MG1655
W3110
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Gene Report : dnaQ
PEC Original Annotations
Essentiality
     Class non-essential
     References (PMID)
J Bacteriol. 1994;176(3):815-21.
holE, the gene coding for the theta subunit of DNA polymerase III of Escherichia coli: characterization of a holE mutant and comparison with a dnaQ (epsilon-subunit) mutant.
Slater SC, Lifsics MR, O'Donnell M, Maurer R. ( 8300534 )
     Deletion OCR36 (D)  
Related gene (W3110 PEC)
     Gene Search Search MG1655 PEC by gene name:  dnaQ
Related strains
     Strains Search Search strains by gene name:  dnaQ   Search strains by all related name:  dnaQ b0215 ECK0215 JW0205 mutD

General information  (Go to Linear View:)
 Gene Name dnaQ  
 Alternative name b0215,ECK0215,JW0205,mutD  
 Location, Length 236,067 - 236,798 (  +  ) ;   5.09 min ; 732 (bp) ,   243 (aa) Go to Linear View
 Product DNA polymerase III epsilon subunit  
 Operon Name dnaQ  
 Note DNA polymerase III, epsilon subunit; GO_component: GO:0005737 - cytoplasm; GO_process: GO:0006261 - DNA-dependent DNA replication; GO_process: GO:0006457 - protein folding  
 Function enzyme; DNA - replication, repair,restriction/modification  
 Gene Ontology GO:0000287 ; magnesium ion binding ( dnaQ )
GO:0003676 ; nucleic acid binding ( dnaQ )
GO:0003677 ; DNA binding ( dnaQ )
GO:0003887 ; DNA-directed DNA polymerase activity ( dnaQ )
GO:0004518 ; nuclease activity ( dnaQ )
GO:0004527 ; exonuclease activity ( dnaQ )
GO:0005515 ; protein binding ( dnaQ )
GO:0005622 ; intracellular ( dnaQ )
GO:0006260 ; DNA replication ( dnaQ )
GO:0016740 ; transferase activity ( dnaQ )
GO:0016779 ; nucleotidyltransferase activity ( dnaQ )
GO:0016787 ; hydrolase activity ( dnaQ )
GO:0030145 ; manganese ion binding ( dnaQ )
GO:0046872 ; metal ion binding ( dnaQ )
 PID 1786409  
 EC number
  (KEGG Pathway)
 
2.7.7.7  
SWISS-PROT  ( Show details [ 2 more] )
  botton Entry name(Acc.no) DP3E_ECOLI ( P03007 )
    -  Protein name DNA polymerase III, epsilon chain  
    -  Synonyms EC 2.7.7.7  
    -  Gene name Name=dnaQ; Synonyms=mutD; OrderedLocusNames=b0215;  

 Linear View (Whole Mode)
View Location
   225.0  –  250.0 (KBP)

Homology Analysis
BLAST
    Bacteria
         GTOP dnaQ (  homologous genes of other bacterias  )  
    PDB     (database updated : 2007.02.20 )
         PSI-BLAST Chain A, Structure Of The N-Terminal Exonuclease Domain Of The Epsilon Subunit Of E.Coli Dna Polymerase Iii At Ph 8.5  
    SWISS-PROT     (database updated : 2007.02.20 )
         BLAST DNA polymerase III subunit epsilon  
         PSI-BLAST DNA polymerase III subunit epsilon
    nr     (database updated : 2007.02.20 )
         BLAST DNA polymerase III epsilon chain [Escherichia coli]  
Pfam 28.0   (database updated : 2015-05 )
    Pfam
PROSITE
    PROSITE CAMP_PHOSPHO_SITE    PKC_PHOSPHO_SITE    CK2_PHOSPHO_SITE    MYRISTYL    AMIDATION     

