ID E1QXL3_OLSUV Unreviewed; 367 AA.
AC E1QXL3;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=Beta sliding clamp {ECO:0000256|PIRNR:PIRNR000804};
GN OrderedLocusNames=Olsu_1778 {ECO:0000313|EMBL:ADK68866.1};
OS Olsenella uli (strain ATCC 49627 / DSM 7084 / CIP 109912 / JCM 12494 /
OS NCIMB 702895 / VPI D76D-27C) (Lactobacillus uli).
OC Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales; Atopobiaceae;
OC Olsenella.
OX NCBI_TaxID=633147 {ECO:0000313|EMBL:ADK68866.1, ECO:0000313|Proteomes:UP000000333};
RN [1] {ECO:0000313|EMBL:ADK68866.1, ECO:0000313|Proteomes:UP000000333}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49627 / DSM 7084 / CIP 109912 / JCM 12494 / NCIMB 702895 /
RC VPI D76D-27C {ECO:0000313|Proteomes:UP000000333};
RX PubMed=21304694; DOI=10.4056/sigs.1082860;
RA Goker M., Held B., Lucas S., Nolan M., Yasawong M., Glavina Del Rio T.,
RA Tice H., Cheng J.F., Bruce D., Detter J.C., Tapia R., Han C., Goodwin L.,
RA Pitluck S., Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A.,
RA Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA Rohde M., Sikorski J., Pukall R., Woyke T., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Lapidus A.;
RT "Complete genome sequence of Olsenella uli type strain (VPI D76D-27C).";
RL Stand. Genomic Sci. 3:76-84(2010).
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; CP002106; ADK68866.1; -; Genomic_DNA.
DR RefSeq; WP_013252617.1; NZ_JQCO01000002.1.
DR AlphaFoldDB; E1QXL3; -.
DR STRING; 633147.Olsu_1778; -.
DR GeneID; 78513161; -.
DR KEGG; ols:Olsu_1778; -.
DR PATRIC; fig|633147.7.peg.1485; -.
DR eggNOG; COG0592; Bacteria.
DR HOGENOM; CLU_038149_2_1_11; -.
DR OrthoDB; 468978at2; -.
DR Proteomes; UP000000333; Chromosome.
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:UP000000333};
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 128..242
FT /note="DNA polymerase III beta sliding clamp central"
FT /evidence="ECO:0000259|Pfam:PF02767"
FT DOMAIN 244..366
FT /note="DNA polymerase III beta sliding clamp C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02768"
SQ SEQUENCE 367 AA; 39657 MW; 3771618069BA5E5E CRC64;
MKFSVSQSSL SQALAVVSKG MGSNSTLPIL SGILITAAEG TLTFQTTDLT INVRHRIAAM
VEEAGSTVVS GKILMNIVKT LPDAAVSFEG GERVVSISCD KSTFRLNTLD PSDFPEFPQF
ALGRTIELPS SLLSEMVDKV YKVTSRDTSR PILSGVLLSV EENTIRLVAT DSYRLAVCDS
NAETSSADEA FQTIVPGMTF HDVLTLPSMT EKVLIGTTDS QVVFVFGNTT YITRKIEGNF
PNYKQLLPAD CNTSVKVNVS EFASALKRVS VIALANPSVR VDIDTDGGVM KLSASSPDQG
ESTELLPVDV EGQSMSIALN YHYVFDCVNA AANEKEITLE LLSAMQPGIF KSYAKINYLY
LLMPVRM
//
