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 03-OCT-2012, entry version 78. DE RecName: Full=DNA protection during starvation protein 1; DE EC=1.16.-.-; GN Name=dps1; Synonyms=dlp2; GN OrderedLocusNames=BA_2013, GBAA_2013, BAS1871; OS Bacillus anthracis. OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=1392; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (1.46 RP ANGSTROMS) OF 2-147 IN COMPLEX WITH IRON, AND SUBUNIT. RC STRAIN=9131; RX MEDLINE=21964043; 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 MEDLINE=22608414; 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., RA Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., RA Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., RA Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., RA Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., RA 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 RT closely 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+) CC ions, which prevents hydroxyl radical production by the Fenton CC Fe(2+) ion (By similarity). It is capable of binding and CC sequestering Fe(2+) ion. Does not bind DNA. CC -!- CATALYTIC ACTIVITY: 2 Fe(2+) + H(2)O(2) + 2 H(+) = 2 Fe(3+) + 2 CC H(2)O. CC -!- SUBUNIT: The 12 subunits form a hollow sphere into which the CC mineral iron core of up to 500 Fe(3+) can be deposited (By CC similarity). Homododecamer. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- DOMAIN: 12 di-nuclear ferroxidase centers are located at the CC interfaces between subunits related by 2-fold symmetry axes. CC -!- SIMILARITY: Belongs to the dps family. 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; YP_018660.1; NC_007530.2. 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 ProteinModelPortal; Q8RPQ1; -. DR SMR; Q8RPQ1; 2-147. DR DNASU; 1085881; -. DR EnsemblBacteria; EBBACT00000008888; EBBACP00000008644; EBBACG00000008880. DR EnsemblBacteria; EBBACT00000015192; EBBACP00000014813; EBBACG00000015184. DR EnsemblBacteria; EBBACT00000021663; EBBACP00000021148; EBBACG00000021654. DR GeneID; 1085881; -. DR GeneID; 2819796; -. DR GeneID; 2851330; -. DR GenomeReviews; AE016879_GR; BA_2013. DR GenomeReviews; AE017225_GR; BAS1871. DR GenomeReviews; AE017334_GR; GBAA_2013. DR KEGG; ban:BA_2013; -. DR KEGG; bar:GBAA_2013; -. DR KEGG; bat:BAS1871; -. DR eggNOG; COG0783; -. DR HOGENOM; HOG000273542; -. DR KO; K04047; -. DR OMA; FQTLHLM; -. DR ProtClustDB; CLSK916456; -. DR BioCyc; BANT260799:BAS1871-MONOMER; -. DR BioCyc; BANT261594:GBAA2013-MONOMER; -. DR EvolutionaryTrace; Q8RPQ1; -. 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 GO; GO:0006950; P:response to stress; IEA:InterPro. DR Gene3D; G3DSA:1.20.1260.10; Ferritin_rel; 1. DR InterPro; IPR002177; DPS_DNA-bd. DR InterPro; IPR023188; DPS_DNA-bd_CS. DR InterPro; IPR012347; Ferritin-rel. DR InterPro; IPR009078; Ferritin/RNR-like. DR InterPro; IPR008331; Ferritin_DPS_dom. DR Pfam; PF00210; Ferritin; 1. DR PIRSF; PIRSF005900; Dps; 1. DR PRINTS; PR01346; HELNAPAPROT. DR SUPFAM; SSF47240; Ferritin/RR_like; 1. DR PROSITE; PS00818; DPS_1; 1. DR PROSITE; PS00819; DPS_2; FALSE_NEG. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Iron; Iron storage; KW Metal-binding; Oxidoreductase; Reference proteome. FT CHAIN 1 147 DNA protection during starvation protein FT 1. FT /FTId=PRO_0000253325. FT METAL 29 29 Iron 1; shared with dodecameric partner. FT METAL 56 56 Iron 1. FT METAL 60 60 Iron 1. FT METAL 60 60 Iron 2 (Probable). FT HELIX 4 31 FT HELIX 37 64 FT HELIX 73 79 FT HELIX 91 118 FT HELIX 122 145 SQ SEQUENCE 147 AA; 16649 MW; 2741651884FCCCCD CRC64; MSTKTNVVEV LNKQVANWNV LYVKLHNYHW YVTGPHFFTL HEKFEEFYNE AGTYIDELAE RILALEGKPL ATMKEYLATS SVNEGTSKES AEEMVQTLVN DYSALIQELK EGMEVAGEAG DATSADMLLA IHTTLEQHVW MLSAFLK //