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Protein

DNA polymerase IV

Gene

dinB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. Overexpression of polIV results in increased frameshift mutagenesis. It is required for stationary-phase adaptive mutation, which provides the bacterium with flexibility in dealing with environmental stress, enhancing long-term survival and evolutionary fitness. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII.5 Publications

Catalytic activityi

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

Cofactori

Mg2+By similarityNote: Binds 2 magnesium ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi8 – 81MagnesiumBy similarity
Sitei13 – 131Substrate discriminationBy similarity
Metal bindingi103 – 1031MagnesiumBy similarity
Active sitei104 – 1041By similarity

GO - Molecular functioni

  • damaged DNA binding Source: InterPro
  • DNA-directed DNA polymerase activity Source: EcoCyc
  • magnesium ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  • cellular response to DNA damage stimulus Source: EcoliWiki
  • DNA-dependent DNA replication Source: UniProtKB-HAMAP
  • DNA synthesis involved in DNA repair Source: EcoliWiki
  • SOS response Source: EcoCyc
  • translesion synthesis Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

DNA-directed DNA polymerase, Mutator protein, Nucleotidyltransferase, Transferase

Keywords - Biological processi

DNA damage, DNA repair, DNA replication

Keywords - Ligandi

DNA-binding, Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:G6115-MONOMER.
ECOL316407:JW0221-MONOMER.
MetaCyc:G6115-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA polymerase IV (EC:2.7.7.7)
Short name:
Pol IV
Gene namesi
Name:dinB
Synonyms:dinP
Ordered Locus Names:b0231, JW0221
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13141. dinB.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: EcoliWiki
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi8 – 81D → A or H: Loss of function. 1 Publication
Mutagenesisi49 – 491R → A or F: Loss of function. 1 Publication
Mutagenesisi103 – 1031D → A or N: Loss of function. 1 Publication
Mutagenesisi104 – 1041E → A: Loss of function. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 351351DNA polymerase IVPRO_0000173912Add
BLAST

Proteomic databases

PaxDbiQ47155.

Expressioni

Inductioni

By SOS response. A member of the dinB-yafNOP operon (PubMed:12813093). Induced by hydroxyurea (PubMed:20005847).2 Publications

Interactioni

Subunit structurei

Monomer.Curated

Binary interactionsi

WithEntry#Exp.IntActNotes
dnaNP0A9882EBI-1037359,EBI-542385
nusAP0AFF63EBI-1037359,EBI-551571

Protein-protein interaction databases

BioGridi4261678. 35 interactions.
IntActiQ47155. 3 interactions.
STRINGi511145.b0231.

Structurei

Secondary structure

1
351
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 96Combined sources
Helixi12 – 209Combined sources
Helixi22 – 243Combined sources
Beta strandi25 – 273Combined sources
Beta strandi29 – 324Combined sources
Helixi35 – 373Combined sources
Beta strandi40 – 445Combined sources
Helixi46 – 494Combined sources
Turni50 – 523Combined sources
Helixi59 – 657Combined sources
Beta strandi70 – 723Combined sources
Helixi76 – 9116Combined sources
Beta strandi97 – 1015Combined sources
Beta strandi104 – 1085Combined sources
Helixi114 – 1174Combined sources
Helixi119 – 1279Combined sources
Turni128 – 1303Combined sources
Helixi131 – 1344Combined sources
Beta strandi138 – 1458Combined sources
Helixi146 – 15510Combined sources
Beta strandi161 – 1633Combined sources
Helixi166 – 1683Combined sources
Helixi169 – 1757Combined sources
Helixi178 – 1803Combined sources
Helixi186 – 1949Combined sources
Helixi200 – 2045Combined sources
Helixi208 – 2158Combined sources
Helixi217 – 22610Combined sources
Beta strandi243 – 25311Combined sources
Helixi256 – 27722Combined sources
Beta strandi284 – 2929Combined sources
Beta strandi297 – 3037Combined sources
Helixi309 – 32315Combined sources
Beta strandi329 – 3379Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OK7X-ray1.65C336-351[»]
1UNNX-ray1.90C/D243-351[»]
4IR1X-ray2.38A/F2-351[»]
4IR9X-ray2.33A/F2-351[»]
4IRCX-ray2.67A/F2-341[»]
4IRDX-ray2.48A/F2-341[»]
4IRKX-ray2.32A/B2-341[»]
4Q43X-ray2.45A/F2-351[»]
4Q44X-ray2.71A/F2-341[»]
4Q45X-ray2.18A/F2-341[»]
4R8UX-ray2.30A2-340[»]
B2-338[»]
ProteinModelPortaliQ47155.
SMRiQ47155. Positions 2-340.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ47155.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 185182UmuCAdd
BLAST

