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P00582 (DPO1_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 159. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA polymerase I

Short name=POL I
EC=2.7.7.7
Gene names
Name:polA
Synonyms:resA
Ordered Locus Names:b3863, JW3835
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length928 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

In addition to polymerase activity, this DNA polymerase exhibits 3' to 5' and 5' to 3' exonuclease activity. It is able to utilize nicked circular duplex DNA as a template and can unwind the parental DNA strand from its template.

Catalytic activity

Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).

Subunit structure

Single-chain monomer with multiple functions.

Sequence similarities

Belongs to the DNA polymerase type-A family.

Contains 1 3'-5' exonuclease domain.

Contains 1 5'-3' exonuclease domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 928928DNA polymerase I
PRO_0000101239

Regions

Domain1 – 3233235'-3' exonuclease
Domain324 – 5171943'-5' exonuclease
Region324 – 928605Klenow fragment
Region521 – 928408Polymerase

Secondary structure

............................................................................................................ 928
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00582 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: DAAE1C448A59030C

FASTA928103,118
        10         20         30         40         50         60 
MVQIPQNPLI LVDGSSYLYR AYHAFPPLTN SAGEPTGAMY GVLNMLRSLI MQYKPTHAAV 

        70         80         90        100        110        120 
VFDAKGKTFR DELFEHYKSH RPPMPDDLRA QIEPLHAMVK AMGLPLLAVS GVEADDVIGT 

       130        140        150        160        170        180 
LAREAEKAGR PVLISTGDKD MAQLVTPNIT LINTMTNTIL GPEEVVNKYG VPPELIIDFL 

       190        200        210        220        230        240 
ALMGDSSDNI PGVPGVGEKT AQALLQGLGG LDTLYAEPEK IAGLSFRGAK TMAAKLEQNK 

       250        260        270        280        290        300 
EVAYLSYQLA TIKTDVELEL TCEQLEVQQP AAEELLGLFK KYEFKRWTAD VEAGKWLQAK 

       310        320        330        340        350        360 
GAKPAAKPQE TSVADEAPEV TATVISYDNY VTILDEETLK AWIAKLEKAP VFAFDTETDS 

       370        380        390        400        410        420 
LDNISANLVG LSFAIEPGVA AYIPVAHDYL DAPDQISRER ALELLKPLLE DEKALKVGQN 

       430        440        450        460        470        480 
LKYDRGILAN YGIELRGIAF DTMLESYILN SVAGRHDMDS LAERWLKHKT ITFEEIAGKG 

       490        500        510        520        530        540 
KNQLTFNQIA LEEAGRYAAE DADVTLQLHL KMWPDLQKHK GPLNVFENIE MPLVPVLSRI 

       550        560        570        580        590        600 
ERNGVKIDPK VLHNHSEELT LRLAELEKKA HEIAGEEFNL SSTKQLQTIL FEKQGIKPLK 

       610        620        630        640        650        660 
KTPGGAPSTS EEVLEELALD YPLPKVILEY RGLAKLKSTY TDKLPLMINP KTGRVHTSYH 

       670        680        690        700        710        720 
QAVTATGRLS STDPNLQNIP VRNEEGRRIR QAFIAPEDYV IVSADYSQIE LRIMAHLSRD 

       730        740        750        760        770        780 
KGLLTAFAEG KDIHRATAAE VFGLPLETVT SEQRRSAKAI NFGLIYGMSA FGLARQLNIP 

       790        800        810        820        830        840 
RKEAQKYMDL YFERYPGVLE YMERTRAQAK EQGYVETLDG RRLYLPDIKS SNGARRAAAE 

       850        860        870        880        890        900 
RAAINAPMQG TAADIIKRAM IAVDAWLQAE QPRVRMIMQV HDELVFEVHK DDVDAVAKQI 

