(data stored in ACNUC7421 zone)

SWISSPROT: D6XUZ6_BACIE

ID   D6XUZ6_BACIE            Unreviewed;       380 AA.
AC   D6XUZ6;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 61.
DE   RecName: Full=Beta sliding clamp {ECO:0000256|PIRNR:PIRNR000804};
GN   OrderedLocusNames=Bsel_0002 {ECO:0000313|EMBL:ADH97554.1};
OS   Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Sporolactobacillaceae;
OC   unclassified Sporolactobacillaceae.
OX   NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH97554.1, ECO:0000313|Proteomes:UP000000271};
RN   [1] {ECO:0000313|EMBL:ADH97554.1, ECO:0000313|Proteomes:UP000000271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC   {ECO:0000313|Proteomes:UP000000271};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Stolz J.;
RT   "Complete sequence of Bacillus selenitireducens MLS10.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Confers DNA tethering and processivity to DNA
CC       polymerases and other proteins. Acts as a clamp, forming a ring
CC       around DNA (a reaction catalyzed by the clamp-loading complex)
CC       which diffuses in an ATP-independent manner freely and
CC       bidirectionally along dsDNA. Initially characterized for its
CC       ability to contact the catalytic subunit of DNA polymerase III
CC       (Pol III), a complex, multichain enzyme responsible for most of
CC       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|PIRNR:PIRNR000804,
CC       ECO:0000256|SAAS:SAAS00729396}.
CC   -!- SIMILARITY: Belongs to the beta sliding clamp family.
CC       {ECO:0000256|PIRNR:PIRNR000804, ECO:0000256|SAAS:SAAS00859809}.
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DR   EMBL; CP001791; ADH97554.1; -; Genomic_DNA.
DR   RefSeq; WP_013170984.1; NC_014219.1.
DR   STRING; 439292.Bsel_0002; -.
DR   EnsemblBacteria; ADH97554; ADH97554; Bsel_0002.
DR   KEGG; bse:Bsel_0002; -.
DR   eggNOG; ENOG4105CZ8; Bacteria.
DR   eggNOG; COG0592; LUCA.
DR   HOGENOM; HOG000071792; -.
DR   KO; K02338; -.
DR   OMA; NYEAVIP; -.
DR   OrthoDB; 1040142at2; -.
DR   BioCyc; BSEL439292:G1GLR-2-MONOMER; -.
DR   Proteomes; UP000000271; 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   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   PANTHER; PTHR30478; PTHR30478; 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   TIGRFAMs; TIGR00663; dnan; 1.
PE   3: Inferred from homology;
DR   PRODOM; D6XUZ6.
DR   SWISS-2DPAGE; D6XUZ6.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000271};
KW   Cytoplasm {ECO:0000256|PIRNR:PIRNR000804,
KW   ECO:0000256|SAAS:SAAS00729481};
KW   DNA replication {ECO:0000256|PIRNR:PIRNR000804,
KW   ECO:0000256|SAAS:SAAS00729460};
KW   DNA-binding {ECO:0000256|SAAS:SAAS00859811};
KW   DNA-directed DNA polymerase {ECO:0000256|PIRNR:PIRNR000804,
KW   ECO:0000256|SAAS:SAAS00729479};
KW   Nucleotidyltransferase {ECO:0000256|PIRNR:PIRNR000804,
KW   ECO:0000256|SAAS:SAAS00729386, ECO:0000313|EMBL:ADH97554.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000271};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000804,
KW   ECO:0000256|SAAS:SAAS00729371, ECO:0000313|EMBL:ADH97554.1}.
FT   DOMAIN        1    127       DNA_pol3_beta. {ECO:0000259|Pfam:
FT                                PF00712}.
FT   DOMAIN      137    252       DNA_pol3_beta_2. {ECO:0000259|Pfam:
FT                                PF02767}.
FT   DOMAIN      256    377       DNA_pol3_beta_3. {ECO:0000259|Pfam:
FT                                PF02768}.
SQ   SEQUENCE   380 AA;  42225 MW;  CF54721694A9F9EA CRC64;
     MKFTIQRDAF VQSVADVSKA ISPRTTIQIL TGIKIVADQD GITLTGSDSD LSIESFIPKE
     KDGEELVNIQ EEGSIVLQAR FFGDMIKKLP ETSIEVAVND QFIAQITSGG SVFNINGIDP
     DEYPRLPDVE EADLFRMPKN LLKTLIRQTA FAVSSVETRP ILTGIHWHLE DSVLTCTATD
     SHRLAMRMAK VDDNENNLSF SNVVIPGKTL TELNKILNDT DELLEVVVAG NQILFKGDYF
     LLYSRLLEGN YPATKNMIPT GSKTSVKLET KRLLDAIERA LLLSREGKNN VVHVKNLESG
     ELEITSVTPE VGKVTEHVTT MSYEGDELKI SFNGKNLIDA LRVMEASEVH INFTGAMSPF
     VLKPIDEDHM LHLFSPVRTY
//

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