DPS_ECODH
ID DPS_ECODH Reviewed; 167 AA.
AC B1X7E2;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=DNA protection during starvation protein {ECO:0000255|HAMAP-Rule:MF_01441};
DE EC=1.16.-.- {ECO:0000255|HAMAP-Rule:MF_01441};
GN Name=dps {ECO:0000255|HAMAP-Rule:MF_01441}; OrderedLocusNames=ECDH10B_0880;
OS Escherichia coli (strain K12 / DH10B).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=316385;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / DH10B;
RX PubMed=18245285; DOI=10.1128/jb.01695-07;
RA Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B.,
RA Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B.,
RA Posfai G., Weinstock G.M., Blattner F.R.;
RT "The complete genome sequence of Escherichia coli DH10B: insights into the
RT biology of a laboratory workhorse.";
RL J. Bacteriol. 190:2597-2606(2008).
CC -!- FUNCTION: During stationary phase, binds the chromosome non-
CC specifically, forming a highly ordered and stable dps-DNA co-crystal
CC within which chromosomal DNA is condensed and protected from diverse
CC damages. It protects DNA from oxidative damage by sequestering
CC intracellular Fe(2+) ion and storing it in the form of Fe(3+)
CC oxyhydroxide mineral, which can be released after reduction. One
CC hydrogen peroxide oxidizes two Fe(2+) ions, which prevents hydroxyl
CC radical production by the Fenton reaction. Dps also protects the cell
CC from UV and gamma irradiation, iron and copper toxicity, thermal stress
CC and acid and base shocks. Also shows a weak catalase activity.
CC {ECO:0000255|HAMAP-Rule:MF_01441}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(2+) + 2 H(+) + H2O2 = 2 Fe(3+) + 2 H2O;
CC Xref=Rhea:RHEA:48712, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01441};
CC -!- SUBUNIT: Homododecamer. The 12 subunits form a hollow sphere into which
CC the mineral iron core of up to 500 Fe(3+) can be deposited.
CC {ECO:0000255|HAMAP-Rule:MF_01441}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, nucleoid {ECO:0000255|HAMAP-
CC Rule:MF_01441}.
CC -!- SIMILARITY: Belongs to the Dps family. {ECO:0000255|HAMAP-
CC Rule:MF_01441}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000948; ACB02013.1; -; Genomic_DNA.
DR RefSeq; WP_000100800.1; NC_010473.1.
DR AlphaFoldDB; B1X7E2; -.
DR SMR; B1X7E2; -.
DR GeneID; 67413850; -.
DR KEGG; ecd:ECDH10B_0880; -.
DR HOGENOM; CLU_098183_1_2_6; -.
DR OMA; DDYSIGR; -.
DR BioCyc; ECOL316385:ECDH10B_RS04525-MON; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
DR GO; GO:0009295; C:nucleoid; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008199; F:ferric iron binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016722; F:oxidoreductase activity, acting on metal ions; IEA:InterPro.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IEA:UniProtKB-KW.
DR GO; GO:0030261; P:chromosome condensation; IEA:UniProtKB-KW.
DR CDD; cd01043; DPS; 1.
DR Gene3D; 1.20.1260.10; -; 1.
DR HAMAP; MF_01441; Dps; 1.
DR InterPro; IPR002177; DPS_DNA-bd.
DR InterPro; IPR023188; DPS_DNA-bd_CS.
DR InterPro; IPR023067; Dps_gammaproteobac.
DR InterPro; IPR012347; Ferritin-like.
DR InterPro; IPR009078; Ferritin-like_SF.
DR InterPro; IPR008331; Ferritin_DPS_dom.
DR PANTHER; PTHR42932; PTHR42932; 1.
DR Pfam; PF00210; Ferritin; 1.
DR PIRSF; PIRSF005900; Dps; 1.
DR PRINTS; PR01346; HELNAPAPROT.
DR SUPFAM; SSF47240; SSF47240; 1.
DR PROSITE; PS00818; DPS_1; 1.
DR PROSITE; PS00819; DPS_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; DNA condensation; DNA-binding; Iron; Iron storage;
KW Metal-binding; Oxidoreductase.
FT CHAIN 1..167
FT /note="DNA protection during starvation protein"
FT /id="PRO_1000145902"
FT BINDING 51
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01441"
FT BINDING 78
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01441"
FT BINDING 82
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01441"
FT BINDING 82
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01441"
SQ SEQUENCE 167 AA; 18695 MW; 596A79B1C6A5E60B CRC64;
MSTAKLVKSK ATNLLYTRND VSDSEKKATV ELLNRQVIQF IDLSLITKQA HWNMRGANFI
AVHEMLDGFR TALIDHLDTM AERAVQLGGV ALGTTQVINS KTPLKSYPLD IHNVQDHLKE
LADRYAIVAN DVRKAIGEAK DDDTADILTA ASRDLDKFLW FIESNIE
