ID   DPS_STRSE               Reviewed;         172 AA.
AC   C5VZF1; Q4A3W3; Q4A3W4; Q4A3W5; Q4A3W6; Q4A3W7; Q4A3W8; Q4A3W9; Q4A3X0;
AC   Q9F5J9;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=DNA protection during starvation protein;
DE            EC=1.16.-.-;
GN   Name=dps; Synonyms=dpr; OrderedLocusNames=SSU1500;
OS   Streptococcus suis (strain P1/7).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=218494;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=16091046; DOI=10.1111/j.1365-2958.2005.04756.x;
RA   Pulliainen A.T., Kauko A., Haataja S., Papageorgiou A.C., Finne J.;
RT   "Dps/Dpr ferritin-like protein: insights into the mechanism of iron
RT   incorporation and evidence for a central role in cellular iron
RT   homeostasisin Streptococcus suis.";
RL   Mol. Microbiol. 57:1086-1100(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P1/7;
RX   PubMed=19603075; DOI=10.1371/journal.pone.0006072;
RA   Holden M.T.G., Hauser H., Sanders M., Ngo T.H., Cherevach I., Cronin A.,
RA   Goodhead I., Mungall K., Quail M.A., Price C., Rabbinowitsch E., Sharp S.,
RA   Croucher N.J., Chieu T.B., Mai N.T.H., Diep T.S., Chinh N.T., Kehoe M.,
RA   Leigh J.A., Ward P.N., Dowson C.G., Whatmore A.M., Chanter N., Iversen P.,
RA   Gottschalk M., Slater J.D., Smith H.E., Spratt B.G., Xu J., Ye C.,
RA   Bentley S., Barrell B.G., Schultsz C., Maskell D.J., Parkhill J.;
RT   "Rapid evolution of virulence and drug resistance in the emerging zoonotic
RT   pathogen Streptococcus suis.";
RL   PLoS ONE 4:E6072-E6072(2009).
CC   -!- FUNCTION: Protects DNA from oxidative damage by sequestering
CC       intracellular Fe(2+) ion and storing it in the form of Fe(3+)
CC       oxyhydroxide mineral. One hydrogen peroxide oxidizes two Fe(2+) ions,
CC       which prevents hydroxyl radical production by the Fenton reaction (By
CC       similarity). It binds and incorporates Fe(2+) iron. Is responsible for
CC       hydrogen peroxide resistance. Does not bind DNA (By similarity).
CC       {ECO:0000250}.
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   -!- SUBUNIT: Homododecamer. The 12 subunits form a hollow sphere into which
CC       the mineral iron core can probably be deposited. Can store up to 480
CC       Fe(3+) (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- DOMAIN: 12 di-nuclear ferroxidase centers are located at the interfaces
CC       between subunits related by 2-fold symmetry axes. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the Dps family. {ECO:0000305}.
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DR   EMBL; AJ833012; CAH55673.1; -; Genomic_DNA.
DR   EMBL; AM946016; CAR47134.1; -; Genomic_DNA.
DR   RefSeq; WP_012027605.1; NC_012925.1.
DR   AlphaFoldDB; C5VZF1; -.
DR   SMR; C5VZF1; -.
DR   GeneID; 8153788; -.
DR   KEGG; ssi:SSU1500; -.
DR   HOGENOM; CLU_098183_4_0_9; -.
DR   OMA; LYLQTHN; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006879; P:cellular iron ion homeostasis; IEA:UniProtKB-KW.
DR   CDD; cd01043; DPS; 1.
DR   Gene3D; 1.20.1260.10; -; 1.
DR   InterPro; IPR002177; DPS_DNA-bd.
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.
PE   3: Inferred from homology;
KW   Cytoplasm; Iron; Iron storage; Metal-binding; Oxidoreductase.
FT   CHAIN           1..172
FT                   /note="DNA protection during starvation protein"
FT                   /id="PRO_0000387985"
FT   BINDING         47
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /ligand_note="ligand shared between two dodecameric
FT                   partners"
FT                   /evidence="ECO:0000250"
FT   BINDING         74
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /ligand_note="ligand shared between two dodecameric
FT                   partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250"
FT   BINDING         78
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /ligand_note="ligand shared between two dodecameric
FT                   partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250"
FT   BINDING         78
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   172 AA;  19595 MW;  2792777D349E60DB CRC64;
     MMKQKYYQSP AEIASFSPRP SLADSKAVLN QAVADLSVAH SILHQVHWYM RGRGFMIWHP
     KMDEYMEEID GYLDEMSERL ITLGGAPFST LKEFSENSQL KEVLGDYNVT IEEQLARVVE
     VFRYLAALFQ KGFDVSDEEG DSVTNDIFNV AKASIEKHIW MLQAELGQAP KL