GenomeNet

Database: UniProt
Entry: A0A074MKY6_9SPHN
LinkDB: A0A074MKY6_9SPHN
Original site: A0A074MKY6_9SPHN 
ID   A0A074MKY6_9SPHN        Unreviewed;       375 AA.
AC   A0A074MKY6;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Beta sliding clamp {ECO:0000256|ARBA:ARBA00021035, ECO:0000256|PIRNR:PIRNR000804};
GN   ORFNames=EH32_14860 {ECO:0000313|EMBL:KEO92538.1};
OS   Erythrobacter litoralis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX   NCBI_TaxID=39960 {ECO:0000313|EMBL:KEO92538.1, ECO:0000313|Proteomes:UP000027866};
RN   [1] {ECO:0000313|EMBL:KEO92538.1, ECO:0000313|Proteomes:UP000027866}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 8509 {ECO:0000313|EMBL:KEO92538.1,
RC   ECO:0000313|Proteomes:UP000027866};
RA   Zheng Q.;
RT   "A comprehensive comparison of genomes of Erythrobacter spp. Strains.";
RL   Submitted (APR-2014) 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:KEO92538.1}.
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; JMIX01000009; KEO92538.1; -; Genomic_DNA.
DR   RefSeq; WP_034904821.1; NZ_JMIX01000009.1.
DR   AlphaFoldDB; A0A074MKY6; -.
DR   KEGG; elq:Ga0102493_112302; -.
DR   PATRIC; fig|39960.10.peg.1395; -.
DR   OrthoDB; 8421503at2; -.
DR   Proteomes; UP000027866; 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:UP000027866};
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          131..252
FT                   /note="DNA polymerase III beta sliding clamp central"
FT                   /evidence="ECO:0000259|Pfam:PF02767"
FT   DOMAIN          255..374
FT                   /note="DNA polymerase III beta sliding clamp C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02768"
SQ   SEQUENCE   375 AA;  40660 MW;  47172239D56AF937 CRC64;
     MKATIERATL LRCLSHVQSV VERRNTIPIL SNVLIEASEG GAVKVMATDL DLQVVETMTA
     ASVDSPGAIT VSAHLLFDIA RKLPDGSQVS LETADNRMEV KAGRSRFKLP TLPRDDFPVI
     VEGDLPTSFE LPARTLAELI DRTRFAISTE ETRYYLNGIF LHVTDEDEPV LKAAATDGHR
     LARFTIARPE GASGMPDVIV PRKAVGELRK LLDEALDGNV LVDLSASKIR FTLGGEGGVV
     LTSKLIDGTF PDYSRVIPTG NDKLLKVDPK LFFAGVDRVA TIATEKTRAV KMGLEPDKVT
     LSVTSPDNGT ATEELAASYA SESFEIGFNA NYLKDILDQI DADEVELHLA DAGAPTLIRK
     DESSPALYVL MPMRV
//
DBGET integrated database retrieval system