(data stored in ACNUC10821 zone)

SWISSPROT: C8U1W4_ECO10

ID   C8U1W4_ECO10            Unreviewed;       351 AA.
AC   C8U1W4;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 67.
DE   RecName: Full=DNA polymerase IV {ECO:0000256|HAMAP-Rule:MF_01113};
DE            Short=Pol IV {ECO:0000256|HAMAP-Rule:MF_01113};
DE            EC=2.7.7.7 {ECO:0000256|HAMAP-Rule:MF_01113};
GN   Name=dinB {ECO:0000256|HAMAP-Rule:MF_01113,
GN   ECO:0000313|EMBL:BAI29122.1};
GN   OrderedLocusNames=ECO103_0248 {ECO:0000313|EMBL:BAI29122.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29122.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29122.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
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:0000256|HAMAP-Rule:MF_01113}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC         diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-
CC         COMP:11130, Rhea:RHEA-COMP:11131, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:61560, ChEBI:CHEBI:83828; EC=2.7.7.7;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01113,
CC         ECO:0000256|SAAS:SAAS01115616};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01113};
CC       Note=Binds 2 magnesium ions per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01113};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01113,
CC       ECO:0000256|SAAS:SAAS00737835}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01113,
CC       ECO:0000256|SAAS:SAAS00737775}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-Y family.
CC       {ECO:0000256|HAMAP-Rule:MF_01113, ECO:0000256|SAAS:SAAS00538466}.
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DR   EMBL; AP010958; BAI29122.1; -; Genomic_DNA.
DR   RefSeq; WP_001226183.1; NC_013353.1.
DR   SMR; C8U1W4; -.
DR   EnsemblBacteria; BAI29122; BAI29122; ECO103_0248.
DR   KEGG; eoh:ECO103_0248; -.
DR   HOGENOM; HOG000082707; -.
DR   KO; K02346; -.
DR   OMA; DMQSFYA; -.
DR   BioCyc; ECOL585395:ECO103_RS01305-MONOMER; -.
DR   Proteomes; UP000000959; 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-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR   GO; GO:0006261; P:DNA-dependent DNA replication; IEA:UniProtKB-UniRule.
DR   CDD; cd03586; PolY_Pol_IV_kappa; 1.
DR   Gene3D; 3.30.1490.100; -; 1.
DR   HAMAP; MF_01113; DNApol_IV; 1.
DR   InterPro; IPR036775; DNA_pol_Y-fam_lit_finger_sf.
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   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; C8U1W4.
DR   SWISS-2DPAGE; C8U1W4.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01113,
KW   ECO:0000256|SAAS:SAAS00737824};
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_01113,
KW   ECO:0000256|SAAS:SAAS00737805};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_01113,
KW   ECO:0000256|SAAS:SAAS00737784};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_01113,
KW   ECO:0000256|SAAS:SAAS00737790};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_01113,
KW   ECO:0000256|SAAS:SAAS00737844};
KW   DNA-directed DNA polymerase {ECO:0000256|HAMAP-Rule:MF_01113,
KW   ECO:0000256|SAAS:SAAS00737803};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01113,
KW   ECO:0000256|SAAS:SAAS00737808};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01113,
KW   ECO:0000256|SAAS:SAAS00737787};
KW   Mutator protein {ECO:0000256|HAMAP-Rule:MF_01113};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_01113,
KW   ECO:0000256|SAAS:SAAS00737766};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01113,
KW   ECO:0000256|SAAS:SAAS00737757}.
FT   DOMAIN        4    185       UmuC. {ECO:0000259|PROSITE:PS50173}.
FT   ACT_SITE    104    104       {ECO:0000256|HAMAP-Rule:MF_01113}.
FT   METAL         8      8       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01113}.
FT   METAL       103    103       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01113}.
FT   SITE         13     13       Substrate discrimination.
FT                                {ECO:0000256|HAMAP-Rule:MF_01113}.
SQ   SEQUENCE   351 AA;  39489 MW;  D1AE13CE8C63527E CRC64;
     MRKIIHVDMD CFFAAVEMRD NPALRDIPIA IGGSRERRGV ISTANYPARK FGVRSAMPTG
     MALKLCPHLT LLPGRFDAYK EASNHIREIF SRYTSRIEPL SLDEAYLDVT DSVHCHGSAT
     LIAQEIRQTI FSELQLTASA GVAPVKFLAK IASDMNKPNG QFVITPAEVP AFLQTLPLAK
     IPGVGKVSAA KLEAMGLRTC GDVQKCDLVM LLKRFGKFGR ILWERSQGID ERDVNSERLR
     KSVGVERTMA EDIHHWSECE AIIERLYPEL ERRLAKVKPD LLIARQGVKL KFDDFQQTTQ
     EHVWPRLNKA DLIATARKTW DERRGGRGVR LVGLHVTLLD PQMERQLVLG L
//

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