DPS_SALG2
ID DPS_SALG2 Reviewed; 167 AA.
AC B5R797;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 73.
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=SG0810;
OS Salmonella gallinarum (strain 287/91 / NCTC 13346).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=550538;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=287/91 / NCTC 13346;
RX PubMed=18583645; DOI=10.1101/gr.077404.108;
RA Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S.,
RA Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A.,
RA Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B.,
RA Ormond D., Abdellah Z., Brooks K., Cherevach I., Chillingworth T.,
RA Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K., Moule S.,
RA Mungall K., Saunders M., Whitehead S., Chabalgoity J.A., Maskell D.,
RA Humphreys T., Roberts M., Barrow P.A., Dougan G., Parkhill J.;
RT "Comparative genome analysis of Salmonella enteritidis PT4 and Salmonella
RT gallinarum 287/91 provides insights into evolutionary and host adaptation
RT pathways.";
RL Genome Res. 18:1624-1637(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. {ECO:0000255|HAMAP-
CC 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 {ECO:0000255|HAMAP-Rule:MF_01441}.
CC -!- SIMILARITY: Belongs to the Dps family. {ECO:0000255|HAMAP-
CC Rule:MF_01441}.
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DR EMBL; AM933173; CAR36704.1; -; Genomic_DNA.
DR RefSeq; WP_000100805.1; NC_011274.1.
DR AlphaFoldDB; B5R797; -.
DR SMR; B5R797; -.
DR EnsemblBacteria; CAR36704; CAR36704; SG0810.
DR KEGG; seg:SG0810; -.
DR HOGENOM; CLU_098183_1_2_6; -.
DR OMA; DDYSIGR; -.
DR Proteomes; UP000008321; Chromosome.
DR GO; GO:0005737; C:cytoplasm; 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_1000145912"
FT BINDING 51
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01441"
FT BINDING 78
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01441"
FT BINDING 82
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01441"
SQ SEQUENCE 167 AA; 18717 MW; C5732F4D1F667C14 CRC64;
MSTAKLVKTK ASNLLYTRND VSESDKKATV ELLNRQVIQF IDLSLITKQA HWNMRGANFI
AVHEMLDGFR TALTDHLDTM AERAVQLGGV ALGTTQVINS KTPLKSYPLD IHNVQDHLKE
LADRYAVVAN DVRKAIGEAK DEDTADIFTA ASRDLDKFLW FIESNIE
