ID DPS1_BACAN Reviewed; 147 AA. AC Q8RPQ1; Q6HZV3; Q6KTT5; Q81RM9; DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2002, sequence version 1. DT 25-MAY-2022, entry version 133. DE RecName: Full=DNA protection during starvation protein 1; DE EC=1.16.-.-; GN Name=dps1; Synonyms=dlp2; OrderedLocusNames=BA_2013, GBAA_2013, BAS1871; OS Bacillus anthracis. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=1392; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (1.46 ANGSTROMS) RP OF 2-147 IN COMPLEX WITH IRON, AND SUBUNIT. RC STRAIN=9131; RX PubMed=11836250; DOI=10.1074/jbc.m112378200; RA Papinutto E., Dundon W.G., Pitulis N., Battistutta R., Montecucco C., RA Zanotti G.; RT "Structure of two iron-binding proteins from Bacillus anthracis."; RL J. Biol. Chem. 277:15093-15098(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ames / isolate Porton; RX PubMed=12721629; DOI=10.1038/nature01586; RA Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., RA Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., RA Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., RA Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L., RA DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., RA Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., RA Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., RA Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., RA White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., RA Hanna P.C., Kolstoe A.-B., Fraser C.M.; RT "The genome sequence of Bacillus anthracis Ames and comparison to closely RT related bacteria."; RL Nature 423:81-86(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ames ancestor; RX PubMed=18952800; DOI=10.1128/jb.01347-08; RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D., RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.; RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'."; RL J. Bacteriol. 191:445-446(2009). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Sterne; RA Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., RA Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., RA Richardson P., Rubin E., Tice H.; RT "Complete genome sequence of Bacillus anthracis Sterne."; RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases. 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 Fe(2+) ion (By CC similarity). It is capable of binding and sequestering Fe(2+) ion. Does CC 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: The 12 subunits form a hollow sphere into which the mineral CC iron core of up to 500 Fe(3+) can be deposited (By similarity). CC Homododecamer. {ECO:0000250, ECO:0000269|PubMed:11836250}. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF374269; AAM18636.1; -; Genomic_DNA. DR EMBL; AE016879; AAP25903.1; -; Genomic_DNA. DR EMBL; AE017334; AAT31135.1; -; Genomic_DNA. DR EMBL; AE017225; AAT54186.1; -; Genomic_DNA. DR RefSeq; NP_844417.1; NC_003997.3. DR RefSeq; WP_000105197.1; NZ_WXXJ01000029.1. DR RefSeq; YP_028135.1; NC_005945.1. DR PDB; 1JIG; X-ray; 1.46 A; A/B/C/D=2-147. DR PDBsum; 1JIG; -. DR AlphaFoldDB; Q8RPQ1; -. DR SMR; Q8RPQ1; -. DR STRING; 260799.BAS1871; -. DR DNASU; 1085881; -. DR EnsemblBacteria; AAP25903; AAP25903; BA_2013. DR EnsemblBacteria; AAT31135; AAT31135; GBAA_2013. DR GeneID; 45021934; -. DR KEGG; ban:BA_2013; -. DR KEGG; bar:GBAA_2013; -. DR KEGG; bat:BAS1871; -. DR PATRIC; fig|198094.11.peg.1988; -. DR eggNOG; COG0783; Bacteria. DR HOGENOM; CLU_098183_2_2_9; -. DR OMA; LYLQTHN; -. DR EvolutionaryTrace; Q8RPQ1; -. DR Proteomes; UP000000427; Chromosome. DR Proteomes; UP000000594; 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. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Iron; Iron storage; Metal-binding; Oxidoreductase; KW Reference proteome. FT CHAIN 1..147 FT /note="DNA protection during starvation protein 1" FT /id="PRO_0000253325" FT METAL 29 FT /note="Iron 1; shared with dodecameric partner" FT /evidence="ECO:0000269|PubMed:11836250" FT METAL 56 FT /note="Iron 1" FT /evidence="ECO:0000269|PubMed:11836250" FT METAL 60 FT /note="Iron 1" FT /evidence="ECO:0000269|PubMed:11836250" FT METAL 60 FT /note="Iron 2" FT /evidence="ECO:0000305|PubMed:11836250" FT HELIX 4..31 FT /evidence="ECO:0007829|PDB:1JIG" FT HELIX 37..64 FT /evidence="ECO:0007829|PDB:1JIG" FT HELIX 73..79 FT /evidence="ECO:0007829|PDB:1JIG" FT HELIX 91..118 FT /evidence="ECO:0007829|PDB:1JIG" FT HELIX 122..145 FT /evidence="ECO:0007829|PDB:1JIG" SQ SEQUENCE 147 AA; 16649 MW; 2741651884FCCCCD CRC64; MSTKTNVVEV LNKQVANWNV LYVKLHNYHW YVTGPHFFTL HEKFEEFYNE AGTYIDELAE RILALEGKPL ATMKEYLATS SVNEGTSKES AEEMVQTLVN DYSALIQELK EGMEVAGEAG DATSADMLLA IHTTLEQHVW MLSAFLK //