ID A0A3P5WHX2_9RHOB Unreviewed; 372 AA.
AC A0A3P5WHX2;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=Beta sliding clamp {ECO:0000256|ARBA:ARBA00021035, ECO:0000256|PIRNR:PIRNR000804};
GN Name=dnaN {ECO:0000313|EMBL:VDC20372.1};
GN ORFNames=XINFAN_00458 {ECO:0000313|EMBL:VDC20372.1};
OS Pseudogemmobacter humi.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Pseudogemmobacter.
OX NCBI_TaxID=2483812 {ECO:0000313|EMBL:VDC20372.1, ECO:0000313|Proteomes:UP000277498};
RN [1] {ECO:0000313|EMBL:VDC20372.1, ECO:0000313|Proteomes:UP000277498}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACIP111625 {ECO:0000313|EMBL:VDC20372.1};
RA Criscuolo A.;
RL Submitted (NOV-2018) 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; UXAW01000033; VDC20372.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3P5WHX2; -.
DR OrthoDB; 8421503at2; -.
DR Proteomes; UP000277498; 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-binding {ECO:0000256|ARBA:ARBA00023125};
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:UP000277498};
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 134..249
FT /note="DNA polymerase III beta sliding clamp central"
FT /evidence="ECO:0000259|Pfam:PF02767"
FT DOMAIN 252..371
FT /note="DNA polymerase III beta sliding clamp C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02768"
SQ SEQUENCE 372 AA; 40384 MW; 736A9B3157373FCF CRC64;
MKLSIERGTL LKALAQAQSV VERRNTIPIL ANVLIEAEGA QVSFRATDLD IEVVDRADAM
VERAGATTVS AIMLHEIVRK LPDGALVNLS EDGASGRLTI TAGRSTFSLA TLPKEDFPVM
ASSEYATNFS APAADLRRLF DKAKFAISTE ETRYYLNGVY LHVSTSEDGP VLRAVATDGH
RLARIDAALP GGAEAMPGVI VPRKTVNELR KLLDDDEAKI AVSVSETKIR FATPAITLTS
KVIDGTFPDY TRVIPQHNTR RLEVDASEFA RAVDRVATVS SERSRAVKLS LDEDRLVLSV
NAPDSGAAEE ELAVAYGDER LEIGFNAKYL LEIASQVDRE NAVFLFNSSG DPTLMREGND
TSAVYVVMPM RV
//