       910        920 
HQLMENCTRL DVPLLVEVGS GENWDQAH 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of the Escherichia coli polA gene and primary structure of DNA polymerase I."
Joyce C.M., Kelley W.S., Grindley N.D.F.
J. Biol. Chem. 257:1958-1964(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[2]"Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes."
Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.
Nucleic Acids Res. 21:3391-3398(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Identification of two genes immediately downstream from the polA gene of Escherichia coli."
Joyce C.M., Grindley N.D.
J. Bacteriol. 152:1211-1219(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 918-928.
Strain: K12.
[6]"Genetic characterization of early amber mutations in the Escherichia coli polA gene and purification of the amber peptides."
Kelley W.S., Joyce C.M.
J. Mol. Biol. 164:529-560(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 284-350.
[7]"Escherichia coli DNA polymerase I. Sequence characterization and secondary structure prediction."
Brown W.E., Stump K.H., Kelley W.S.
J. Biol. Chem. 257:1965-1972(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: AMINO-ACID COMPOSITION, PARTIAL PROTEIN SEQUENCE.
[8]"Escherichia coli proteome analysis using the gene-protein database."
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY 2D-GEL.
[9]"Structure of large fragment of Escherichia coli DNA polymerase I complexed with dTMP."
Ollis D.L., Brick P., Hamlin R., Xuong N.G., Steitz T.A.
Nature 313:762-766(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF KLENOW FRAGMENT.
[10]"Structural basis for the 3'-5' exonuclease activity of Escherichia coli DNA polymerase I: a two metal ion mechanism."
Beese L.S., Steitz T.A.
EMBO J. 10:25-33(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF KLENOW FRAGMENT.
[11]"Structure of DNA polymerase I Klenow fragment bound to duplex DNA."
Beese L.S., Derbyshire V., Steitz T.A.
Science 260:352-355(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF KLENOW FRAGMENT.
[12]"Crystal structures of the Klenow fragment of DNA polymerase I complexed with deoxynucleoside triphosphate and pyrophosphate."
Beese L.S., Friedman J.M., Steitz T.A.
Biochemistry 32:14095-14101(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.9 ANGSTROMS) OF KLENOW FRAGMENT.
[13]"Structural principles for the inhibition of the 3'-5' exonuclease activity of Escherichia coli DNA polymerase I by phosphorothioates."
Brautigam C.A., Steitz T.A.
J. Mol. Biol. 277:363-377(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF KLENOW FRAGMENT.
[14]"Structures of normal single-stranded DNA and deoxyribo-3'-S-phosphorothiolates bound to the 3'-5' exonucleolytic active site of DNA polymerase I from Escherichia coli."
Brautigam C.A., Sun S., Piccirilli J.A., Steitz T.A.
Biochemistry 38:696-704(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF KLENOW FRAGMENT.
[15]"Structural origins of the exonuclease resistance of a zwitterionic RNA."
Teplova M., Wallace S.T., Tereshko V., Minasov G., Symons A.M., Cook P.D., Manoharan M., Egli M.
Proc. Natl. Acad. Sci. U.S.A. 96:14240-14245(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.08 ANGSTROMS) OF KLENOW FRAGMENT.
[16]"Sequential proton NMR resonance assignments, circular dichroism, and structural properties of a 50-residue substrate-binding peptide from DNA polymerase I."
Mullen G.P., Vaughn J.B. Jr., Mildvan A.S.
Arch. Biochem. Biophys. 301:174-183(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 728-777.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
V00317 Genomic DNA. Translation: CAA23607.1.
L19201 Genomic DNA. Translation: AAB02998.1.
U00096 Genomic DNA. Translation: AAC76861.1.
AP009048 Genomic DNA. Translation: BAE77445.1.
J01663 Genomic DNA. Translation: AAA24402.1.
J01664 Genomic DNA. Translation: AAA24404.1.
PIRDJECI. A92360.
RefSeqNP_418300.1. NC_000913.3.
YP_491586.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1D8YX-ray2.08A325-928[»]
1D9DX-ray2.18A325-928[»]
1D9FX-ray3.00A325-928[»]
1DPIX-ray2.80A324-928[»]
1KFDX-ray3.90A324-928[»]
1KFSX-ray2.10A325-928[»]
1KLNX-ray3.20A324-928[»]
1KRPX-ray2.20A325-928[»]
1KSPX-ray2.30A325-928[»]
1QSLX-ray2.20A325-928[»]
2KFNX-ray2.03A325-928[»]
2KFZX-ray2.03A325-928[»]
2KZMX-ray2.60A325-928[»]
2KZZX-ray2.25A325-928[»]
ProteinModelPortalP00582.
SMRP00582. Positions 5-928.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-10524N.
IntActP00582. 28 interactions.
MINTMINT-1225247.
STRING511145.b3863.

Chemistry

BindingDBP00582.
ChEMBLCHEMBL4298.
DrugBankDB00548. Azelaic Acid.

2D gel databases

SWISS-2DPAGEP00582.

Proteomic databases

PaxDbP00582.
PRIDEP00582.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76861; AAC76861; b3863.
BAE77445; BAE77445; BAE77445.
GeneID12933188.
948356.
KEGGecj:Y75_p3322.
eco:b3863.
PATRIC32123225. VBIEscCol129921_3973.

Organism-specific databases

EchoBASEEB0739.
EcoGeneEG10746. polA.

Phylogenomic databases

eggNOGCOG0258.
HOGENOMHOG000020998.
KOK02335.
OMARMALNAP.
OrthoDBEOG6SJJH7.
PhylomeDBP00582.
ProtClustDBPRK05755.

Enzyme and pathway databases

BioCycEcoCyc:EG10746-MONOMER.
ECOL316407:JW3835-MONOMER.
MetaCyc:EG10746-MONOMER.
SABIO-RKP00582.

Gene expression databases

GenevestigatorP00582.

Family and domain databases

Gene3D3.30.420.10. 1 hit.
InterProIPR002562. 3'-5'_exonuclease_dom.
IPR020046. 5-3_exonucl_a-hlix_arch_N.
IPR020045. 5-3_exonuclease_C.
IPR002421. 5-3_exonuclease_N.
IPR019760. DNA-dir_DNA_pol_A_CS.
IPR001098. DNA-dir_DNA_pol_A_palm_dom.
IPR018320. DNA_polymerase_1.
IPR002298. DNA_polymerase_A.
IPR008918. HhH2.
IPR003583. Hlx-hairpin-Hlx_DNA-bd_motif.
IPR012337. RNaseH-like_dom.
[Graphical view]
PfamPF01367. 5_3_exonuc. 1 hit.
PF02739. 5_3_exonuc_N. 1 hit.
PF00476. DNA_pol_A. 1 hit.
PF01612. DNA_pol_A_exo1. 1 hit.
[Graphical view]
PRINTSPR00868. DNAPOLI.
SMARTSM00474. 35EXOc. 1 hit.
SM00475. 53EXOc. 1 hit.
SM00278. HhH1. 1 hit.
SM00279. HhH2. 1 hit.
SM00482. POLAc. 1 hit.
[Graphical view]
SUPFAMSSF47807. SSF47807. 1 hit.
SSF53098. SSF53098. 1 hit.
TIGRFAMsTIGR00593. pola. 1 hit.
PROSITEPS00447. DNA_POLYMERASE_A. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00582.
PROP00582.

Entry information

Entry nameDPO1_ECOLI
AccessionPrimary (citable) accession number: P00582
Secondary accession number(s): Q2M8G1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: April 16, 2014
This is version 159 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene