ID A6LPB2_CLOB8 Unreviewed; 366 AA.
AC A6LPB2;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 01-MAY-2013, entry version 45.
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 ProtClustDB; PRK05643; -.
DR BioCyc; CBEI290402:GHL5-143-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 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
//