Domaini

The catalytic core consists of fingers, palm and thumb subdomains, but the fingers and thumb subdomains are much smaller than in high-fidelity polymerases; residues from five sequence motifs of the Y-family cluster around an active site cleft that can accommodate DNA and nucleotide substrates with relaxed geometric constraints, with consequently higher rates of misincorporation and low processivity. It lacks the O helices present in high-fidelity DNA polymerases in the fingers domain (By similarity).By similarity

Sequence similaritiesi

Belongs to the DNA polymerase type-Y family.Curated
Contains 1 umuC domain.Curated

Phylogenomic databases

eggNOGiENOG4105CQ3. Bacteria.
COG0389. LUCA.
InParanoidiQ47155.
KOiK02346.
OMAiHTLPWAT.
OrthoDBiEOG6FZ4D8.
PhylomeDBiQ47155.

Family and domain databases

Gene3Di3.30.1490.100. 1 hit.
HAMAPiMF_01113. DNApol_IV.
InterProiIPR017961. DNA_pol_Y-fam_little_finger.
IPR022880. DNApol_IV.
IPR024728. PolY_HhH_motif.
IPR001126. UmuC.
[Graphical view]
PfamiPF00817. IMS. 1 hit.
PF11799. IMS_C. 1 hit.
PF11798. IMS_HHH. 1 hit.
[Graphical view]
SUPFAMiSSF100879. SSF100879. 1 hit.
PROSITEiPS50173. UMUC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q47155-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRKIIHVDMD CFFAAVEMRD NPALRDIPIA IGGSRERRGV ISTANYPARK
60 70 80 90 100
FGVRSAMPTG MALKLCPHLT LLPGRFDAYK EASNHIREIF SRYTSRIEPL
110 120 130 140 150
SLDEAYLDVT DSVHCHGSAT LIAQEIRQTI FNELQLTASA GVAPVKFLAK
160 170 180 190 200
IASDMNKPNG QFVITPAEVP AFLQTLPLAK IPGVGKVSAA KLEAMGLRTC
210 220 230 240 250
GDVQKCDLVM LLKRFGKFGR ILWERSQGID ERDVNSERLR KSVGVERTMA
260 270 280 290 300
EDIHHWSECE AIIERLYPEL ERRLAKVKPD LLIARQGVKL KFDDFQQTTQ
310 320 330 340 350
EHVWPRLNKA DLIATARKTW DERRGGRGVR LVGLHVTLLD PQMERQLVLG

