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Database: UniProt/TrEMBL
Entry: A8F8Y5_BACP2
LinkDB: A8F8Y5_BACP2
Original site: A8F8Y5_BACP2 
ID   A8F8Y5_BACP2            Unreviewed;       421 AA.
AC   A8F8Y5;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   19-FEB-2014, entry version 44.
DE   RecName: Full=DNA polymerase III subunit beta;
DE            EC=2.7.7.7;
GN   Name=dnaN; OrderedLocusNames=BPUM_0002;
OS   Bacillus pumilus (strain SAFR-032).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=315750;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SAFR-032;
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: DNA polymerase III is a complex, multichain enzyme
CC       responsible for most of the replicative synthesis in bacteria.
CC       This DNA polymerase also exhibits 3' to 5' exonuclease activity.
CC       The beta chain is required for initiation of replication once it
CC       is clamped onto DNA, it slides freely (bidirectional and ATP-
CC       independent) along duplex DNA (By similarity).
CC   -!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) =
CC       diphosphate + DNA(n+1).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
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DR   EMBL; CP000813; ABV60702.1; -; Genomic_DNA.
DR   RefSeq; YP_001485262.1; NC_009848.1.
DR   ProteinModelPortal; A8F8Y5; -.
DR   STRING; 315750.BPUM_0002; -.
DR   EnsemblBacteria; ABV60702; ABV60702; BPUM_0002.
DR   GeneID; 5619212; -.
DR   KEGG; bpu:BPUM_0002; -.
DR   PATRIC; 18963703; VBIBacPum16546_0002.
DR   eggNOG; COG0592; -.
DR   HOGENOM; HOG000071792; -.
DR   KO; K02338; -.
DR   OMA; DYNRVIP; -.
DR   OrthoDB; EOG65J53F; -.
DR   ProtClustDB; PRK05643; -.
DR   BioCyc; BPUM315750:GH6N-2-MONOMER; -.
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:InterPro.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006261; P:DNA-dependent DNA replication; IEA:GOC.
DR   GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IEA:GOC.
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   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; Cytoplasm; DNA replication;
KW   DNA-directed DNA polymerase; Nucleotidyltransferase; Transferase.
SQ   SEQUENCE   421 AA;  47241 MW;  943380A2E2FB158A CRC64;
     MWIGCLSFLF TDLSTYSQAL LLLLRFLLIK YIYMSLRKFR RTTMKFTIQK DRLVESVQDV
     LKAVSSRTTI PILTGIKIVA SDEGVSLTGS DSDISIESFI PQRDGDLEVI TIDRPGSIVL
     QARFFSEIVK KLPMATVEIE VEQNHLTIIR SGSAEFNLNG LDAEEYPHLP QIEEHHAFQI
     PTDLLKNLIR QTVFAVSTSE TRPILTGVNW KVEKGELICT ATDSHRLALR KAKLDIDEES
     SYNVVIPGKS LTELSRILDD GQDLVSIVIT ETQVLFKAQN VLFFSRLLDG NYPDTARLIP
     QESKTDVVVN TKEFLQAIDR ASLLAREGRN NVVKLSADPE QSLEISSNSP EIGKVVETVQ
     ADDIKGEDLK ISFSPKYMLD ALKVLEGTEI HVSFTGAMRP FLLRTPNDDS ILQLILPVRT
     Y
//
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