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Database: UniProt
Entry: A0A1H6MIZ4_9GAMM
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ID   A0A1H6MIZ4_9GAMM        Unreviewed;       367 AA.
AC   A0A1H6MIZ4;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Beta sliding clamp {ECO:0000256|ARBA:ARBA00021035, ECO:0000256|PIRNR:PIRNR000804};
GN   ORFNames=BAZSYMA_ACONTIG00194_3 {ECO:0000313|EMBL:SEH97528.1},
GN   BAZSYMB_SCAFFOLD00001_20 {ECO:0000313|EMBL:SEH74166.1};
OS   Bathymodiolus azoricus thioautotrophic gill symbiont.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts.
OX   NCBI_TaxID=235205 {ECO:0000313|EMBL:SEH97528.1, ECO:0000313|Proteomes:UP000198988};
RN   [1] {ECO:0000313|Proteomes:UP000198559, ECO:0000313|Proteomes:UP000198988}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BazSymA {ECO:0000313|Proteomes:UP000198988}, and BazSymB
RC   {ECO:0000313|Proteomes:UP000198559};
RA   Petersen J., Sayavedra L.;
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:SEH97528.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BazSymA {ECO:0000313|EMBL:SEH97528.1}, and BazSymB
RC   {ECO:0000313|EMBL:SEH74166.1};
RA   Olsen C.W., Carey S., Hinshaw L., Karasin A.I.;
RL   Submitted (JUN-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}.
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DR   EMBL; CVUD02000116; SEH74166.1; -; Genomic_DNA.
DR   EMBL; CDSC02000386; SEH97528.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H6MIZ4; -.
DR   STRING; 235205.BAZSYMB_SCAFFOLD00001_20; -.
DR   OrthoDB; 8421503at2; -.
DR   Proteomes; UP000198559; Unassembled WGS sequence.
DR   Proteomes; UP000198988; 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:UP000198988};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000804}.
FT   DOMAIN          1..117
FT                   /note="DNA polymerase III beta sliding clamp N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00712"
FT   DOMAIN          129..244
FT                   /note="DNA polymerase III beta sliding clamp central"
FT                   /evidence="ECO:0000259|Pfam:PF02767"
FT   DOMAIN          247..365
FT                   /note="DNA polymerase III beta sliding clamp C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02768"
SQ   SEQUENCE   367 AA;  41867 MW;  86D2C4A3FA6368CC CRC64;
     MNIQLTVDEL LEPLQTVIGV VENKPTLPIL SHVLIQLKNG ELTLTTTDME IELHASKKIQ
     SQEEVSFTIY AKDLIDIIRK LKEDTVIEFI IEKSKIYMKT NNNSFELNTF NTQDFPESPK
     IIDSETVNIN RTVLKDLIKK TSFSMGNQDI RAYLNGLYFE VNKDNIIVVA TDGHRLSIGE
     IKQNNNLTSK KTVILPRKAV SELNKILEHD GDENIDIHLS ENYFHLKTDG ATVVSRLIDG
     NFPNYAQVIP TNYENTAIIN RQEFLDNLQQ TSIFVEERTK GVKLAFKDNQ INIFSHSERG
     QAKAKVDVKN FNKETDIAFN INYLMSVLEI LTTDEINMVL PSENSQSCLL SSIDDESYQY
     VVMPMKI
//
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