L
Length:351
Mass (Da):39,516
Last modified:November 1, 1997 - v1
Checksum:i74DF44DCA18D405F
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti36 – 383ERR → ARG in strain: ECOR 45B1.
Natural varianti124 – 1241Q → K in strain: ECOR 35D.
Natural varianti132 – 1321N → S in strain: ECOR 34B1 and ECOR 37UG.
Natural varianti135 – 1351Q → H in strain: ECOR 70B1.
Natural varianti170 – 1701P → S in strain: ECOR 37UG.
Natural varianti171 – 1711A → T in strain: ECOR 45B1, ECOR 46D, ECOR 49D and ECOR 50D.
Natural varianti176 – 1761L → F in strain: ECOR 37UG.
Natural varianti201 – 2011G → S in strain: ECOR 59B2.
Natural varianti210 – 2101M → I in strain: ECOR 37UG, ECOR 45B1, ECOR 51B2, ECOR 52B2, ECOR 58B1 and ECOR 70B1.
Natural varianti210 – 2101M → T in strain: ECOR 35D, ECOR 46D, ECOR 49D, ECOR 50D, ECOR 57B2, ECOR 59B2, ECOR 60B2 and ECOR 62B2.
Natural varianti225 – 2251R → C in strain: ECOR 59B2 and ECOR 60B2.
Natural varianti310 – 3101A → S in strain: ECOR 57B2, ECOR 59B2, ECOR 60B2 and ECOR 62B2.
Natural varianti321 – 3211D → N in strain: ECOR 35D.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D38582 Genomic DNA. Translation: BAA07593.1.
U70214 Genomic DNA. Translation: AAB08651.1.
U00096 Genomic DNA. Translation: AAC73335.1.
AP009048 Genomic DNA. Translation: BAA77901.1.
AF483080 Genomic DNA. Translation: AAL91943.1.
AF483081 Genomic DNA. Translation: AAL91944.1.
AF483082 Genomic DNA. Translation: AAL91945.1.
AF483083 Genomic DNA. Translation: AAL91946.1.
AF483084 Genomic DNA. Translation: AAL91947.1.
AF483085 Genomic DNA. Translation: AAL91948.1.
AF483086 Genomic DNA. Translation: AAL91949.1.
AF483087 Genomic DNA. Translation: AAL91950.1.
AF483088 Genomic DNA. Translation: AAL91951.1.
AF483089 Genomic DNA. Translation: AAL91952.1.
AF483090 Genomic DNA. Translation: AAL91953.1.
AF483091 Genomic DNA. Translation: AAL91954.1.
AF483092 Genomic DNA. Translation: AAL91955.1.
AF483093 Genomic DNA. Translation: AAL91956.1.
AF483094 Genomic DNA. Translation: AAL91957.1.
AF483095 Genomic DNA. Translation: AAL91958.1.
AF483096 Genomic DNA. Translation: AAL91959.1.
AF483097 Genomic DNA. Translation: AAL91960.1.
AF483098 Genomic DNA. Translation: AAL91961.1.
AF483099 Genomic DNA. Translation: AAL91962.1.
AF483100 Genomic DNA. Translation: AAL91963.1.
AF483101 Genomic DNA. Translation: AAL91964.1.
AF483102 Genomic DNA. Translation: AAL91965.1.
AF483103 Genomic DNA. Translation: AAL91966.1.
AF483104 Genomic DNA. Translation: AAL91967.1.
AF483105 Genomic DNA. Translation: AAL91968.1.
PIRiH64747.
RefSeqiNP_414766.1. NC_000913.3.
WP_001226164.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73335; AAC73335; b0231.
BAA77901; BAA77901; BAA77901.
GeneIDi944922.
KEGGiecj:JW0221.
eco:b0231.
PATRICi32115577. VBIEscCol129921_0233.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D38582 Genomic DNA. Translation: BAA07593.1.
U70214 Genomic DNA. Translation: AAB08651.1.
U00096 Genomic DNA. Translation: AAC73335.1.
AP009048 Genomic DNA. Translation: BAA77901.1.
AF483080 Genomic DNA. Translation: AAL91943.1.
AF483081 Genomic DNA. Translation: AAL91944.1.
AF483082 Genomic DNA. Translation: AAL91945.1.
AF483083 Genomic DNA. Translation: AAL91946.1.
AF483084 Genomic DNA. Translation: AAL91947.1.
AF483085 Genomic DNA. Translation: AAL91948.1.
AF483086 Genomic DNA. Translation: AAL91949.1.
AF483087 Genomic DNA. Translation: AAL91950.1.
AF483088 Genomic DNA. Translation: AAL91951.1.
AF483089 Genomic DNA. Translation: AAL91952.1.
AF483090 Genomic DNA. Translation: AAL91953.1.
AF483091 Genomic DNA. Translation: AAL91954.1.
AF483092 Genomic DNA. Translation: AAL91955.1.
AF483093 Genomic DNA. Translation: AAL91956.1.
AF483094 Genomic DNA. Translation: AAL91957.1.
AF483095 Genomic DNA. Translation: AAL91958.1.
AF483096 Genomic DNA. Translation: AAL91959.1.
AF483097 Genomic DNA. Translation: AAL91960.1.
AF483098 Genomic DNA. Translation: AAL91961.1.
AF483099 Genomic DNA. Translation: AAL91962.1.
AF483100 Genomic DNA. Translation: AAL91963.1.
AF483101 Genomic DNA. Translation: AAL91964.1.
AF483102 Genomic DNA. Translation: AAL91965.1.
AF483103 Genomic DNA. Translation: AAL91966.1.
AF483104 Genomic DNA. Translation: AAL91967.1.
AF483105 Genomic DNA. Translation: AAL91968.1.
PIRiH64747.
RefSeqiNP_414766.1. NC_000913.3.
WP_001226164.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OK7X-ray1.65C336-351[»]
1UNNX-ray1.90C/D243-351[»]
4IR1X-ray2.38A/F2-351[»]
4IR9X-ray2.33A/F2-351[»]
4IRCX-ray2.67A/F2-341[»]
4IRDX-ray2.48A/F2-341[»]
4IRKX-ray2.32A/B2-341[»]
4Q43X-ray2.45A/F2-351[»]
4Q44X-ray2.71A/F2-341[»]
4Q45X-ray2.18A/F2-341[»]
4R8UX-ray2.30A2-340[»]
B2-338[»]
ProteinModelPortaliQ47155.
SMRiQ47155. Positions 2-340.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261678. 35 interactions.
IntActiQ47155. 3 interactions.
STRINGi511145.b0231.

