(data stored in ACNUC9435 zone)

SWISSPROT: 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   11-DEC-2019, entry version 136.
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}.
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   PDBsum; 1QGH; -.
DR   PDBsum; 2BJY; -.
DR   PDBsum; 2BK6; -.
DR   PDBsum; 2BKC; -.
DR   PDBsum; 6HUI; -.
DR   PDBsum; 6HV1; -.
DR   PDBsum; 6HVQ; -.
DR   PDBsum; 6HX2; -.
DR   SMR; P80725; -.
DR   STRING; 272626.lin0942; -.
DR   EnsemblBacteria; CAC96173; CAC96173; CAC96173.
DR   KEGG; lin:fri; -.
DR   eggNOG; ENOG4105HUF; Bacteria.
DR   eggNOG; COG0783; LUCA.
DR   HOGENOM; HOG000273542; -.
DR   KO; K04047; -.
DR   OMA; DDYSIGR; -.
DR   OrthoDB; 1742631at2; -.
DR   BioCyc; GCF_000195795:LIN_RS04815-MONOMER; -.
DR   BRENDA; 1.16.3.1; 3044.
DR   EvolutionaryTrace; P80725; -.
DR   Proteomes; UP000002513; Chromosome.
DR   GO; GO:0005623; C:cell; IEA:GOC.
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, oxidizing 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;
DR   PRODOM; P80725.
DR   SWISS-2DPAGE; P80725.
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   METAL           31
FT                   /note="Iron 1; shared with dodecameric partner"
FT                   /evidence="ECO:0000269|PubMed:10625425"
FT   METAL           58
FT                   /note="Iron 1"
FT                   /evidence="ECO:0000269|PubMed:10625425"
FT   METAL           62
FT                   /note="Iron 1"
FT                   /evidence="ECO:0000269|PubMed:10625425"
FT   METAL           62
FT                   /note="Iron 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:0000244|PDB:6HX2"
FT   HELIX           9..33
FT                   /evidence="ECO:0000244|PDB:6HX2"
FT   HELIX           39..66
FT                   /evidence="ECO:0000244|PDB:6HX2"
FT   HELIX           75..81
FT                   /evidence="ECO:0000244|PDB:6HX2"
FT   HELIX           95..123
FT                   /evidence="ECO:0000244|PDB:6HX2"
FT   HELIX           126..149
FT                   /evidence="ECO:0000244|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
//

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