ID   DPS_AGRFC               Reviewed;         162 AA.
AC   Q8UCK6; Q7CWY8;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=DNA protection during starvation protein;
DE            EC=1.16.-.-;
GN   Name=dps; OrderedLocusNames=Atu2477; ORFNames=AGR_C_4495;
OS   Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens
OS   (strain C58)).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC   Agrobacterium tumefaciens complex.
OX   NCBI_TaxID=176299;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C58 / ATCC 33970;
RX   PubMed=11743193; DOI=10.1126/science.1066804;
RA   Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., Okura V.K.,
RA   Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L., Chen Y.,
RA   Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr., Chapman P.,
RA   Clendenning J., Deatherage G., Gillet W., Grant C., Kutyavin T., Levy R.,
RA   Li M.-J., McClelland E., Palmieri A., Raymond C., Rouse G.,
RA   Saenphimmachak C., Wu Z., Romero P., Gordon D., Zhang S., Yoo H., Tao Y.,
RA   Biddle P., Jung M., Krespan W., Perry M., Gordon-Kamm B., Liao L., Kim S.,
RA   Hendrick C., Zhao Z.-Y., Dolan M., Chumley F., Tingey S.V., Tomb J.-F.,
RA   Gordon M.P., Olson M.V., Nester E.W.;
RT   "The genome of the natural genetic engineer Agrobacterium tumefaciens
RT   C58.";
RL   Science 294:2317-2323(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C58 / ATCC 33970;
RX   PubMed=11743194; DOI=10.1126/science.1066803;
RA   Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B.,
RA   Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K.,
RA   Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C., Allinger M.,
RA   Doughty D., Scott C., Lappas C., Markelz B., Flanagan C., Crowell C.,
RA   Gurson J., Lomo C., Sear C., Strub G., Cielo C., Slater S.;
RT   "Genome sequence of the plant pathogen and biotechnology agent
RT   Agrobacterium tumefaciens C58.";
RL   Science 294:2323-2328(2001).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEX WITH IRON, FUNCTION IN
RP   DNA PROTECTION, AND SUBUNIT.
RC   STRAIN=GV3101;
RX   PubMed=12660233; DOI=10.1074/jbc.m302114200;
RA   Ceci P., Ilari A., Falvo E., Chiancone E.;
RT   "The Dps protein of Agrobacterium tumefaciens does not bind to DNA but
RT   protects it toward oxidative cleavage: X-ray crystal structure, iron
RT   binding, and hydroxyl-radical scavenging properties.";
RL   J. Biol. Chem. 278:20319-20326(2003).
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, which can be released after reduction. It
CC       efficiently inhibits hydroxyl radical production by the Fenton
CC       reaction. Does not bind DNA. {ECO:0000269|PubMed:12660233}.
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:12660233}.
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}.
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DR   EMBL; AE007869; AAK88212.1; -; Genomic_DNA.
DR   PIR; AC2881; AC2881.
DR   PIR; C97657; C97657.
DR   RefSeq; NP_355427.1; NC_003062.2.
DR   RefSeq; WP_006312098.1; NC_003062.2.
DR   PDB; 1O9R; X-ray; 1.45 A; A/B/C/D/E/F=1-162.
DR   PDBsum; 1O9R; -.
DR   AlphaFoldDB; Q8UCK6; -.
DR   SMR; Q8UCK6; -.
DR   STRING; 176299.Atu2477; -.
DR   EnsemblBacteria; AAK88212; AAK88212; Atu2477.
DR   GeneID; 66222674; -.
DR   KEGG; atu:Atu2477; -.
DR   PATRIC; fig|176299.10.peg.2490; -.
DR   eggNOG; COG0783; Bacteria.
DR   HOGENOM; CLU_098183_1_2_5; -.
DR   OMA; DDYSIGR; -.
DR   PhylomeDB; Q8UCK6; -.
DR   BioCyc; AGRO:ATU2477-MON; -.
DR   EvolutionaryTrace; Q8UCK6; -.
DR   Proteomes; UP000000813; Chromosome circular.
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..162
FT                   /note="DNA protection during starvation protein"
FT                   /id="PRO_0000253329"
FT   BINDING         40
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000269|PubMed:12660233"
FT   BINDING         67
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         71
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000269|PubMed:12660233"
FT   HELIX           12..42
FT                   /evidence="ECO:0007829|PDB:1O9R"
FT   HELIX           48..75
FT                   /evidence="ECO:0007829|PDB:1O9R"
FT   HELIX           84..90
FT                   /evidence="ECO:0007829|PDB:1O9R"
FT   HELIX           103..130
FT                   /evidence="ECO:0007829|PDB:1O9R"
FT   HELIX           134..156
FT                   /evidence="ECO:0007829|PDB:1O9R"
SQ   SEQUENCE   162 AA;  17823 MW;  8C34BF85B570ED15 CRC64;
     MKTHKTKNDL PSNAKSTVIG ILNESLASVI DLALVTKQAH WNLKGPQFIA VHELLDTFRT
     QLDNHGDTIA ERVVQLGGTA LGSLQAVSST TKLKAYPTDI YKIHDHLDAL IERYGEVANM
     IRKAIDDSDE AGDPTTADIF TAASRDLDKS LWFLEAHVQE KS