(data stored in ACNUC7421 zone)

SWISSPROT: DPO4_ECO57

ID   DPO4_ECO57              Reviewed;         351 AA.
AC   Q8X7Q1;
DT   02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   07-JUN-2017, entry version 99.
DE   RecName: Full=DNA polymerase IV {ECO:0000255|HAMAP-Rule:MF_01113};
DE            Short=Pol IV {ECO:0000255|HAMAP-Rule:MF_01113};
DE            EC=2.7.7.7 {ECO:0000255|HAMAP-Rule:MF_01113};
GN   Name=dinB {ECO:0000255|HAMAP-Rule:MF_01113}; Synonyms=dinP;
GN   OrderedLocusNames=Z0292, ECs0258;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Poorly processive, error-prone DNA polymerase involved
CC       in untargeted mutagenesis. Copies undamaged DNA at stalled
CC       replication forks, which arise in vivo from mismatched or
CC       misaligned primer ends. These misaligned primers can be extended
CC       by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity.
CC       May be involved in translesional synthesis, in conjunction with
CC       the beta clamp from PolIII. {ECO:0000255|HAMAP-Rule:MF_01113}.
CC   -!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) =
CC       diphosphate + DNA(n+1). {ECO:0000255|HAMAP-Rule:MF_01113}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01113};
CC       Note=Binds 2 magnesium ions per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01113};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01113}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01113}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-Y family.
CC       {ECO:0000255|HAMAP-Rule:MF_01113}.
DR   EMBL; AE005174; AAG54556.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB33681.1; -; Genomic_DNA.
DR   PIR; B90661; B90661.
DR   PIR; H85511; H85511.
DR   RefSeq; NP_308285.1; NC_002695.1.
DR   RefSeq; WP_001226188.1; NZ_LPWC02000002.1.
DR   ProteinModelPortal; Q8X7Q1; -.
DR   SMR; Q8X7Q1; -.
DR   STRING; 155864.Z0292; -.
DR   EnsemblBacteria; AAG54556; AAG54556; Z0292.
DR   EnsemblBacteria; BAB33681; BAB33681; BAB33681.
DR   GeneID; 914349; -.
DR   KEGG; ece:Z0292; -.
DR   KEGG; ecs:ECs0258; -.
DR   PATRIC; fig|386585.9.peg.360; -.
DR   eggNOG; ENOG4105CQ3; Bacteria.
DR   eggNOG; COG0389; LUCA.
DR   HOGENOM; HOG000082707; -.
DR   KO; K02346; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   CDD; cd03586; PolY_Pol_IV_kappa; 1.
DR   Gene3D; 3.30.1490.100; -; 1.
DR   HAMAP; MF_01113; DNApol_IV; 1.
DR   InterPro; IPR017961; DNA_pol_Y-fam_little_finger.
DR   InterPro; IPR022880; DNApol_IV.
DR   InterPro; IPR024728; PolY_HhH_motif.
DR   InterPro; IPR001126; UmuC.
DR   PANTHER; PTHR11076:SF45; PTHR11076:SF45; 1.
DR   Pfam; PF00817; IMS; 1.
DR   Pfam; PF11799; IMS_C; 1.
DR   Pfam; PF11798; IMS_HHH; 1.
DR   SUPFAM; SSF100879; SSF100879; 1.
DR   PROSITE; PS50173; UMUC; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q8X7Q1.
DR   SWISS-2DPAGE; Q8X7Q1.
KW   Complete proteome; Cytoplasm; DNA damage; DNA repair; DNA replication;
KW   DNA-binding; DNA-directed DNA polymerase; Magnesium; Metal-binding;
KW   Mutator protein; Nucleotidyltransferase; Transferase.
FT   CHAIN         1    351       DNA polymerase IV.
FT                                /FTId=PRO_0000173914.
FT   DOMAIN        4    185       UmuC. {ECO:0000255|HAMAP-Rule:MF_01113}.
FT   ACT_SITE    104    104       {ECO:0000255|HAMAP-Rule:MF_01113}.
FT   METAL         8      8       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01113}.
FT   METAL       103    103       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01113}.
FT   SITE         13     13       Substrate discrimination.
FT                                {ECO:0000255|HAMAP-Rule:MF_01113}.
SQ   SEQUENCE   351 AA;  39491 MW;  50B13B3D49AE947C CRC64;
     MRKIIHVDMD CFFAAVEMRD NPALRDIPIA IGGSRERRGV ISTANYPARK FGVRSAMPTG
     MALKLCPHLT LLPGRFDAYK EASNHIREIF SRYTSRIEPL SLDEAYLDVT DSVHCHGSAT
     LIAQEIRQTI FSELQLTASA GVTPVKFLAK IASDMNKPNG QFVITPAEVS AFLQTLPLAK
     IPGVGKVSAA KLEAMGLRTC GDVQKCDLVI LLKRFGKFGR ILWERSQGID ERDVNSERLR
     KSVGVERTMA EDIHHWSECE AIIERLYPEL ERRLAKVKPD LLIARQGVKL KFDDFQQTTQ
     EHVWPRLNKA DLIATARKTW DERRGGRGVR LVGLHVTLLD PQMERQLVLG L
//

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