DPS_LISIN
ID DPS_LISIN Reviewed; 156 AA.
AC P80725; Q9RE06;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=DNA protection during starvation protein;
DE EC=1.16.-.-;
DE AltName: Full=Ferritin-like protein;
DE AltName: Full=Non-heme iron-containing ferritin;
GN Name=dps; Synonyms=flp, fri; OrderedLocusNames=lin0942;
OS Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=272626;
RN [1]
RP PROTEIN SEQUENCE, AND FUNCTION.
RX PubMed=9013563; DOI=10.1074/jbc.272.6.3259;
RA Bozzi M., Mignogna G., Stefanini S., Barra D., Longhi C., Valenti P.,
RA Chiancone E.;
RT "A novel non-heme iron-binding ferritin related to the DNA-binding proteins
RT of the Dps family in Listeria innocua.";
RL J. Biol. Chem. 272:3259-3265(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
RC STRAIN=LS1;
RX PubMed=12383509; DOI=10.1016/s0378-1119(02)00839-9;
RA Polidoro M., De Biase D., Montagnini B., Guarrera L., Cavallo S.,
RA Valenti P., Stefanini S., Chiancone E.;
RT "The expression of the dodecameric ferritin in Listeria spp. is induced by
RT iron limitation and stationary growth phase.";
RL Gene 296:121-128(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-680 / CLIP 11262;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
RN [4]
RP FUNCTION IN DNA PROTECTION, AND IRON INCORPORATION.
RX PubMed=15823015; DOI=10.1021/bi0472705;
RA Su M., Cavallo S., Stefanini S., Chiancone E., Chasteen N.D.;
RT "The so-called Listeria innocua ferritin is a Dps protein. Iron
RT incorporation, detoxification, and DNA protection properties.";
RL Biochemistry 44:5572-5578(2005).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) IN COMPLEX WITH IRON, AND SUBUNIT.
RX PubMed=10625425; DOI=10.1038/71236;
RA Ilari A., Stefanini S., Chiancone E., Tsernoglou D.;
RT "The dodecameric ferritin from Listeria innocua contains a novel
RT intersubunit iron-binding site.";
RL Nat. Struct. Biol. 7:38-43(2000).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.19 ANGSTROMS) OF MUTANTS GLY-31 AND GLY-43, AND
RP MUTAGENESIS OF HIS-31 AND HIS-43.
RX PubMed=15823016; DOI=10.1021/bi050005e;
RA Ilari A., Latella M.C., Ceci P., Ribacchi F., Su M., Giangiacomo L.,
RA Stefanini S., Chasteen N.D., Chiancone E.;
RT "The unusual intersubunit ferroxidase center of Listeria innocua Dps is
RT required for hydrogen peroxide detoxification but not for iron uptake. A
RT study with site-specific mutants.";
RL Biochemistry 44:5579-5587(2005).
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. Does
CC not bind DNA. {ECO:0000269|PubMed:12383509,
CC ECO:0000269|PubMed:15823015, ECO:0000269|PubMed:9013563}.
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 of up to 500 Fe(3+) can be deposited.
CC {ECO:0000269|PubMed:10625425}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- INDUCTION: By iron limitation and stationary growth phase.
CC {ECO:0000269|PubMed:12383509}.
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; AJ244014; CAB65175.2; -; Genomic_DNA.
DR EMBL; AL596167; CAC96173.1; -; Genomic_DNA.
DR PIR; AE1550; AE1550.
DR RefSeq; WP_003761404.1; NC_003212.1.
DR PDB; 1QGH; X-ray; 2.35 A; A/B/C/D/E/F/G/H/I/J/K/L=1-156.
DR PDB; 2BJY; X-ray; 2.60 A; A/B/C/D/E/F/G/H/I/J/K/L=1-156.
DR PDB; 2BK6; X-ray; 2.19 A; A/B/C/D/E/F=1-156.
DR PDB; 2BKC; X-ray; 2.30 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/X/Y=1-156.
