GenomeNet

Database: UniProt
Entry: A0A2S5X2J0_9MICO
LinkDB: A0A2S5X2J0_9MICO
Original site: A0A2S5X2J0_9MICO 
ID   A0A2S5X2J0_9MICO        Unreviewed;       379 AA.
AC   A0A2S5X2J0;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=Beta sliding clamp {ECO:0000256|PIRNR:PIRNR000804};
GN   ORFNames=C5C17_16280 {ECO:0000313|EMBL:PPG38196.1};
OS   Pseudoclavibacter sp. RFBA6.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Pseudoclavibacter.
OX   NCBI_TaxID=2080573 {ECO:0000313|EMBL:PPG38196.1, ECO:0000313|Proteomes:UP000237697};
RN   [1] {ECO:0000313|EMBL:PPG38196.1, ECO:0000313|Proteomes:UP000237697}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RFBA6 {ECO:0000313|EMBL:PPG38196.1,
RC   ECO:0000313|Proteomes:UP000237697};
RA   Davis E.W.II., Tabima J.F., Weisberg A.J., Lopes L.D., Wiseman M.S.,
RA   Wiseman M.S., Pupko T., Belcher M.S., Sechler A.J., Tancos M.A.,
RA   Schroeder B.K., Murray T.D., Luster D.G., Schneider W.L., Rogers E.,
RA   Andreote F.D., Grunwald N.J., Putnam M.L., Chang J.H.;
RT   "Bacteriophage NCPPB3778 and a type I-E CRISPR drive the evolution of the
RT   US Biological Select Agent, Rathayibacter toxicus.";
RL   Submitted (FEB-2018) 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:PPG38196.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; PSUA01000015; PPG38196.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S5X2J0; -.
DR   Proteomes; UP000237697; 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:UP000237697};
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          127..243
FT                   /note="DNA polymerase III beta sliding clamp central"
FT                   /evidence="ECO:0000259|Pfam:PF02767"
FT   DOMAIN          247..346
FT                   /note="DNA polymerase III beta sliding clamp C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02768"
SQ   SEQUENCE   379 AA;  40639 MW;  AF5D3A354582B8F4 CRC64;
     MKFVVNRDVF SDAVSFVVKL LPQRPTLPIL SGVVVEVGDA GVTLSSFDYE VSSRTSIDAD
     VQEPGAVLVQ GRLLADIANR LPQAPVELSR DDSGVVIRCG SASFHLPTMP IEEFPSLPVV
     EGASGSIAGD VFSEAISQVA VAASREDVAP VITGVNLSLQ ADSMSLVATD RYRVAVRTIE
     WQSSLTETET ALVPAKTLAE VGKSLGSSGE ITITLVKDDI RELIAFSAGN KTVTSLLIKG
     NFPAVERLFP AETPHYAVLT VSDIVDAVRR VQLVLEREAA LRFTFTTEGL HLEALGSEQA
     QASENLDAVL HGNDMVVSLK PQFLLDGVGA IHSPFVRIAF TNSENPNKPG PVLLTSQTSR
     DEGESTNYRY LLQPNLLMR
//
DBGET integrated database retrieval system