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Entry: A0A1H5VAZ6_9RHOO
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ID   A0A1H5VAZ6_9RHOO        Unreviewed;       373 AA.
AC   A0A1H5VAZ6;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Beta sliding clamp {ECO:0000256|ARBA:ARBA00021035, ECO:0000256|PIRNR:PIRNR000804};
GN   ORFNames=SAMN05216242_10784 {ECO:0000313|EMBL:SEF84286.1}, Tchl_0002
GN   {ECO:0000313|EMBL:APR02878.1};
OS   Thauera chlorobenzoica.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC   Thauera.
OX   NCBI_TaxID=96773 {ECO:0000313|EMBL:APR02878.1, ECO:0000313|Proteomes:UP000185739};
RN   [1] {ECO:0000313|EMBL:SEF84286.1, ECO:0000313|Proteomes:UP000236741}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3CB-1 {ECO:0000313|EMBL:SEF84286.1,
RC   ECO:0000313|Proteomes:UP000236741};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:APR02878.1, ECO:0000313|Proteomes:UP000185739}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3CB1 {ECO:0000313|EMBL:APR02878.1,
RC   ECO:0000313|Proteomes:UP000185739};
RA   Goris T., Mergelsberg M., Boll M.;
RT   "Complete genome sequence of Thauera chlorobenzoica, a Betaproteobacterium
RT   degrading haloaromatics anaerobically to CO2 and halides.";
RL   Submitted (DEC-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}.
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DR   EMBL; CP018839; APR02878.1; -; Genomic_DNA.
DR   EMBL; FNVJ01000007; SEF84286.1; -; Genomic_DNA.
DR   RefSeq; WP_075146590.1; NZ_FNVJ01000007.1.
DR   AlphaFoldDB; A0A1H5VAZ6; -.
DR   STRING; 96773.Tchl_0002; -.
DR   KEGG; tcl:Tchl_0002; -.
DR   OrthoDB; 8421503at2; -.
DR   Proteomes; UP000185739; Chromosome.
DR   Proteomes; UP000236741; 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; 3.70.10.10; -; 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   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000804}.
FT   DOMAIN          4..120
FT                   /note="DNA polymerase III beta sliding clamp N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00712"
FT   DOMAIN          132..250
FT                   /note="DNA polymerase III beta sliding clamp central"
FT                   /evidence="ECO:0000259|Pfam:PF02767"
FT   DOMAIN          253..372
FT                   /note="DNA polymerase III beta sliding clamp C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02768"
SQ   SEQUENCE   373 AA;  41021 MW;  41446E2E520B5F02 CRC64;
     MLLLTTTRDA LLAPLQSVAG IVEKRHTLPI LSNVLIEKHG DQLTMLATDI EIQIRTTTGG
     HIGGEDVAIT VGARKLQDIL RALPDSADVS LALDDKRLTV KAGRSRFQLQ TLPAADYPQL
     SPPDSDAARL TIGQRAFKRQ LAQVSYAMAQ QDIRYYLNGL LLIADGGELR MVATDGHRLA
     YAAAALEAPF DAQAGTRTEA ILPRKTVLEL ARQLADSDDP LEILLAGNQA VFRFGPIELV
     TKLIDGKFPD YERVIPQAHP NLVSFARQPL LAALQRAAIL TTDKFRGVRM VLEDGVLKIV
     STNAEQEEAH DELEIDYHGD KLDIGFNVTY LLDVLNNLSS DTIDWHFNDG NSSVLITLPG
     NDQFKYVVMP MRI
//
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