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Database: UniProt/TrEMBL
Entry: A8F8Y5_BACP2
LinkDB: A8F8Y5_BACP2
Original site: A8F8Y5_BACP2 
ID   A8F8Y5_BACP2            Unreviewed;       378 AA.
AC   A8F8Y5;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 2.
DT   28-FEB-2018, entry version 74.
DE   RecName: Full=Beta sliding clamp {ECO:0000256|PIRNR:PIRNR000804};
GN   OrderedLocusNames=BPUM_0002 {ECO:0000313|EMBL:ABV60702.2};
OS   Bacillus pumilus (strain SAFR-032).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=315750 {ECO:0000313|EMBL:ABV60702.2, ECO:0000313|Proteomes:UP000001355};
RN   [1] {ECO:0000313|EMBL:ABV60702.2, ECO:0000313|Proteomes:UP000001355}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SAFR-032 {ECO:0000313|EMBL:ABV60702.2,
RC   ECO:0000313|Proteomes:UP000001355};
RX   PubMed=17895969; DOI=10.1371/journal.pone.0000928;
RA   Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D.,
RA   Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C.,
RA   Dinh H., Lee S., Nazareth L., Blyth P., Holder M., Buhay C.,
RA   Tirumalai M.R., Liu Y., Dasgupta I., Bokhetache L., Fujita M.,
RA   Karouia F., Eswara Moorthy P., Siefert J., Uzman A., Buzumbo P.,
RA   Verma A., Zwiya H., McWilliams B.D., Olowu A., Clinkenbeard K.D.,
RA   Newcombe D., Golebiewski L., Petrosino J.F., Nicholson W.L., Fox G.E.,
RA   Venkateswaran K., Highlander S.K., Weinstock G.M.;
RT   "Paradoxical DNA repair and peroxide resistance gene conservation in
RT   Bacillus pumilus SAFR-032.";
RL   PLoS ONE 2:E928-E928(2007).
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; CP000813; ABV60702.2; -; Genomic_DNA.
DR   RefSeq; WP_041815072.1; NC_009848.4.
DR   ProteinModelPortal; A8F8Y5; -.
DR   STRING; 315750.BPUM_0002; -.
DR   EnsemblBacteria; ABV60702; ABV60702; BPUM_0002.
DR   GeneID; 31666583; -.
DR   KEGG; bpu:BPUM_0002; -.
DR   eggNOG; ENOG4105CZ8; Bacteria.
DR   eggNOG; COG0592; LUCA.
DR   HOGENOM; HOG000071792; -.
DR   KO; K02338; -.
DR   OrthoDB; POG091H02B3; -.
DR   BioCyc; BPUM315750:G1G9U-2-MONOMER; -.
DR   Proteomes; UP000001355; 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;
KW   Complete proteome {ECO:0000313|Proteomes:UP000001355};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001355};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000804,
KW   ECO:0000256|SAAS:SAAS00729371}.
FT   DOMAIN        1    127       DNA_pol3_beta. {ECO:0000259|Pfam:
FT                                PF00712}.
FT   DOMAIN      136    251       DNA_pol3_beta_2. {ECO:0000259|Pfam:
FT                                PF02767}.
FT   DOMAIN      254    376       DNA_pol3_beta_3. {ECO:0000259|Pfam:
FT                                PF02768}.
SQ   SEQUENCE   378 AA;  42022 MW;  06EF05DB899FA59C CRC64;
     MKFTIQKDRL VESVQDVLKA VSSRTTIPIL TGIKIVASDE GVSLTGSDSD ISIESFIPQR
     DGDLEVITID RPGSIVLQAR FFSEIVKKLP MATVEIEVEQ NHLTIIRSGS AEFNLNGLDA
     EEYPHLPQIE EHHAFQIPTD LLKNLIRQTV FAVSTSETRP ILTGVNWKVE KGELICTATD
     SHRLALRKAK LDIDEESSYN VVIPGKSLTE LSRILDDGQD LVSIVITETQ VLFKAQNVLF
     FSRLLDGNYP DTARLIPQES KTDVVVNTKE FLQAIDRASL LAREGRNNVV KLSADPEQSL
     EISSNSPEIG KVVETVQADD IKGEDLKISF SPKYMLDALK VLEGTEIHVS FTGAMRPFLL
     RTPNDDSILQ LILPVRTY
//
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