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Database: UniProt
Entry: A0A161LJM9_9ACTN
LinkDB: A0A161LJM9_9ACTN
Original site: A0A161LJM9_9ACTN 
ID   A0A161LJM9_9ACTN        Unreviewed;       368 AA.
AC   A0A161LJM9;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Beta sliding clamp {ECO:0000256|PIRNR:PIRNR000804};
GN   ORFNames=PS9374_04855 {ECO:0000313|EMBL:GAT69184.1};
OS   Planomonospora sphaerica.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Streptosporangiaceae; Planomonospora.
OX   NCBI_TaxID=161355 {ECO:0000313|EMBL:GAT69184.1, ECO:0000313|Proteomes:UP000077701};
RN   [1] {ECO:0000313|EMBL:GAT69184.1, ECO:0000313|Proteomes:UP000077701}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 9374 {ECO:0000313|EMBL:GAT69184.1,
RC   ECO:0000313|Proteomes:UP000077701};
RA   Dohra H., Suzuki T., Inoue Y., Kodani S.;
RT   "Draft Genome Sequence of Planomonospora sphaerica JCM9374, a Rare
RT   Actinomycete.";
RL   Genome Announc. 4:e00779-16(2016).
RN   [2] {ECO:0000313|Proteomes:UP000077701}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 9374 {ECO:0000313|Proteomes:UP000077701};
RA   Suzuki T., Dohra H., Kodani S.;
RT   "Planomonospora sphaerica JCM9374 whole genome shotgun sequence.";
RL   Submitted (APR-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}.
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:GAT69184.1}.
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DR   EMBL; BDCX01000012; GAT69184.1; -; Genomic_DNA.
DR   RefSeq; WP_068900375.1; NZ_BDCX01000012.1.
DR   AlphaFoldDB; A0A161LJM9; -.
DR   STRING; 161355.PS9374_04855; -.
DR   OrthoDB; 468978at2; -.
DR   Proteomes; UP000077701; 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; 3.10.150.10; DNA Polymerase III, subunit A, domain 2; 3.
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:UP000077701};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000804}.
FT   DOMAIN          1..120
FT                   /note="DNA polymerase III beta sliding clamp N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00712"
FT   DOMAIN          133..240
FT                   /note="DNA polymerase III beta sliding clamp central"
FT                   /evidence="ECO:0000259|Pfam:PF02767"
FT   DOMAIN          256..355
FT                   /note="DNA polymerase III beta sliding clamp C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02768"
SQ   SEQUENCE   368 AA;  39079 MW;  916BB8F3A3E5DB9A CRC64;
     MKFRVDRDVL AEAVAWAARV LPARPAIPVL SGLLLEARPE QEDLVLSAFD YDVSARASVE
     AEVAEPGRVL IPGRVLAEIT RSLPGKAVEV VADGSEATLT CGSAEFNLRT MPVEDFPTLP
     AMPPVIGAIG GGVFASAVGQ VAPAASRDET LPMLTGVRVD ISGEHVAMAA TDRYRIAARE
     FDWRPERPDA AAAAVVPARV LVEVARSLRG GEVAVALGDG IAGFESVGRS TTVRLLDEQF
     IDYRARLAGD WSIRADVRVA PFVEAIKRIR LVAEPTTAIR LSFGQGQVTI QAGGGEVGRG
     TEVLDAELSG GDIQIAFQSQ FLLDGLSGVE SEFVRLNMES PTRPALITEV PGDAVPAFRY
     LVMSLRQA
//
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