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Database: UniProt/TrEMBL
Entry: A6LPB2_CLOB8
LinkDB: A6LPB2_CLOB8
Original site: A6LPB2_CLOB8 
ID   A6LPB2_CLOB8            Unreviewed;       366 AA.
AC   A6LPB2;
DT   24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2007, sequence version 1.
DT   19-FEB-2014, entry version 49.
DE   RecName: Full=DNA polymerase III subunit beta;
DE            EC=2.7.7.7;
GN   OrderedLocusNames=Cbei_0002;
OS   Clostridium beijerinckii (strain ATCC 51743 / NCIMB 8052) (Clostridium
OS   acetobutylicum).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=290402;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51743 / NCIMB 8052;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Sims D., Brettin T., Bruce D., Tapia R., Brainard J.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Bennet G., Cann I., Chen J.-S., Contreras A.L.,
RA   Jones D., Kashket E., Mitchell W., Stoddard S., Schwarz W.,
RA   Qureshi N., Young M., Shi Z., Ezeji T., White B., Blaschek H.,
RA   Richardson P.;
RT   "Complete sequence of Clostridium beijerinckii NCIMB 8052.";
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000721; ABR32192.1; -; Genomic_DNA.
DR   RefSeq; YP_001307148.1; NC_009617.1.
DR   ProteinModelPortal; A6LPB2; -.
DR   STRING; 290402.Cbei_0002; -.
DR   EnsemblBacteria; ABR32192; ABR32192; Cbei_0002.
DR   GeneID; 5291236; -.
DR   KEGG; cbe:Cbei_0002; -.
DR   PATRIC; 19343772; VBICloBei69853_0002.
DR   eggNOG; COG0592; -.
DR   HOGENOM; HOG000071792; -.
DR   KO; K02338; -.
DR   OMA; DYNRVIP; -.
DR   OrthoDB; EOG65J53F; -.
DR   ProtClustDB; PRK05643; -.
DR   BioCyc; CBEI290402:GHL5-2-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   366 AA;  41480 MW;  8F5D22917C7AAFCB CRC64;
     MIFTCEKQKI LEGISIVQKA ITGKSTMPIL EGIYINANNS TITLIGSDMD VSIQTLVDAT
     IMEEGSIVID AKIFGEIIRK LPNSTIRIET MENQLIKITC EKSIFDVVYM NTNEFPELPE
     INENLKISVN QNILKNMIKG TSFAIAQDET RPILQGILFE VRNKNLNLVA LDGYRLAIKS
     EFLDTDIDIE VVIPGKTLNE VSKILEDIDE IVDITFTNNH ILFNLKRTKI ISRLLEGKFI
     NYKSLLPQEH KLFVNVNRQE LQNAIERASL MAKDGNTNLI KLDLHQDNLV ITSNSQLGKV
     RDEISIKLQG DEIEIAFNSK YLLDVLKNME DNEVVMKMTS GISPCVIEEH NNENAKYLVL
     PVRLMR
//
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