ID A0A1I0RND3_9BACT Unreviewed; 373 AA.
AC A0A1I0RND3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Beta sliding clamp {ECO:0000256|PIRNR:PIRNR000804};
GN ORFNames=SAMN05216290_3862 {ECO:0000313|EMBL:SEW42612.1};
OS Roseivirga pacifica.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Roseivirgaceae;
OC Roseivirga.
OX NCBI_TaxID=1267423 {ECO:0000313|EMBL:SEW42612.1, ECO:0000313|Proteomes:UP000199437};
RN [1] {ECO:0000313|Proteomes:UP000199437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.12402 {ECO:0000313|Proteomes:UP000199437};
RA Varghese N., Submissions S.;
RL Submitted (OCT-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; FOIR01000005; SEW42612.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0RND3; -.
DR STRING; 1267423.SAMN05216290_3862; -.
DR OrthoDB; 8421503at2; -.
DR Proteomes; UP000199437; 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:UP000199437};
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 130..243
FT /note="DNA polymerase III beta sliding clamp central"
FT /evidence="ECO:0000259|Pfam:PF02767"
FT DOMAIN 246..363
FT /note="DNA polymerase III beta sliding clamp C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02768"
SQ SEQUENCE 373 AA; 41434 MW; 14BC7E3A6CC2B96D CRC64;
MKFIVSSAEL LKRLSNINGV ITTNPVVPIL ENFLFEIKEG LLTVTASDLQ TSMITEIDVE
AKEDGSIAVP ARILMDTLKN LPEQPVTFSI DQETYSVEIN SDNGRYKLAG ENATDFPKVP
EVSDGYSVDM STEVLSSAIS NTIFATSNDE LRPAMTGVYV KLDDTNTTFV ATDGHRLVRY
RRVDVASDSG MSIIIPRKAL NLLKSTLPSE NSNVIVEFNA SNAYFNFNNI RMICRLIDER
FPDYENVIPQ ENPIEMSIDR SELLGSLKRI SIYANKTTHQ IRLKITGSEL TISAEDLDFS
NEAKETLACE HEGEDIEIGF NAKFLVEMLG NIHSKQITLQ MSAPNRAGLI VPAESDDSED
ILMLVMPVML NSY
//