ID A0A086ZKZ7_9BIFI Unreviewed; 374 AA.
AC A0A086ZKZ7;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Beta sliding clamp {ECO:0000256|PIRNR:PIRNR000804};
GN Name=dnaN {ECO:0000313|EMBL:NMF02621.1};
GN ORFNames=BBOU_1170 {ECO:0000313|EMBL:KFI47197.1}, HF843_05455
GN {ECO:0000313|EMBL:NMF02621.1};
OS Bifidobacterium boum.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=78343 {ECO:0000313|EMBL:KFI47197.1, ECO:0000313|Proteomes:UP000029093};
RN [1] {ECO:0000313|EMBL:KFI47197.1, ECO:0000313|Proteomes:UP000029093}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 10736 {ECO:0000313|EMBL:KFI47197.1,
RC ECO:0000313|Proteomes:UP000029093};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:NMF02621.1, ECO:0000313|Proteomes:UP000583419}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WCA-130-P53-4B {ECO:0000313|EMBL:NMF02621.1,
RC ECO:0000313|Proteomes:UP000583419};
RA Hitch T.C.A., Wylensek D., Clavel T.;
RL Submitted (APR-2020) 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:KFI47197.1}.
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; JGYQ01000015; KFI47197.1; -; Genomic_DNA.
DR EMBL; JABAGJ010000006; NMF02621.1; -; Genomic_DNA.
DR RefSeq; WP_026503015.1; NZ_JGYQ01000015.1.
DR AlphaFoldDB; A0A086ZKZ7; -.
DR OrthoDB; 468978at2; -.
DR Proteomes; UP000029093; Unassembled WGS sequence.
DR Proteomes; UP000583419; 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 Reference proteome {ECO:0000313|Proteomes:UP000029093};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000804}.
FT DOMAIN 1..118
FT /note="DNA polymerase III beta sliding clamp N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00712"
FT DOMAIN 127..243
FT /note="DNA polymerase III beta sliding clamp central"
FT /evidence="ECO:0000259|Pfam:PF02767"
FT DOMAIN 247..357
FT /note="DNA polymerase III beta sliding clamp C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02768"
SQ SEQUENCE 374 AA; 40950 MW; E7C9B32A69952284 CRC64;
MKVEVNTTSL ADAVAWTTRV IDARPASPIL AGIKLEAIDG TLQLSTFNFE ISARDHIEAG
VDEAGSSVVQ GKILADITKS LPSEKTYLAT ENSTLIITSG KAKFTMQLMP ESEYPDLPAV
PRILGKVDGE TFHQAVDQAC VAVSREETRP VLTGVYMQFE GDKVVMTSTD RFRLSRATFT
WSPENPDVST STLLRGSLLR DVARTLNDSQ NVVIDFDEDN PSLIAFENAG RISTSQLIDG
EFPAIDRLFA DEYPIQAVID KQQLISSIKR VSLVAERNAP IRMAFSDGSV TLSAGVADEN
QASDVIDVDF DGEDITVAFN PGYLIEGLSA IAEPFVRMKM TTAIKPVEFN GQQEADSDES
MDYRYLLVPM RFTN
//
