ID D9SMK8_CLOC7 Unreviewed; 367 AA.
AC D9SMK8;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 01-MAY-2013, entry version 17.
DE RecName: Full=DNA polymerase III subunit beta;
DE EC=2.7.7.7;
GN OrderedLocusNames=Clocel_0002;
OS Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 /
OS 743B).
OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=573061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35296 / DSM 3052 / OCM 3 / 743B;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N.,
RA Mikhailova N., Hemme C.L., Woyke T.;
RT "Complete sequence of Clostridium cellulovorans 743B.";
RL Submitted (AUG-2010) 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; CP002160; ADL49793.1; -; Genomic_DNA.
DR RefSeq; YP_003841557.1; NC_014393.1.
DR ProteinModelPortal; D9SMK8; -.
DR EnsemblBacteria; ADL49793; ADL49793; Clocel_0002.
DR GeneID; 9606810; -.
DR KEGG; ccb:Clocel_0002; -.
DR PATRIC; 41734914; VBICloCel81632203721_1351.
DR HOGENOM; HOG000071792; -.
DR KO; K02338; -.
DR BioCyc; CCEL573061:GIXD-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: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 367 AA; 40948 MW; F07D10F62A58AF12 CRC64;
MNFTCDKTNL QEAISIAQKA VTGKSTMPIL QGLLLNARGN KLTINSSDID LGIETKCNAN
IKEEGSIVVD SKLFGDIIRK LPNSEIQIKS ISEGTIEITC QRSRFTLVHM KADEFPQLPY
IDEDEIISIP QKLIKNMIRS TIFAIAIDET RPILTGILFE IKNRTLNLVA LDGFRLALKK
ETIDTEQEFS AVIPGKTLHE VVKILEDEGD VDITFTTNHI LFNLGETKVV SRLLEGEFIK
YQAIIPEEHE LSISVNRASL LNSIERASLV SKDASSNLIK FNISEDNIVI TSNSQLGDVR
EEVSIKLLKG NELQIAFNSK YLIDALKIME EETITLQFTS AVSPCIIKNI ENDNVIYLVL
PVRISNS
//