Proteomic databases

PaxDbiQ47155.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73335; AAC73335; b0231.
BAA77901; BAA77901; BAA77901.
GeneIDi944922.
KEGGiecj:JW0221.
eco:b0231.
PATRICi32115577. VBIEscCol129921_0233.

Organism-specific databases

EchoBASEiEB2935.
EcoGeneiEG13141. dinB.

Phylogenomic databases

eggNOGiENOG4105CQ3. Bacteria.
COG0389. LUCA.
InParanoidiQ47155.
KOiK02346.
OMAiHTLPWAT.
OrthoDBiEOG6FZ4D8.
PhylomeDBiQ47155.

Enzyme and pathway databases

BioCyciEcoCyc:G6115-MONOMER.
ECOL316407:JW0221-MONOMER.
MetaCyc:G6115-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ47155.
PROiQ47155.

Family and domain databases

Gene3Di3.30.1490.100. 1 hit.
HAMAPiMF_01113. DNApol_IV.
InterProiIPR017961. DNA_pol_Y-fam_little_finger.
IPR022880. DNApol_IV.
IPR024728. PolY_HhH_motif.
IPR001126. UmuC.
[Graphical view]
PfamiPF00817. IMS. 1 hit.
PF11799. IMS_C. 1 hit.
PF11798. IMS_HHH. 1 hit.
[Graphical view]
SUPFAMiSSF100879. SSF100879. 1 hit.
PROSITEiPS50173. UMUC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "dinP, a new gene in Escherichia coli, whose product shows similarities to UmuC and its homologues."
    Ohmori H., Hatada E., Qiao Y., Tsuji M., Fukuda R.
    Mutat. Res. 347:1-7(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  2. "Systematic sequencing of the Escherichia coli genome: analysis of the 4.0 - 6.0 min (189,987 - 281,416bp) region."
    Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T., Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S., Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K.
    Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. "Sequence of minutes 4-25 of Escherichia coli."
    Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
    Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "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.
  6. "Phylogeny of SOS inducible DNA polymerases of Escherichia coli."
    Bjedov I., Matic I., Denamur E.
    Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 7-342.
    Strain: ECOR 10A, ECOR 13A, ECOR 17A, ECOR 1A, ECOR 20A, ECOR 23A, ECOR 24A, ECOR 26B1, ECOR 27B1, ECOR 34B1, ECOR 35D, ECOR 37UG, ECOR 45B1, ECOR 46D, ECOR 49D, ECOR 4A, ECOR 50D, ECOR 51B2, ECOR 52B2, ECOR 57B2, ECOR 58B1, ECOR 59B2, ECOR 60B2, ECOR 62B2, ECOR 68B1 and ECOR 70B1.
  7. "DNA-damaging agents stimulate gene expression at specific loci in Escherichia coli."
    Kenyon C.J., Walker G.C.
    Proc. Natl. Acad. Sci. U.S.A. 77:2819-2823(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  8. "Multiple pathways for SOS-induced mutagenesis in Escherichia coli: an overexpression of dinB/dinP results in strongly enhancing mutagenesis in the absence of any exogenous treatment to damage DNA."
    Kim S.-R., Maenhaut-Michel G., Yamada M., Yamamoto Y., Matsui K., Sofuni T., Nohmi T., Ohmori H.
    Proc. Natl. Acad. Sci. U.S.A. 94:13792-13797(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Strain: K12.
  9. "The dinB gene encodes a novel E. coli DNA polymerase, DNA pol IV, involved in mutagenesis."
