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Entry: A0A0D6ETT3_9PROT
LinkDB: A0A0D6ETT3_9PROT
Original site: A0A0D6ETT3_9PROT 
ID   A0A0D6ETT3_9PROT        Unreviewed;       366 AA.
AC   A0A0D6ETT3;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=Beta sliding clamp {ECO:0000256|ARBA:ARBA00021035, ECO:0000256|PIRNR:PIRNR000804};
GN   Name=dnaN {ECO:0000313|EMBL:CEZ18900.1};
GN   ORFNames=BN1208_0002 {ECO:0000313|EMBL:CEZ18900.1};
OS   Candidatus Methylopumilus planktonicus.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Methylophilaceae; Methylopumilus.
OX   NCBI_TaxID=1581557 {ECO:0000313|EMBL:CEZ18900.1, ECO:0000313|Proteomes:UP000064007};
RN   [1] {ECO:0000313|Proteomes:UP000064007}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MMS-10A-171 {ECO:0000313|Proteomes:UP000064007};
RA   Salcher M.M.;
RL   Submitted (DEC-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}.
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DR   EMBL; LN827929; CEZ18900.1; -; Genomic_DNA.
DR   RefSeq; WP_046486538.1; NZ_LN827929.1.
DR   AlphaFoldDB; A0A0D6ETT3; -.
DR   STRING; 1581557.BN1208_0002; -.
DR   KEGG; mbat:BN1208_0002; -.
DR   HOGENOM; CLU_038149_4_2_4; -.
DR   OrthoDB; 8421503at2; -.
DR   Proteomes; UP000064007; Chromosome 1.
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:UP000064007};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000804}.
FT   DOMAIN          1..118
FT                   /note="DNA polymerase III beta sliding clamp N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00712"
FT   DOMAIN          130..243
FT                   /note="DNA polymerase III beta sliding clamp central"
FT                   /evidence="ECO:0000259|Pfam:PF02767"
FT   DOMAIN          246..365
FT                   /note="DNA polymerase III beta sliding clamp C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02768"
SQ   SEQUENCE   366 AA;  41634 MW;  F6B7ADA9AFFE056B CRC64;
     MNIKINRDAL LKPLANVVSI VERKHALPIL SNILIQGKDG QVQLTATDLE MQVSLSFKAD
     LKEEIATTIS ARKFFDITRS LPDDCVIDIT IKDSRVAVKA NKSRFAIQTL PAKDYPVMTK
     ASSEAVVITI SQIQLKRLLK QVEFAMAQQD IRYYLNGLLF EVNGNQLNIV GTDGHRLSFT
     SIHLDQNYNK TEVILPRKTV IELIKLLNET EELVSVELYK GQVSFNFNDI KLISKVIDGK
     FPDYTRVVPE GHNNQFTIDR SQFLTSLQRA SILSNEKYRG IRLIIADNNL KLISTNTEQE
     EAEEELEIQY QQDPIDIGFN VTYLIDVLTN IQEDKVTLAF LDTNSSCLFT IPNNNDYKYV
     VMPMRI
//
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