DPS_STRSU
ID DPS_STRSU Reviewed; 172 AA.
AC P0CB53; Q4A3W3; Q4A3W4; Q4A3W5; Q4A3W6; Q4A3W7; Q4A3W8; Q4A3W9; Q4A3X0;
AC Q9F5J9;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=DNA protection during starvation protein;
DE EC=1.16.-.-;
GN Name=dps; Synonyms=dpr;
OS Streptococcus suis.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1307;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 43765;
RX PubMed=11400731; DOI=10.1139/w01-027;
RA Niven D.F., Ekins A.;
RT "Iron content of Streptococcus suis and evidence for a dpr homologue.";
RL Can. J. Microbiol. 47:412-416(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF ASP-74 AND GLU-78.
RC STRAIN=628, and D282;
RX PubMed=12501248; DOI=10.1074/jbc.m210174200;
RA Pulliainen A.T., Haataja S., Kaehkoenen S., Finne J.;
RT "Molecular basis of H2O2 resistance mediated by Streptococcal Dpr.
RT Demonstration of the functional involvement of the putative ferroxidase
RT center by site-directed mutagenesis in Streptococcus suis.";
RL J. Biol. Chem. 278:7996-8005(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF HIS-47; HIS-59;
RP ASP-63; ASP-74; GLU-78; ASP-137 AND ASP-146.
RC STRAIN=12/P32, 6407, 825, 836, 849, 854, BA 70/12, D282, KU5, P805, R75/L1,
RC and TEW/2;
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 [4]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 8-172, AND SUBUNIT.
RX PubMed=15081812; DOI=10.1016/j.jmb.2004.03.009;
RA Kauko A., Haataja S., Pulliainen A.T., Finne J., Papageorgiou A.C.;
RT "Crystal structure of Streptococcus suis Dps-like peroxide resistance
RT protein Dpr: implications for iron incorporation.";
RL J. Mol. Biol. 338:547-558(2004).
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. {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.
CC -!- SIMILARITY: Belongs to the Dps family. {ECO:0000305}.
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DR EMBL; AF319974; AAG33871.1; -; Genomic_DNA.
DR EMBL; AY154459; AAN47189.1; -; Genomic_DNA.
DR EMBL; AJ833004; CAH55665.1; -; Genomic_DNA.
DR EMBL; AJ833005; CAH55666.1; -; Genomic_DNA.
DR EMBL; AJ833006; CAH55667.1; -; Genomic_DNA.
DR EMBL; AJ833007; CAH55668.1; -; Genomic_DNA.
DR EMBL; AJ833008; CAH55669.1; -; Genomic_DNA.
DR EMBL; AJ833009; CAH55670.1; -; Genomic_DNA.
DR EMBL; AJ833010; CAH55671.1; -; Genomic_DNA.
DR EMBL; AJ833011; CAH55672.1; -; Genomic_DNA.
DR EMBL; AJ833013; CAH55674.1; -; Genomic_DNA.
DR EMBL; AJ833014; CAH55675.1; -; Genomic_DNA.
DR EMBL; AJ833015; CAH55676.1; -; Genomic_DNA.
DR EMBL; AJ833016; CAH55677.1; -; Genomic_DNA.
DR RefSeq; WP_004194743.1; NZ_VKJM01000007.1.
DR RefSeq; WP_012027605.1; NZ_WODB01000005.1.
DR RefSeq; WP_014736235.1; NZ_RSDQ01000007.1.
DR PDB; 1UMN; X-ray; 1.95 A; A/B/C/D/E/F/G/H/I/J/K/L=8-172.
DR PDB; 2BW1; X-ray; 1.81 A; A/B/C/D/E/F/G/H/I/J/K/L=9-172.
DR PDB; 2CF7; X-ray; 1.50 A; A/B/C/D/E/F/G/H/I/J/K/L=9-172.
DR PDB; 2UX1; X-ray; 1.80 A; A/B/C/D/E/F/G/H/I/J/K/L=9-172.
DR PDB; 2V15; X-ray; 2.10 A; A/B/C/D/E/F/G/H/I/J/K/L=8-172.
DR PDB; 2XJM; X-ray; 2.30 A; A/B/C/D/E/F/G/H/I/J/K/L=8-172.
