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DPS_YERPE
ID   DPS_YERPE               Reviewed;         167 AA.
AC   Q7CJ65; Q74T65;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 107.
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};
GN   OrderedLocusNames=YPO2510, y1677, YP_2325;
OS   Yersinia pestis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=632;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CO-92 / Biovar Orientalis;
RX   PubMed=11586360; DOI=10.1038/35097083;
RA   Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA   Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA   Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA   Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA   Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA   Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA   Stevens K., Whitehead S., Barrell B.G.;
RT   "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL   Nature 413:523-527(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KIM10+ / Biovar Mediaevalis;
RX   PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA   Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA   Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA   Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA   Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT   "Genome sequence of Yersinia pestis KIM.";
RL   J. Bacteriol. 184:4601-4611(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=91001 / Biovar Mediaevalis;
RX   PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA   Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA   Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA   Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA   Wang J., Huang P., Yang R.;
RT   "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT   avirulent to humans.";
RL   DNA Res. 11:179-197(2004).
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; AL590842; CAL21138.1; -; Genomic_DNA.
DR   EMBL; AE009952; AAM85246.1; -; Genomic_DNA.
DR   EMBL; AE017042; AAS62531.1; -; Genomic_DNA.
DR   PIR; AG0306; AG0306.
DR   RefSeq; WP_002210233.1; NZ_WUCM01000061.1.
DR   RefSeq; YP_002347474.1; NC_003143.1.
DR   PDB; 4DYU; X-ray; 2.75 A; A/B/C/D/E/F/G/H/I/J/K/L=1-167.
DR   PDBsum; 4DYU; -.
DR   AlphaFoldDB; Q7CJ65; -.
DR   SMR; Q7CJ65; -.
DR   STRING; 214092.YPO2510; -.
DR   PaxDb; Q7CJ65; -.
DR   DNASU; 1146624; -.
DR   EnsemblBacteria; AAM85246; AAM85246; y1677.
DR   EnsemblBacteria; AAS62531; AAS62531; YP_2325.
DR   GeneID; 66845030; -.
DR   KEGG; ype:YPO2510; -.
DR   KEGG; ypk:y1677; -.
DR   KEGG; ypm:YP_2325; -.
DR   PATRIC; fig|214092.21.peg.2927; -.
DR   eggNOG; COG0783; Bacteria.
DR   HOGENOM; CLU_098183_1_2_6; -.
DR   OMA; DDYSIGR; -.
DR   Proteomes; UP000000815; Chromosome.
DR   Proteomes; UP000001019; Chromosome.
DR   Proteomes; UP000002490; 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.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; DNA condensation; DNA-binding; Iron; Iron storage;
KW   Metal-binding; Oxidoreductase; Reference proteome.
FT   CHAIN           1..167
FT                   /note="DNA protection during starvation protein"
FT                   /id="PRO_0000271599"
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"
FT   HELIX           23..52
FT                   /evidence="ECO:0007829|PDB:4DYU"
FT   HELIX           59..86
FT                   /evidence="ECO:0007829|PDB:4DYU"
FT   HELIX           95..101
FT                   /evidence="ECO:0007829|PDB:4DYU"
FT   HELIX           114..138
FT                   /evidence="ECO:0007829|PDB:4DYU"
FT   HELIX           142..164
FT                   /evidence="ECO:0007829|PDB:4DYU"
SQ   SEQUENCE   167 AA;  18871 MW;  66FCAE078C993A45 CRC64;
     MSTAKLVKTK PSELLYTRND VEEHVKVATI KRLNQMVIQF IDLSLITKQA HWNMRGANFV
     AVHEMLDGFR TALTDHLDTF AERAVQLGGV ALGTAQVIND KTPLKSYPTN IHSVQEHLKA
     LAERYAIVAN DIRKAITEVE DENSADMFTA ASRDLDKFLW FIESNIE
 
 
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