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Database: UniProt/TrEMBL
Entry: C9RXR8_GEOSY
LinkDB: C9RXR8_GEOSY
Original site: C9RXR8_GEOSY 
ID   C9RXR8_GEOSY            Unreviewed;       378 AA.
AC   C9RXR8;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   01-MAY-2013, entry version 26.
DE   RecName: Full=DNA polymerase III subunit beta;
DE            EC=2.7.7.7;
GN   OrderedLocusNames=GYMC61_0002;
OS   Geobacillus sp. (strain Y412MC61).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=544556;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y412MC61;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Brumm P., Mead D.;
RT   "Complete sequence of chromosome of Geobacillus sp. Y412MC61.";
RL   Submitted (OCT-2009) 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; CP001794; ACX76702.1; -; Genomic_DNA.
DR   RefSeq; YP_003251184.1; NC_013411.1.
DR   STRING; 544556.GYMC61_0002; -.
DR   EnsemblBacteria; ACX76702; ACX76702; GYMC61_0002.
DR   GeneID; 8523773; -.
DR   KEGG; gyc:GYMC61_0002; -.
DR   PATRIC; 32161336; VBIGeoSp85804_0002.
DR   eggNOG; COG0592; -.
DR   HOGENOM; HOG000071792; -.
DR   KO; K02338; -.
DR   OMA; DYNRVIP; -.
DR   BioCyc; GSP544556:GI3L-42-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   378 AA;  42063 MW;  6B9ADEAD96ECE0FA CRC64;
     MNISIDREAL AKSVQDVMKA VSTRTTIPIL TGIKLTATAS GVTLTGSDSD ISIESFIPLE
     KEGKLLVDVK RPGSIVLQAR FFSEIVKKLP QQTVEIERED NFLTIIRSGH SEFRLNGLNA
     DEYPRLPQIE EENVFQIPAD LLKTVIRQTV FAVSTSETRP ILTGVNWKVE HGELVCTATD
     SHRLAMRKVK IESENEVSYN VVIPGKSLNE LSKILDDGNH PVDIVMTANQ VLFKAEHLLF
     FSRLLDGNYP ETARLIPTES KTTMIVNAKE FLQAIDRASL LAREGRNNVV KLTTLPGGML
     EISSISPEIG KVTEQLQTES LEGEELNISF SAKYMMDALR ALDGTDIQIS FTGAMRPFLL
     RPLHTDSMLQ LILPVRTY
//
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