DR PDB; 6HUI; X-ray; 3.00 A; A/B/C/D/E/F=1-156.
DR PDB; 6HV1; X-ray; 2.55 A; A/B/C/D/E/F=1-156.
DR PDB; 6HVQ; X-ray; 1.90 A; A/B/C/D/E/F=1-156.
DR PDB; 6HX2; X-ray; 1.60 A; A/B/C/D/E/F=1-156.
DR PDB; 6SEV; X-ray; 2.00 A; A/B/C/D/E/F=7-156.
DR PDBsum; 1QGH; -.
DR PDBsum; 2BJY; -.
DR PDBsum; 2BK6; -.
DR PDBsum; 2BKC; -.
DR PDBsum; 6HUI; -.
DR PDBsum; 6HV1; -.
DR PDBsum; 6HVQ; -.
DR PDBsum; 6HX2; -.
DR PDBsum; 6SEV; -.
DR AlphaFoldDB; P80725; -.
DR SMR; P80725; -.
DR STRING; 272626.lin0942; -.
DR EnsemblBacteria; CAC96173; CAC96173; CAC96173.
DR GeneID; 61169961; -.
DR KEGG; lin:fri; -.
DR eggNOG; COG0783; Bacteria.
DR HOGENOM; CLU_098183_4_0_9; -.
DR OMA; HWMFQAE; -.
DR OrthoDB; 1742631at2; -.
DR BRENDA; 1.16.3.1; 3044.
DR EvolutionaryTrace; P80725; -.
DR Proteomes; UP000002513; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
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 CDD; cd01043; DPS; 1.
DR Gene3D; 1.20.1260.10; -; 1.
DR InterPro; IPR002177; DPS_DNA-bd.
DR InterPro; IPR023188; DPS_DNA-bd_CS.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Iron; Iron storage;
KW Metal-binding; Oxidoreductase.
FT CHAIN 1..156
FT /note="DNA protection during starvation protein"
FT /id="PRO_0000201657"
FT BINDING 31
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:0000269|PubMed:10625425"
FT BINDING 58
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:0000269|PubMed:10625425"
FT BINDING 62
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:0000269|PubMed:10625425"
FT BINDING 62
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:10625425"
FT MUTAGEN 31
FT /note="H->G: Slight decrease in DNA protection and
FT significant decrease in iron affinity. Retains only one
FT third of wild-type DNA protection and loses iron binding
FT ability; when associated with G-43."
FT /evidence="ECO:0000269|PubMed:15823016"
FT MUTAGEN 43
FT /note="H->G: Slight decrease in DNA protection and
FT significant decrease iron affinity. Retains only one third
FT of wild-type DNA protection and loses iron-binding ability;
FT when associated with G-31."
FT /evidence="ECO:0000269|PubMed:15823016"
FT CONFLICT 63
FT /note="R -> L (in Ref. 2)"
FT /evidence="ECO:0000305"
FT HELIX 3..5
FT /evidence="ECO:0007829|PDB:6HX2"
FT HELIX 9..33
FT /evidence="ECO:0007829|PDB:6HX2"
FT HELIX 39..66
FT /evidence="ECO:0007829|PDB:6HX2"
FT HELIX 75..81
FT /evidence="ECO:0007829|PDB:6HX2"
FT HELIX 95..123
FT /evidence="ECO:0007829|PDB:6HX2"
FT HELIX 126..149
FT /evidence="ECO:0007829|PDB:6HX2"
SQ SEQUENCE 156 AA; 18049 MW; 5FC9FFF5EE7FB6F8 CRC64;
MKTINSVDTK EFLNHQVANL NVFTVKIHQI HWYMRGHNFF TLHEKMDDLY SEFGEQMDEV
AERLLAIGGS PFSTLKEFLE NASVEEAPYT KPKTMDQLME DLVGTLELLR DEYKQGIELT
DKEGDDVTND MLIAFKASID KHIWMFKAFL GKAPLE
