ECO:0000259|Pfam:PF02767"
FT   DOMAIN          245..362
FT                   /note="DNA polymerase III beta sliding clamp C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02768"
SQ   SEQUENCE   363 AA;  41476 MW;  68D091DA4A7C8A1D CRC64;
     MMKFTVNQRE FSDALAIASK AIISKTPLDI LKGFYLEAYE NELTITGNNL EIGIRTSIDA
     AVETEGKSVI DAKILSDIIR KLPNEEVTVS IKDGNVLLQC QKLKFTIKEM LDNGFPTVDE
     LEEAVYQNIH PAILEEMIKK THFAVTTDET KPVFMGELVE LEDNQMNVIA LDGFRLAYKK
     CELKSSVGSR SMIIPGKTMV EIMRLCQTME EDVKIGIEDR HASFLFGRTL VNTQLIQGEF
     SKYEEIIPKE FSTKIKVNRQ KFIDALDRAT LVSKNYLVKL RIQNDELLIT AHDNEVGNLE
     EILDVELEGK NLEIAFNIRF FLDSLKVMED EYIYMNFNTN VSPCIIKPEF ETDYTYLVLP
     VRI
//
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