ID A0A0B7H4J2_9FLAO Unreviewed; 373 AA.
AC A0A0B7H4J2;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Beta sliding clamp {ECO:0000256|PIRNR:PIRNR000804};
GN ORFNames=CCYN2B_120113 {ECO:0000313|EMBL:CEN32822.1};
OS Capnocytophaga cynodegmi.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Capnocytophaga.
OX NCBI_TaxID=28189 {ECO:0000313|EMBL:CEN32822.1, ECO:0000313|Proteomes:UP000038055};
RN [1] {ECO:0000313|Proteomes:UP000038055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ccyn2B {ECO:0000313|Proteomes:UP000038055};
RA MANFREDI Pablo;
RL Submitted (JAN-2015) 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; CDOD01000004; CEN32822.1; -; Genomic_DNA.
DR RefSeq; WP_041990304.1; NZ_CDOD01000004.1.
DR AlphaFoldDB; A0A0B7H4J2; -.
DR STRING; 28189.CCYN74_110059; -.
DR eggNOG; COG0592; Bacteria.
DR Proteomes; UP000038055; 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:UP000038055};
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 131..242
FT /note="DNA polymerase III beta sliding clamp central"
FT /evidence="ECO:0000259|Pfam:PF02767"
FT DOMAIN 246..350
FT /note="DNA polymerase III beta sliding clamp C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02768"
SQ SEQUENCE 373 AA; 41240 MW; BE1D86C1A7D7A1B7 CRC64;
MKFIVSSSYL LKKLQVIGGV INSSNTMPIL DNFLFELSPN VLTISASDLE TTVKGALEVE
SDSEGSIAVP AKLLVEILKT FAEQPLTFVA KDNNTIEISS THGKYSLAYL NGEEFPKPVT
LSEANKVTLL GDVLATAIQK TIFAVGNDDL RPTMSGIFFE FNEEGLTFVA TDAHKLVKYQ
RTDIKATETS EFIMPKKPLN LLKGILAGSE TEVIVEYNES NAKFSFDGME FICRLIDGKY
PNYDAVIPKE NPNKLVVNRS QFLNSARRVS IFSNKTTHQV RLKVAGSDLQ VSAEDIDHSN
KADERLVCNY QGDDMEIGFN SRFLIEMLNN LDSDEVMLEM SMPNRAGILT PLDGLDPGEK
VLMLAMPIML NNS
//
