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DNA protection during starvation protein (EC 1.16.-.-) (Ferritin-like protein) (Non-heme iron-containing ferritin)

 DPS_LISIN               Reviewed;         156 AA.
P80725; Q9RE06;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 1.
20-DEC-2017, entry version 126.
RecName: Full=DNA protection during starvation protein;
EC=1.16.-.-;
AltName: Full=Ferritin-like protein;
AltName: Full=Non-heme iron-containing ferritin;
Name=dps; Synonyms=flp, fri; OrderedLocusNames=lin0942;
Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262).
Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
NCBI_TaxID=272626;
[1]
PROTEIN SEQUENCE, AND FUNCTION.
PubMed=9013563; DOI=10.1074/jbc.272.6.3259;
Bozzi M., Mignogna G., Stefanini S., Barra D., Longhi C., Valenti P.,
Chiancone E.;
"A novel non-heme iron-binding ferritin related to the DNA-binding
proteins of the Dps family in Listeria innocua.";
J. Biol. Chem. 272:3259-3265(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
STRAIN=LS1;
PubMed=12383509; DOI=10.1016/S0378-1119(02)00839-9;
Polidoro M., De Biase D., Montagnini B., Guarrera L., Cavallo S.,
Valenti P., Stefanini S., Chiancone E.;
"The expression of the dodecameric ferritin in Listeria spp. is
induced by iron limitation and stationary growth phase.";
Gene 296:121-128(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC BAA-680 / CLIP 11262;
PubMed=11679669; DOI=10.1126/science.1063447;
Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A.,
Baquero F., Berche P., Bloecker H., Brandt P., Chakraborty T.,
Charbit A., Chetouani F., Couve E., de Daruvar A., Dehoux P.,
Domann E., Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O.,
Entian K.-D., Fsihi H., Garcia-del Portillo F., Garrido P.,
Gautier L., Goebel W., Gomez-Lopez N., Hain T., Hauf J., Jackson D.,
Jones L.-M., Kaerst U., Kreft J., Kuhn M., Kunst F., Kurapkat G.,
Madueno E., Maitournam A., Mata Vicente J., Ng E., Nedjari H.,
Nordsiek G., Novella S., de Pablos B., Perez-Diaz J.-C., Purcell R.,
Remmel B., Rose M., Schlueter T., Simoes N., Tierrez A.,
Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
"Comparative genomics of Listeria species.";
Science 294:849-852(2001).
[4]
FUNCTION IN DNA PROTECTION, AND IRON INCORPORATION.
PubMed=15823015; DOI=10.1021/bi0472705;
Su M., Cavallo S., Stefanini S., Chiancone E., Chasteen N.D.;
"The so-called Listeria innocua ferritin is a Dps protein. Iron
incorporation, detoxification, and DNA protection properties.";
Biochemistry 44:5572-5578(2005).
[5]
X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) IN COMPLEX WITH IRON, AND
SUBUNIT.
PubMed=10625425; DOI=10.1038/71236;
Ilari A., Stefanini S., Chiancone E., Tsernoglou D.;
"The dodecameric ferritin from Listeria innocua contains a novel
intersubunit iron-binding site.";
Nat. Struct. Biol. 7:38-43(2000).
[6]
X-RAY CRYSTALLOGRAPHY (2.19 ANGSTROMS) OF MUTANTS GLY-31 AND GLY-43,
AND MUTAGENESIS OF HIS-31 AND HIS-43.
PubMed=15823016; DOI=10.1021/bi050005e;
Ilari A., Latella M.C., Ceci P., Ribacchi F., Su M., Giangiacomo L.,
Stefanini S., Chasteen N.D., Chiancone E.;
"The unusual intersubunit ferroxidase center of Listeria innocua Dps
is required for hydrogen peroxide detoxification but not for iron
uptake. A study with site-specific mutants.";
Biochemistry 44:5579-5587(2005).
-!- FUNCTION: Protects DNA from oxidative damage by sequestering
intracellular Fe(2+) ion and storing it in the form of Fe(3+)
oxyhydroxide mineral. One hydrogen peroxide oxidizes two Fe(2+)
ions, which prevents hydroxyl radical production by the Fenton
reaction. Does not bind DNA. {ECO:0000269|PubMed:12383509,
ECO:0000269|PubMed:15823015, ECO:0000269|PubMed:9013563}.
-!- CATALYTIC ACTIVITY: 2 Fe(2+) + H(2)O(2) + 2 H(+) = 2 Fe(3+) + 2
H(2)O.
