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Database: UniProt
Entry: A0A3E0U3G0_9GAMM
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ID   A0A3E0U3G0_9GAMM        Unreviewed;       367 AA.
AC   A0A3E0U3G0;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=Beta sliding clamp {ECO:0000256|ARBA:ARBA00021035, ECO:0000256|PIRNR:PIRNR000804};
GN   ORFNames=DXX92_00010 {ECO:0000313|EMBL:REL33867.1}, DXX94_11320
GN   {ECO:0000313|EMBL:REL31254.1};
OS   Thalassotalea euphylliae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Thalassotalea.
OX   NCBI_TaxID=1655234 {ECO:0000313|EMBL:REL31254.1, ECO:0000313|Proteomes:UP000256899};
RN   [1] {ECO:0000313|Proteomes:UP000256899, ECO:0000313|Proteomes:UP000256999}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H2 {ECO:0000313|EMBL:REL33867.1,
RC   ECO:0000313|Proteomes:UP000256999}, and H3
RC   {ECO:0000313|Proteomes:UP000256899};
RA   Summers S., Rice S.A., Freckelton M.L., Nedved B.T., Hadfield M.G.;
RT   "Thalassotalea euphylliae genome.";
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:REL31254.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=H3 {ECO:0000313|EMBL:REL31254.1};
RA   Ferrada E.E., Latorre B.A.;
RL   Submitted (AUG-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:REL31254.1}.
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DR   EMBL; QUOT01000001; REL31254.1; -; Genomic_DNA.
DR   EMBL; QUOV01000001; REL33867.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3E0U3G0; -.
DR   OrthoDB; 8421503at2; -.
DR   Proteomes; UP000256899; Unassembled WGS sequence.
DR   Proteomes; UP000256999; 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:UP000256899};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000804}.
FT   DOMAIN          1..119
FT                   /note="DNA polymerase III beta sliding clamp N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00712"
FT   DOMAIN          131..244
FT                   /note="DNA polymerase III beta sliding clamp central"
FT                   /evidence="ECO:0000259|Pfam:PF02767"
FT   DOMAIN          246..366
FT                   /note="DNA polymerase III beta sliding clamp C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02768"
SQ   SEQUENCE   367 AA;  41212 MW;  BBFA9CBF403D4431 CRC64;
     MKFSLNRESL LKPLLLVSGA VERKSTLPIL SNILFEISDQ SLTLTATDLE LEMVAGTQIE
     NEGDSGKLTV PAKKLLDICK SLPEDSRLTF EAQGETVIIS TGRSRYSLST LPATDFPNIE
     EWKGDVEFRI MKSELLRLIE STHFSMANQD VRYYLNGMSI ETEGSEIRSV ATDGHRLAIC
     KIANESLALP ARQVIVPRKG ILEIIRLLDP VDEEIQVFLG SNHVRIIDNE YSFTSKLVDG
     RFPDYRRVLP RNGDKVLETN KDLLRQVLSR ASILSNEKFK GVRLNFAANE LKITANNPEQ
     EQAEEVIEIS FPYEDLEIGF NVSYVLDVLN AIKEQEVKFT LADANSSVVI EGRESGEALY
     VVMPMRL
//
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