ID A8F8Y5_BACP2 Unreviewed; 421 AA.
AC A8F8Y5;
DT 13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2007, sequence version 1.
DT 01-MAY-2013, entry version 39.
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 ProtClustDB; PRK05643; -.
DR BioCyc; BPUM315750:GH6N-95-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:0006260; P:DNA replication; IEA:UniProtKB-KW.
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
//
