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Database: UniProt
Entry: A0A323VFB7_9ACTN
LinkDB: A0A323VFB7_9ACTN
Original site: A0A323VFB7_9ACTN 
ID   A0A323VFB7_9ACTN        Unreviewed;       386 AA.
AC   A0A323VFB7;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=Beta sliding clamp {ECO:0000256|PIRNR:PIRNR000804};
GN   ORFNames=DMO24_07465 {ECO:0000313|EMBL:PZA21966.1}, FHX36_003088
GN   {ECO:0000313|EMBL:MBB3677353.1};
OS   Modestobacter versicolor.
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Modestobacter.
OX   NCBI_TaxID=429133 {ECO:0000313|EMBL:PZA21966.1, ECO:0000313|Proteomes:UP000247602};
RN   [1] {ECO:0000313|EMBL:PZA21966.1, ECO:0000313|Proteomes:UP000247602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CP153-2 {ECO:0000313|EMBL:PZA21966.1,
RC   ECO:0000313|Proteomes:UP000247602};
RA   Gundlapally S.R.;
RT   "Draft genome sequence of Modestobacter versicolor CP153-2.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:MBB3677353.1, ECO:0000313|Proteomes:UP000580718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16678 {ECO:0000313|EMBL:MBB3677353.1,
RC   ECO:0000313|Proteomes:UP000580718};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (AUG-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:PZA21966.1}.
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DR   EMBL; JACIBU010000001; MBB3677353.1; -; Genomic_DNA.
DR   EMBL; QKNV01000055; PZA21966.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A323VFB7; -.
DR   OrthoDB; 468978at2; -.
DR   Proteomes; UP000247602; Unassembled WGS sequence.
DR   Proteomes; UP000580718; 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:UP000247602};
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..244
FT                   /note="DNA polymerase III beta sliding clamp central"
FT                   /evidence="ECO:0000259|Pfam:PF02767"
FT   DOMAIN          249..358
FT                   /note="DNA polymerase III beta sliding clamp C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02768"
SQ   SEQUENCE   386 AA;  40766 MW;  4E4EADD50FA2E362 CRC64;
     MKFRVAREVL AEAVAWTARS LPPRPSVPVL AGILLEVEGN QLSVSGFDYE VSARSEVDVQ
     STESGRTLVP GRLLAEITRA LPPHPVDVVA EGARLAISCG NAKFSLPTLP VEDYPSLPSL
     PSTAGTVDSD AFAEAVSQVA VAAGRDDTLP MLTGVRLEIE DDLVTLAATD RYRLAVREFA
     WRPETPGLSA AVLVPARTLA DAAKTLTSGP EVTLSLSSGG SGEGILGLSG KDRQTTTRLL
     DAEFVKYRAI MPSESSSFAT LPVGLFTDAA KRVALVAERG TPLRCEFTSG QVTLRAGGTD
     DEGQAEERCD VEFDGDPLTI GFNPTFLLDG LAAVHTDRAR MDFTTALKPA VLSGVEEPSG
     DEGDGGRPAE RAGSYRYLIM PVRLPG
//
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