-!- SUBUNIT: Homododecamer. The 12 subunits form a hollow sphere into
which the mineral iron core of up to 500 Fe(3+) can be deposited.
{ECO:0000269|PubMed:10625425}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
-!- INDUCTION: By iron limitation and stationary growth phase.
{ECO:0000269|PubMed:12383509}.
-!- DOMAIN: 12 di-nuclear ferroxidase centers are located at the
interfaces between subunits related by 2-fold symmetry axes.
-!- SIMILARITY: Belongs to the Dps family. {ECO:0000305}.
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EMBL; AJ244014; CAB65175.2; -; Genomic_DNA.
EMBL; AL596167; CAC96173.1; -; Genomic_DNA.
PIR; AE1550; AE1550.
RefSeq; WP_003761404.1; NC_003212.1.
PDB; 1QGH; X-ray; 2.35 A; A/B/C/D/E/F/G/H/I/J/K/L=1-156.
PDB; 2BJY; X-ray; 2.60 A; A/B/C/D/E/F/G/H/I/J/K/L=1-156.
PDB; 2BK6; X-ray; 2.19 A; A/B/C/D/E/F=1-156.
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.
PDBsum; 1QGH; -.
PDBsum; 2BJY; -.
PDBsum; 2BK6; -.
PDBsum; 2BKC; -.
ProteinModelPortal; P80725; -.
SMR; P80725; -.
STRING; 272626.lin0942; -.
EnsemblBacteria; CAC96173; CAC96173; CAC96173.
KEGG; lin:fri; -.
eggNOG; ENOG4105HUF; Bacteria.
eggNOG; COG0783; LUCA.
HOGENOM; HOG000273542; -.
KO; K04047; -.
OMA; DDYSIGR; -.
OrthoDB; POG091H00MO; -.
BRENDA; 1.16.3.1; 3044.
EvolutionaryTrace; P80725; -.
Proteomes; UP000002513; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
GO; GO:0016722; F:oxidoreductase activity, oxidizing metal ions; IEA:InterPro.
GO; GO:0006879; P:cellular iron ion homeostasis; IEA:UniProtKB-KW.
GO; GO:0006950; P:response to stress; IEA:InterPro.
CDD; cd01043; DPS; 1.
Gene3D; 1.20.1260.10; -; 1.
InterPro; IPR002177; DPS_DNA-bd.
InterPro; IPR023188; DPS_DNA-bd_CS.
InterPro; IPR012347; Ferritin-like.
InterPro; IPR009078; Ferritin-like_SF.
InterPro; IPR008331; Ferritin_DPS_dom.
PANTHER; PTHR42932; PTHR42932; 1.
Pfam; PF00210; Ferritin; 1.
PIRSF; PIRSF005900; Dps; 1.
PRINTS; PR01346; HELNAPAPROT.
SUPFAM; SSF47240; SSF47240; 1.
PROSITE; PS00818; DPS_1; 1.
PROSITE; PS00819; DPS_2; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing;
Iron; Iron storage; Metal-binding; Oxidoreductase.
CHAIN 1 156 DNA protection during starvation protein.
/FTId=PRO_0000201657.
METAL 31 31 Iron 1; shared with dodecameric partner.
{ECO:0000269|PubMed:10625425}.
METAL 58 58 Iron 1. {ECO:0000269|PubMed:10625425}.
METAL 62 62 Iron 1. {ECO:0000269|PubMed:10625425}.
METAL 62 62 Iron 2. {ECO:0000305|PubMed:10625425}.
MUTAGEN 31 31 H->G: Slight decrease in DNA protection
and significant decrease in iron
affinity. Retains only one third of wild-
type DNA protection and loses iron
binding ability; when associated with G-
43. {ECO:0000269|PubMed:15823016}.
MUTAGEN 43 43 H->G: Slight decrease in DNA protection
and significant decrease iron affinity.
Retains only one third of wild-type DNA
protection and loses iron-binding
ability; when associated with G-31.
{ECO:0000269|PubMed:15823016}.
CONFLICT 63 63 R -> L (in Ref. 2). {ECO:0000305}.
HELIX 9 33 {ECO:0000244|PDB:2BK6}.
HELIX 39 66 {ECO:0000244|PDB:2BK6}.
HELIX 75 81 {ECO:0000244|PDB:2BK6}.
HELIX 95 123 {ECO:0000244|PDB:2BK6}.
HELIX 126 149 {ECO:0000244|PDB:2BK6}.
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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