(data stored in SCRATCH zone)

SWISSPROT: B7UJC1_ECO27

ID   B7UJC1_ECO27            Unreviewed;       351 AA.
AC   B7UJC1;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   16-JAN-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:CAS07774.1};
GN   OrderedLocusNames=E2348C_0226 {ECO:0000313|EMBL:CAS07774.1};
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521 {ECO:0000313|EMBL:CAS07774.1, ECO:0000313|Proteomes:UP000008205};
RN   [1] {ECO:0000313|EMBL:CAS07774.1, ECO:0000313|Proteomes:UP000008205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC {ECO:0000313|Proteomes:UP000008205};
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(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; FM180568; CAS07774.1; -; Genomic_DNA.
DR   RefSeq; WP_001226189.1; NC_011601.1.
DR   EnsemblBacteria; CAS07774; CAS07774; E2348C_0226.
DR   KEGG; ecg:E2348C_0226; -.
DR   HOGENOM; HOG000082707; -.
DR   KO; K02346; -.
DR   OMA; DMQSFYA; -.
DR   BioCyc; ECOL574521:E2348C_RS01200-MONOMER; -.
DR   Proteomes; UP000008205; 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; B7UJC1.
DR   SWISS-2DPAGE; B7UJC1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000008205};
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;  39472 MW;  F72CA3541B6CBB77 CRC64;
     MRKIIHVDMD CFFAAVEMRD NPALRDIPIA IGGSRERRGV ISTANYPARK FGVRSAMPTG
     MALKLCPHLT LLPGRFDAYK EASNHIREIF SRYTSRIEPL SLDEAYLEVT DSVHCHGSAT
     LIAQEIRQTI FNELQLTASA GVAPVKFLAK IASDMNKPNG QFVITPAEVP AFLQTLPLAK
     IPGVGKVSAA KLEAMGLRTC GDVQKCDLVT LLKRFGKFGR ILWERSQGID ERDVNSERLR
     KSVGVERTMA EDIHHWSECE AIIERLYPEL ERRLAKVKPD LLIARQGVKL KFDDFQQTTQ
     EHVWPRLNKS ALIATARKTW DERRGGRGVR LVGLHVTLLD PQMERQLVLG L
//

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