Other Cross-Reference
    COG COG0847L 
    EcoCyc dnaQ 

MMBR References
J Biol Chem. 1984;259:5567-5573
The interaction of DNA polymerase III and the product of the Escherichia coli mutator gene, mutD.
DiFrancesco, R., S. K. Bhatnagar, A. Brown, and M. J. Bessman.
Proc Natl Acad Sci U S A. 1983;80:2189-2192
Mutator strains of Escherichia coli, mutD and dnaQ, with defective exonucleolytic editing by DNA polymerase III holoenzyme.
Echols, H., C. Lu, and P. M. J. Burgers.
J Bacteriol. 1997;179:7435-7445
Genetic requirements and mutational specificity of the Escherichia coli SOS mutator activity.
Fijalkowska, I. J., R. L. Dunn, and R. M. Schaaper.
J Bacteriol. 1968;96(4):975-80.
Selection of a mutant of Escherichia coli which has high mutation rates.
Helling RB. ( 4879569 )
Proc Natl Acad Sci U S A. 1981;78:3770-3774
Identification of the dnaQ gene product and location of the structural gene for RNase H of Escherichia coli by cloning of the genes.
Horiuchi, T., H. Maki, M. Maruyana, and M. Sekiguchi.
Annu Rev Biochem. 1995;64:171-200.
DNA polymerase III holoenzyme: structure and function of a chromosomal replicating machine.
Kelman Z, O'Donnell M. ( 7574479 )
Proc Natl Acad Sci U S A. 1983;80:7137-7141
Structure and expression of the dnaQ mutator and the RNase H genes of Escherichia coli: overlap of the promoter regions.
Maki, H., T. Horiuchi, and M. Sekiguchi.
J Mol Biol. 1983;167(4):757-71.
A dominant (mutD5) and a recessive (dnaQ49) mutator of Escherichia coli.
Maruyama M, Horiuchi T, Maki H, Sekiguchi M. ( 6224021 )
J Biol Chem. 1985;260:7122-7125
Transcriptional organization of the convergent overlapping dnaQ-rnh genes of Escherichia coli.
Nomura, T., H. Aiba, and A. Ishihama.
Mol Microbiol. 1997;25(2):237-46.
The ssb-113 allele suppresses the dnaQ49 mutator and alters DNA supercoiling in Escherichia coli.
Quinones A, Neumann S. ( 9282736 )
Proc Natl Acad Sci U S A. 1983;80:7085-7089
Identification of the E-subunit of Escherichia coli DNA polymerase III holoenzyme as the dnaQ gene product: a fidelity subunit for DNA replication.
Scheurmann, R., S. Tam, P. M. J. Burgers, C. Lu, and H. Echols.
J Bacteriol. 1967;94(1):38-47.
Mutator gene of Escherichia coli B.
Siegel EC, Bryson V. ( 5338974 )
Mol Gen Genet. 1986;205(1):9-13.
Structure and function of dnaQ and mutD mutators of Escherichia coli.
Takano K, Nakabeppu Y, Maki H, Horiuchi T, Sekiguchi M. ( 3540531 )
J Bacteriol. 1992;174:7750-7756
The gene coding for 3-deoxy-manno-octulosonic acid transferase and the rfaQ gene are transcribed from divergently arranged promoters in Escherichia coli.
Clementz, T.
J Mol Biol. 1986;190(1):113-7.
DNA sequence and coding properties of mutD(dnaQ) a dominant Escherichia coli mutator gene.
Cox EC, Horner DL. ( 3023634 )
Genetics 1974;77:169-184
Selection for high mutation rates in chemostats.
Cox, E. C., and T. Gibson.

Sequences
Amino acid
FASTA format
0001 MSTAITRQIV LDTETTGMNQ IGAHYEGHKI IEIGAVEVVN RRLTGNNFHV YLKPDRLVDP EAFGVHGIAD 
0071 EFLLDKPTFA EVADEFMDYI RGAELVIHNA AFDIGFMDYE FSLLKRDIPK TNTFCKVTDS LAVARKMFPG 
0141 KRNSLDALCA RYEIDNSKRT LHGALLDAQI LAEVYLAMTG GQTSMAFAME GETQQQQGEA TIQRIVRQAS 
0211 KLRVVFATDE EIAAHEARLD LVQKKGGSCL WRA

Nucleotide
FASTA format

View sequence out neighbor 100bp
-100                                             CGAACCATCG GTGAAAATTT CTACCTGTTT 
-070 AAGCATCTCT GGTAGACTTC CTGTAATTGA ATCGAACTGT AAAACGACAA GTCTGACATA AATGACCGCT 
0001 atgagcactg caattacacg ccagatcgtt ctcgataccg aaaccaccgg tatgaaccag attggtgcgc 
0071 actatgaagg ccacaagatc attgagattg gtgccgttga agtggtgaac cgtcgcctga cgggcaataa 
0141 cttccatgtt tatctcaaac ccgatcggct ggtggatccg gaagcctttg gcgtacatgg tattgccgat 
0211 gaatttttgc tcgataagcc cacgtttgcc gaagtagccg atgagttcat ggactatatt cgcggcgcgg 
0281 agttggtgat ccataacgca gcgttcgata tcggctttat ggactacgag ttttcgttgc ttaagcgcga 
0351 tattccgaag accaatactt tctgtaaggt caccgatagc cttgcggtgg cgaggaaaat gtttcccggt 
0421 aagcgcaaca gcctcgatgc gttatgtgct cgctacgaaa tagataacag taaacgaacg ctgcacgggg 
0491 cattactcga tgcccagatc cttgcggaag tttatctggc gatgaccggt ggtcaaacgt cgatggcttt 
0561 tgcgatggaa ggagagacac aacagcaaca aggtgaagca acaattcagc gcattgtacg tcaggcaagt 
0631 aagttacgcg ttgtttttgc gacagatgaa gagattgcag ctcatgaagc ccgtctcgat ctggtgcaga 
0701 agaaaggcgg aagttgcctc tggcgagcat aaATACCTGT GAAAGGCGCT AAAAATAGCG ACTTGGGCGA 
0771 TTTTTGCAGC AAACGATTCA AAAGATGAGA AAAACCGTTG ACGAAGGTCG AGGCAATCCG TA