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Database: UniProt
Entry: A0A014NPW7_9BURK
LinkDB: A0A014NPW7_9BURK
Original site: A0A014NPW7_9BURK 
ID   A0A014NPW7_9BURK        Unreviewed;       373 AA.
AC   A0A014NPW7;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=Beta sliding clamp {ECO:0000256|ARBA:ARBA00021035, ECO:0000256|PIRNR:PIRNR000804};
GN   ORFNames=AX13_06910 {ECO:0000313|EMBL:EXU81523.1};
OS   Comamonas aquatica DA1877.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Comamonas.
OX   NCBI_TaxID=1457173 {ECO:0000313|EMBL:EXU81523.1, ECO:0000313|Proteomes:UP000020766};
RN   [1] {ECO:0000313|EMBL:EXU81523.1, ECO:0000313|Proteomes:UP000020766}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DA1877 {ECO:0000313|EMBL:EXU81523.1,
RC   ECO:0000313|Proteomes:UP000020766};
RA   Watson E., Macneil L.T., Ritter A.D., Yilmaz L.S., Rosebrock A.P.,
RA   Caudy A.A., Walhout A.J.;
RT   "Interspecies Systems Biology Uncovers Metabolites Affecting C. elegans
RT   Gene Expression and Life History Traits.";
RL   Submitted (JAN-2014) 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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EXU81523.1}.
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DR   EMBL; JBOK01000002; EXU81523.1; -; Genomic_DNA.
DR   RefSeq; WP_042412102.1; NZ_JBOK01000002.1.
DR   AlphaFoldDB; A0A014NPW7; -.
DR   STRING; 225991.MA05_01940; -.
DR   GeneID; 74940296; -.
DR   PATRIC; fig|1457173.3.peg.395; -.
DR   Proteomes; UP000020766; 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   Reference proteome {ECO:0000313|Proteomes:UP000020766};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000804}.
FT   DOMAIN          8..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;  40808 MW;  0B9699DFDFC31C12 CRC64;
     MIVLKATQDK VLAVLQSVSG IVERRHTLPI LANVLIKKTG NALQFTTSDL EIQIRTTAEL
     GGDTGDFSTT IGARKLIDIL KTMPGDQTVG LESQQSKMIL KGGKSRFTLQ TLPAEDFPLV
     QEAANFGPAF SVPQKVLKDL MGQVSFAMAV QDIRYYLNGI LFVAEGNTLS LVATDGHRLA
     FASAELDVDV GEKQEVILPR KTVLELQRLL SDVGGENSPR IEMQFANNQA KFTFGGMEFV
     TKLVEGKFPD YNRVIPRNHH NSVTLGRAPL LASLQRTAIM TSDKFKGVRL TIEPGTLRVA
     SNNADQEEAV DELDIDYGGD TIDIGFNVTY LLDVLANMSQ DMVKIELADS NSSALVSIPG
     NDNFKYVVMP MRI
//
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