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Database: UniProt
Entry: A0A0X1TKI7_9FIRM
LinkDB: A0A0X1TKI7_9FIRM
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ID   A0A0X1TKI7_9FIRM        Unreviewed;       378 AA.
AC   A0A0X1TKI7;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Beta sliding clamp {ECO:0000256|ARBA:ARBA00021035, ECO:0000256|PIRNR:PIRNR000804};
GN   ORFNames=AT726_06165 {ECO:0000313|EMBL:AMC08545.1};
OS   Turicibacter sp. H121.
OC   Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC   Turicibacteraceae; Turicibacter.
OX   NCBI_TaxID=1712675 {ECO:0000313|EMBL:AMC08545.1, ECO:0000313|Proteomes:UP000057144};
RN   [1] {ECO:0000313|Proteomes:UP000057144}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H121 {ECO:0000313|Proteomes:UP000057144};
RA   Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AMC08545.1, ECO:0000313|Proteomes:UP000057144}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H121 {ECO:0000313|EMBL:AMC08545.1,
RC   ECO:0000313|Proteomes:UP000057144};
RX   PubMed=27013036;
RA   Auchtung T.A., Holder M.E., Gesell J.R., Ajami N.J., Duarte R.T., Itoh K.,
RA   Caspi R.R., Petrosino J.F., Horai R., Zarate-Blades C.R.;
RT   "Complete Genome Sequence of Turicibacter sp. Strain H121, Isolated from
RT   the Feces of a Contaminated Germ-Free Mouse.";
RL   Genome Announc. 4:0-0(2016).
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; CP013476; AMC08545.1; -; Genomic_DNA.
DR   RefSeq; WP_068759249.1; NZ_CP013476.1.
DR   AlphaFoldDB; A0A0X1TKI7; -.
DR   STRING; 1712675.AT726_06165; -.
DR   KEGG; tur:AT726_06165; -.
DR   OrthoDB; 8421503at2; -.
DR   Proteomes; UP000057144; 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:UP000057144};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000804}.
FT   DOMAIN          1..126
FT                   /note="DNA polymerase III beta sliding clamp N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00712"
FT   DOMAIN          137..250
FT                   /note="DNA polymerase III beta sliding clamp central"
FT                   /evidence="ECO:0000259|Pfam:PF02767"
FT   DOMAIN          254..376
FT                   /note="DNA polymerase III beta sliding clamp C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02768"
SQ   SEQUENCE   378 AA;  42573 MW;  4311C881ACB25BC5 CRC64;
     MKIKVDRQLL LTQLSYISKA IPTKTPLPVL TGIKFVVAEE GLYLTTSDSD ITINTFLPLE
     VNDTQVIQID SVGSIIIPGK YFIEIIKKLN GDNIEISTFE GNYVTIKCGR SEYTLNGFDV
     TQYPNIELIK HDNPIHLEKQ LLKTIIRQTV FSTANSENRP VLTGVNFRYD ADELMCVATD
     SFRLSKKLVP LNKLHEPFNI VIPGRSLIEL SKILDDSHES VDVYLANNQI LFQIGNISFQ
     SRLLDGIYPE TKEFVPTTFG IEIKANYHEL YNAFDRAALI ARDQVSNVVK LNILPEEGKL
     LITANSPEVG KVEEEVQVEM ISGGELRIAC SALFIIDALK AINNSEVIMS FNGDMRPFIL
     RDQYDETTIQ LIVPVRME
//
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