ID E6K3E5_9BACT Unreviewed; 374 AA.
AC E6K3E5;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Beta sliding clamp {ECO:0000256|PIRNR:PIRNR000804};
GN Name=dnaN {ECO:0000313|EMBL:EFU32028.1};
GN ORFNames=HMPREF6485_0130 {ECO:0000313|EMBL:EFU32028.1};
OS Segatella buccae ATCC 33574.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Segatella.
OX NCBI_TaxID=873513 {ECO:0000313|EMBL:EFU32028.1, ECO:0000313|Proteomes:UP000003112};
RN [1] {ECO:0000313|EMBL:EFU32028.1, ECO:0000313|Proteomes:UP000003112}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33574 {ECO:0000313|EMBL:EFU32028.1,
RC ECO:0000313|Proteomes:UP000003112};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (OCT-2010) 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:EFU32028.1}.
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DR EMBL; AEPD01000005; EFU32028.1; -; Genomic_DNA.
DR RefSeq; WP_004342423.1; NZ_GL586311.1.
DR AlphaFoldDB; E6K3E5; -.
DR STRING; 873513.HMPREF6485_0130; -.
DR eggNOG; COG0592; Bacteria.
DR HOGENOM; CLU_038149_4_1_10; -.
DR Proteomes; UP000003112; 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:UP000003112};
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 133..245
FT /note="DNA polymerase III beta sliding clamp central"
FT /evidence="ECO:0000259|Pfam:PF02767"
FT DOMAIN 248..370
FT /note="DNA polymerase III beta sliding clamp C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02768"
SQ SEQUENCE 374 AA; 41376 MW; 30ED94263BC33100 CRC64;
MRFTLSSTAL SSRLNTLARV INSKNALPIL DCFLFQVENN RLLITAGDGE NVMQSALELD
SCEGEGEFAV PNRTILDAVK ELPEQPLNFD IDTQSFAIKI VYQNGLYNFT AQNAEEYPRM
QPVEDGATTM TMDAAVLVDN ISRSLFATAQ DELRPVMNGI YFDLTPDALA IVASDGHKLV
RNKNFNIKSE TPAAFILPKK PASLLKNVLS KDGGEVIVKF NDRSAEMRFS DGVLYCRLIE
GRYPNYNSVI PQDNPNRVTI DRRALLGALR RVLPFASESS QLVRFHVESG RMELSGEDID
FATSAKEQVT CEYSGQPMSI GFKGGSMQEI LSSLESDEVV IELADPSRAG TVMPSQQPEN
EDVLMLLMPM LLND
//