DR PDB; 2XJN; X-ray; 2.10 A; A/B/C/D/E/F/G/H/I/J/K/L=8-172.
DR PDB; 2XJO; X-ray; 2.10 A; A/B/C/D/E/F/G/H/I/J/K/L=8-172.
DR PDB; 2XKQ; X-ray; 2.40 A; A/B/C/D/E/F/G/H/I/J/K/L=8-172.
DR PDBsum; 1UMN; -.
DR PDBsum; 2BW1; -.
DR PDBsum; 2CF7; -.
DR PDBsum; 2UX1; -.
DR PDBsum; 2V15; -.
DR PDBsum; 2XJM; -.
DR PDBsum; 2XJN; -.
DR PDBsum; 2XJO; -.
DR PDBsum; 2XKQ; -.
DR AlphaFoldDB; P0CB53; -.
DR SMR; P0CB53; -.
DR STRING; 996306.SSUR61_1952; -.
DR GeneID; 8153788; -.
DR PATRIC; fig|1307.476.peg.1583; -.
DR eggNOG; COG0783; Bacteria.
DR OMA; LYLQTHN; -.
DR OrthoDB; 1742631at2; -.
DR EvolutionaryTrace; P0CB53; -.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Iron; Iron storage; Metal-binding; Oxidoreductase.
FT CHAIN 1..172
FT /note="DNA protection during starvation protein"
FT /id="PRO_0000253337"
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"
FT VARIANT 27
FT /note="A -> S (in strain: 825)"
FT VARIANT 42
FT /note="I -> L (in strain: 849)"
FT VARIANT 91
FT /note="L -> F (in strain: 854)"
FT VARIANT 103
FT /note="V -> A (in strain: KU5)"
FT VARIANT 104
FT /note="L -> P (in strain: 6407, 825, 849, BA 70/12 and
FT KU5)"
FT VARIANT 110
FT /note="T -> M (in strain: 6407 and 825)"
FT VARIANT 116
FT /note="A -> V (in strain: 849 and BA 70/12)"
FT VARIANT 154
FT /note="S -> N (in strain: 836)"
FT VARIANT 171
FT /note="K -> G (in strain: KU5)"
FT MUTAGEN 47
FT /note="H->A: Decreases the iron incorporation
FT considerably."
FT /evidence="ECO:0000269|PubMed:16091046"
FT MUTAGEN 59
FT /note="H->A: Decreases the iron incorporation considerably
FT and induces Fe(2+) oxidation-dependent degradation."
FT /evidence="ECO:0000269|PubMed:16091046"
FT MUTAGEN 63
FT /note="D->A: Decreases the iron incorporation but is still
FT capable of binding iron to some extent."
FT /evidence="ECO:0000269|PubMed:16091046"
FT MUTAGEN 74
FT /note="D->A: Abolishes the iron incorporation."
FT /evidence="ECO:0000269|PubMed:12501248,
FT ECO:0000269|PubMed:16091046"
FT MUTAGEN 78
FT /note="E->A: Abolishes the iron incorporation."
FT /evidence="ECO:0000269|PubMed:12501248,
FT ECO:0000269|PubMed:16091046"
FT MUTAGEN 78
FT /note="E->D: Decreases the iron incorporation
FT considerably."
FT /evidence="ECO:0000269|PubMed:12501248,
FT ECO:0000269|PubMed:16091046"
FT MUTAGEN 137
FT /note="D->A,F: No major effects."
FT /evidence="ECO:0000269|PubMed:16091046"
FT MUTAGEN 146
FT /note="D->A: No major effects."
FT /evidence="ECO:0000269|PubMed:16091046"
FT MUTAGEN 146
FT /note="D->F: Decreases the iron incorporation
FT considerably."
FT /evidence="ECO:0000269|PubMed:16091046"
FT HELIX 25..49
FT /evidence="ECO:0007829|PDB:2CF7"
FT HELIX 55..82
FT /evidence="ECO:0007829|PDB:2CF7"
FT HELIX 91..97
FT /evidence="ECO:0007829|PDB:2CF7"
FT HELIX 111..139
FT /evidence="ECO:0007829|PDB:2CF7"
FT HELIX 142..165
FT /evidence="ECO:0007829|PDB:2CF7"
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