    Wagner J., Gruz P., Kim S.-R., Yamada M., Matsui K., Fuchs R.P.P., Nohmi T.
    Mol. Cell 4:281-286(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, MUTAGENESIS OF ASP-8; ARG-49; ASP-103 AND GLU-104.
    Strain: K12.
  10. "All three SOS-inducible DNA polymerases (Pol II, Pol IV and Pol V) are involved in induced mutagenesis."
    Napolitano R., Janel-Bintz R., Wagner J., Fuchs R.P.P.
    EMBO J. 19:6259-6265(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Strain: K12 / MG1655 / ATCC 47076.
  11. "SOS mutator DNA polymerase IV functions in adaptive mutation and not adaptive amplification."
    McKenzie G.J., Lee P.L., Lombardo M.-J., Hastings P.J., Rosenberg S.M.
    Mol. Cell 7:571-579(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "The processivity factor beta controls DNA polymerase IV traffic during spontaneous mutagenesis and translesion synthesis in vivo."
    Lenne-Samuel N., Wagner J., Etienne H., Fuchs R.P.P.
    EMBO Rep. 3:45-49(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "SOS-induced DNA polymerases enhance long-term survival and evolutionary fitness."
    Yeiser B., Pepper E.D., Goodman M.F., Finkel S.E.
    Proc. Natl. Acad. Sci. U.S.A. 99:8737-8741(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  14. "The dinB operon and spontaneous mutation in Escherichia coli."
    McKenzie G.J., Magner D.B., Lee P.L., Rosenberg S.M.
    J. Bacteriol. 185:3972-3977(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION, OPERON STRUCTURE.
    Strain: K12 / MG1655 / ATCC 47076.
  15. "Error-prone DNA polymerases: novel structures and the benefits of infidelity."
    Friedberg E.C., Fischhaber P.L., Kisker C.
    Cell 107:9-12(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  16. "Adaptive mutations, mutator DNA polymerases and genetic change strategies of pathogens."
    McKenzie G.J., Rosenberg S.M.
    Curr. Opin. Microbiol. 4:586-594(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  17. "Hydroxyurea induces hydroxyl radical-mediated cell death in Escherichia coli."
    Davies B.W., Kohanski M.A., Simmons L.A., Winkler J.A., Collins J.J., Walker G.C.
    Mol. Cell 36:845-860(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY HYDROXYUREA.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
  18. "Error-prone repair DNA polymerases in prokaryotes and eukaryotes."
    Goodman M.F.
    Annu. Rev. Biochem. 71:17-50(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  19. "Structural basis for recruitment of translesion DNA polymerase Pol IV/DinB to the beta-clamp."
    Bunting K.A., Roe S.M., Pearl L.H.
    EMBO J. 22:5883-5892(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 243-351 IN COMPLEX WITH DNAN.

Entry informationi

Entry nameiDPO4_ECOLI
AccessioniPrimary (citable) accession number: Q47155
Secondary accession number(s): Q47683
, Q8RJ78, Q8RJ81, Q8RJ86, Q8RJ87, Q8RNI5, Q8RNI6, Q8RNI7, Q8RNI8, Q8RNI9, Q8RNJ0, Q8RNJ1, Q8RNJ2, Q8RNJ3, Q8RNJ4, Q8RNJ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: April 13, 2016
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.