GenomeNet

Database: UniProt
Entry: A0A0J8YE38_9GAMM
LinkDB: A0A0J8YE38_9GAMM
Original site: A0A0J8YE38_9GAMM 
ID   A0A0J8YE38_9GAMM        Unreviewed;       366 AA.
AC   A0A0J8YE38;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Beta sliding clamp {ECO:0000256|ARBA:ARBA00021035, ECO:0000256|PIRNR:PIRNR000804};
GN   ORFNames=AI28_14870 {ECO:0000313|EMBL:KMV68178.1};
OS   bacteria symbiont BFo1 of Frankliniella occidentalis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae.
OX   NCBI_TaxID=1628855 {ECO:0000313|EMBL:KMV68178.1, ECO:0000313|Proteomes:UP000037152};
RN   [1] {ECO:0000313|EMBL:KMV68178.1, ECO:0000313|Proteomes:UP000037152}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BFo1 {ECO:0000313|EMBL:KMV68178.1,
RC   ECO:0000313|Proteomes:UP000037152};
RA   Facey P.D., Hitchings M.D., Hegarty M.J., Pachebat J.A., Morgan L.V.,
RA   Hoeppner J.E., Whitten M.A., Dyson P.J., Del Sol R.;
RT   "The draft genomes, genome evolution and classification of BFo1 and BFo2
RT   two insect symbionts isolated from Western Flower Thrips (Frankliniella
RT   occidentalis [Pergande]).";
RL   Submitted (MAY-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:KMV68178.1}.
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; JMSO01000227; KMV68178.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0J8YE38; -.
DR   STRING; 1628855.WB66_20725; -.
DR   PATRIC; fig|1628855.3.peg.3009; -.
DR   Proteomes; UP000037152; 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   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          129..243
FT                   /note="DNA polymerase III beta sliding clamp central"
FT                   /evidence="ECO:0000259|Pfam:PF02767"
FT   DOMAIN          245..365
FT                   /note="DNA polymerase III beta sliding clamp C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02768"
SQ   SEQUENCE   366 AA;  40588 MW;  59E97595D5A0D840 CRC64;
     MKFIVEREHL LKPLQQVSSP LGGRPTLPIL GNLLLQVNEG TLLLTGTDLE MEMVARVALT
     QDHEPGATTV PARKFFDICR GLPEGAEITV ILDGERMLVR SGRSRFSLST LPASDFPNLD
     DWQSEVEFTL PQATMKRLIE ATQFSMAHQD VRYYLNGMLF ETEGEELRTV ATDGHRLAVC
     SMPVGQALPS HSVIVPRKGV IELVRLLDGG DTPLQVQIGS NNIRAHVGDF IFTSKLVDGR
     FPDYRRVLPK NPDKTLDASC DLLKQAFSRA AILSNEKFRG VRLYISENQL KITANNPEQE
     EAEEMLDVTY GGTDLEIGFN VSYVLDVLNA LKCENVRLLL TDSVSSVQIE DAASQSAAYV
     VMPMRL
//
DBGET integrated database retrieval system